eng
Содержание
1.
Трехмерная структура белков
1.1.
Структура нативного состояния
1.2.
Переходные состояния при сворачивании белковой молекулы
1.3.
Структурные детерминанты констант скорости сворачивания
1.4.
Использование имитационных моделей сворачивания белков
2.
Жидкостная хроматография биомолекул
2.1.
Ионно-обменная хроматография
2.2.
Гель-фильтрация
2.3.
Аффинная хроматография
2.4.
Противоточная хроматография и ультрафильтрация
3.
Масс-спектрометрия
3.1.
Принципы действия и типы спектрометров
3.1.1.
Секторный масс-спектрометр
3.1.2.
Квадрупольный масс-спектрометр
3.1.3.
Масс-спектрометр с ионной ловушкой
3.1.4.
Масс-спектрометр с измерением времени пролета
3.1.5.
Масс-спектрометр с Фурье-преобразованием сигнала
3.1.6.
Ионизация, ионный транспорт и детекция ионов
3.1.7.
Фрагментация ионов
3.1.8.
Комбинация с хроматографическими методами
3.2
Биофизические применения
4.
Рентгеноструктурный анализ
4.1.
Преобразование Фурье и рентгеновская кристаллография
4.1.1.
Преобразование Фурье
4.1.2.
Рентгеновская кристаллография белков
4.1.2.1.
Краткий исторический обзор
4.1.2.2.
Получение кристаллов, пригодных для анализа
4.1.2.3.
Получение дифракционной картины
4.1.2.4.
Определение фаз: включение тяжелых атомов
4.1.2.5.
Вычисление электронной плотности и установление структуры
4.1.2.6.
Криокристаллография и кристаллография с временным разрешением
4.2.
Рассеяние рентгеновых лучей
4.2.1.
Малоугловое рассеяние рентгеновых лучей (SAXS)
4.2.2.
Возвратное рассеяние рентгеновых лучей
5.
Инфракрасная спектроскопия белков
5.1.
Спектрометры и приспособления
5.1.1.
Сканирующая инфракрасная спектрометрия
5.1.2.
Инфракрасные спектрометры с Фурье-преобразованием сигнала (FTIR)
5.1.3.
Измерение возвратного рассеяния света (LIDAR), оптическая когерентная томография, ослабленное полное отражение и ИК-микроскопы
5.2.
Применения
6.
Электронная микроскопия
6.1.
Просвечивающий электронный микроскоп (TEM)
6.1.1.
Основная конструкция
6.1.2.
Разрешение
6.1.3.
Источники электронов
6.1.4.
Решетчатые подложки
6.1.5.
Электронные линзы
6.1.6.
Взаимодействие электронов с образцом и электронная спектроскопия
6.1.7.
Примеры биофизических применений
6.2.
Сканирующий просвечивающий электронный микроскоп (STEM)
7.
Сканирующая микроскопия
7.1.
Атомно-силовая микроскопия (AFM)
7.2.
Сканирующий туннельный микроскоп (STM)
7.3.
Сканирующий околополевой оптический микроскоп (SNOM)
7.3.1.
Преодоление пределов классической оптики
7.3.2.
Конструкция апертуры для субдлинноволновой оптики
7.3.3.
Примеры применения
7.4.
Микроскоп со сканированием ионной проводимости, микроскоп теплового сканирования и другие сканирующие микроскопы
8.
Биофизическая нанотехнология
8.1.
Измерение сил в единичной белковой молекуле
8.2.
Измерение сил в единичном комплексе ДНК с ДНК-полимеразой
8.3.
Молекулярное узнавание
8.4.
Белковые наночипы и белковая инженерия
8.5.
Изучение и манипуляции с растущими кристаллами белков
8.6.
Нанопипетки, молекулярные диоды, самоорганизующиеся нанотранзисторы, трансфекция наночастицами и другие биофизические нанотехнологии
9.
Протеомика: высокопроизводительный функциональный анализ белков
9.1.
Обнаружение мишени
9.2.
Протеомика взаимодействий
9.3.
Химическая протеомика
9.4.
Технология “лаборатории в одном чипе” и масс-спектрометрические сканнеры
9.5.
Структурная протеомика
10.
Спектроскопия ионной подвижности
10.1.
Основная конструкция спектрометров
10.2.
Разрешение и чувствительность
10.3.
“Нюхатели” на основе спектрометров ионной подвижности
10.4.
Особенности конструкции
10.5.
Обнаружение биологических агентов
11.
Акустические эффекты микроволн и теоретическая концепция технологии передачи мысли
11.1.
Теоретическая концепция
11.1.1.
Основы концепции технологии передачи мысли
11.1.2.
Описание технологии
11.1.2.1.
Частоты
11.1.2.2.
Источники излучения
11.2.
Примеры возможных применений
11.2.1.
Автоматизированное устройство
11.2.2.
Небольшое ручное устройство
11.2.3.
Биомедицинская микроволновая акустика и передача мысли
12.
Заключение
13.
Литература
14.
Предметный указатель
Список цитируемой литературы
Список цитируемой литературы
Abkevich VI, Gutin AM, Shakhnovich EI (1995) Impact of local and nonlocal interactions on the thermodynamics and kinetics of protein folding. J Mol Biol 252:460-471
Abola EE, Sussman JL, Prilusky J, Manning NO (1997) Protein data bank archives of three-dimensional macromolecular structures. Methods Enzymol 277:556-571
Achari A, Hale SP, Howard AJ, Clore GM, Gronenborn AM, Hardman KD, Whitlow M (1992) 1.67 Е X-ray structure of the B2 immunoglobulin-binding domain of streptococcal protein G and comparison to the NMR structure of the B1 domain. Biochemistry 31:10449-10457
Adam GC, Sorensen EJ, Cravatt BF (2002a) Chemical strategies for functional proteomics. Mol Cell Proteomics 1:781-790
Adam GC, Sorensen EJ, Cravatt BF (2002b) Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype. Nat Biotechnol 20:805-809
Aitio H, Laakso T, Pihlajamaa T, Torkkeli M, Kilpelainen I, Drakenberg T, Serimaa R, Annila A (2001) Characterization of apo and partially saturated states of calerythrin, an EF-hand protein from S. erythraea: a molten globule when deprived of Ca2+. Protein Sci 10:74-82
Aitken A, Learmonth M (2002) Protein identification by in-gel digestion and mass spectrometric analysis. Mol Biotechnol 20:95-97
Allison DP, Hinterdorfer P, Han W (2002) Biomolecular force measurements and the atomic force microscope. Curr Opin Biotechnol 13:47-51
Alm E, Baker D (1999) Matching theory and experiment in protein folding. Curr Opin Struct Biol 9:189-196
Andersen KV, Poulsen FM (1992) Three-dimensional structure in solution of acyl-coenzyme A binding protein from bovine liver. J Mol Biol 226:1131-1141
Anderson RJ, Bendell DJ, Garnett I, Groundwater PW, Lough WJ, Mills MJ, Savery D, Shattock PE (2002) Identification of indolyl-3-acryloylglycine in the urine of people with autism. J Pharm Pharmacol 54:295-298
Andolfi L, Cannistraro S, Canters GW, Facci P, Ficca AG, van Amsterdam IM, Verbeet MP (2002) A poplar plastocyanin mutant suitable for adsorption onto gold surface via disulfide bridge. Arch Biochem Biophys 399:81-88
Andretzky P, Lindner MW, Herrmann JM, Schultz A, Konzog M, Kiesewetter F, Hдusler G (1998) Optical coherence tomography by "Spectral radar". SPIE 3567:78-87
Еqvist J (1999) Long-range electrostatic effects on peptide folding. FEBS Lett 457:414-418
Arai S, Hirai M (1999) Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small angle X-ray scattering. Biophys J 76:2192-2197
Aries RE, Gutteridge CS, Ottley TW (1986) Evaluation of a low-cost, automated pyrolysis mass spectrometer. J Anal Appl Pyrol 9:81-98
Armitage S, Saywell S, Roux C, Lennard C, Greenwood P (2001) The analysis of forensic samples using laser micro-pyrolysis gas chromatography mass spectrometry. J Forensic Sci 46:1043-1052
Asbury GR, Hill HH (2000) Separation of amino acids by ion mobility spectrometry. J Chromatogr A 902:433-437
Ash EA, Nicholls G (1972) Super-resolution aperture scanning microscope. Nature 237:510-513
Astley OM, Donald AM (2001) A small angle X-ray scattering study of the effect of hydration on the microstructure of flax fibers. Biomacromolecules 2:672-680
Avseenko NV, Morozova TY, Ataullakhanov FI, Morozov VN (2001) Immobilization of proteins in immunochemical microarrays fabricated by electrospray deposition. Anal Chem 73:6047-6052
Avseenko NV, Morozova TY, Ataullakhanov FI, Morozov VN (2002) Immunoassay with multicomponent protein microarrays fabricated by electrospray deposition. Anal Chem 74:927-933
Backmann J, Schдfer G, Wyns L, Bцnisch H (1998) Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius. J Mol Biol 284:817-833
Bada M, Walther D, Arcangioli B, Doniach S, Delarue M (2000) Solution structural studies and low-resolution model of the Schizosaccharomyces pombe sap1 protein. J Mol Biol 300:563-574
Bai YW (1999) Equilibrium amide hydrogen exchange and protein folding kinetics. J Biomol NMR 15:65-70
Bai YW (2000) Kinetic evidence of an on-pathway intermediate in the folding of lysozyme. Protein Sci 9:194-196
Bailey JA, Tomson FL, Mecklenburg SL, MacDonald GM, Katsonouri A, Puustinen A, Gennis RB, Woodruff WH, Dyer RB (2002) Time-resolved step-scan Fourier transform infrared spectroscopy of the CO adducts of bovine cytochrome c oxidase and of cytochrome bo3 from Escherichia coli. Biochemistry 41:2675-2683
Baim MA, Eatherton RL, Hill HH (1983) Ion mobility detector for gas chromatography with a direct photoionization source. Anal Chem 55:1761-1766
Baker D (2000) A surprising simplicity to protein folding. Nature 405:39-42
Baker D, DeGrado WF (1999) Engineering and design - editorial overview. Curr Opin Struct Biol 9:485-486
Barrera FN, Garzon MT, Gomez J, Neira JL (2002) Equilibrium unfolding of the C-terminal SAM domain of p73. Biochemistry 41:5743-5753
Barshick SA, Wolf DA, Vass AA (1999) Differentiation of microorganisms based on pyrolysis ion trap mass spectrometry using chemical ionization. Anal Chem 71:633-641
Barth A (2002) Selective monitoring of 3 out of 50,000 protein vibrations. Biopolymers 67:237-241
Baumbach JI, Eiceman GA (1999) Ion mobility spectrometry: arriving on site and moving beyond a low profile. Appl Spectrosc 53:338A-355A
Baumbach JI, Stach J (ed) (1998) Recent Developments in Ion Mobility Spectrometry. International Society for Ion Mobility Spectrometry, Dortmund, Germany
Beamer LJ, Pabo CO (1992) Refined 1.8 Е crystal structure of the lamda-repressor-DNA complex. J Mol Biol 227:177-196
Beegle LW, Kanik I, Matz L, Hill HH (2001) Electrospray ionization high-resolution ion mobility spectrometry for the detection of organic compounds, 1. Amino acids. Anal Chem 73:3028-3034
Begley P, Corbin R, Foulger BE, Simmonds PG (1991) Photoemissive ionization source for ion mobility detectors. J Chromatogr 588:239-249
Bellotti V, Stoppini M, Mangione P, Sunde M, Robinson C, Asti L, Brancaccio D, Ferri G (1998) beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrills. Eur J Biochem 258:61-67
Benoit M, Gabriel D, Gerisch G, Gaub HE (2000) Discrete interactions in cell adhesion measured by single-molecule force spectroscopy. Nature Cell Biol 2:313-317
Berkeley RCW, Goodacre R, Helyer RJ, Kelley T (1990) Pyrolysis-MS in the identification of micro-organisms. Lab Pract 39:81-83
Berks BC, Sargent F, Palmer T (2000) The Tat protein export pathway. Mol Microbiol 35:260-274
Bernal JD (1939) The structure of proteins. Nature 143:663-667
Bernal JD, Crowfoot D (1934) X-ray photographs of crystalline pepsin. Nature 138:133-134
Betzig E, Harootunian A, Isaacson M, Kratschmer E, Lewis A (1986) Near-field scanning optical microscopy (NSOM): development and biophysical applications. Biophys J 49:269-279
Betzig E, Trautmann JK, Harris TD, Weiner JS, Kostelak RL (1991) Breaking the diffraction barrier: optical microscopy on a nanometric scale. Science 251:1468-1470
Betzig E, Finn PL, Weiner JS (1992) Combined shear force and near-field scanning optical microscopy. Appl Phys Lett 60:2484-2486
Bianco A, Corvaja C, Crisma M, Guldi DM, Maggini M, Sartori E, Toniolo C (2002) A helical peptide receptor for [60]fullerene. Chemistry 8:1544-1553
Binnig G, Rohrer H (1987) Scanning tunneling microscopy - from birth to adolescence. Rev Mod Phys 59, No 3, Part I
Binnig G, Gerber C, Quate CF (1986) Atomic force microscopy. Phys Rev Lett 56:930-933
Binnig G, Rohrer H, Gerber C, Weibel E (1982a) Vacuum tunneling. Physica 109 & 110B 2075-2077
Binnig G, Rohrer H, Gerber C, Weibel E (1982b) Surface studies by scanning tunneling microscopy. Phys Rev Lett 49:57-61
Binnig G, Rohrer H, Gerber C, Weibel E (1983) 7(7 reconstruction on Si(111) resolved in real space. Phys Rev Lett 50:120-123
Bird GM, Keller RA (1976) Vapor concentration dependence of plasmagrams. J Chromatographic Sci 14:574-577
Birolo L, Dal Piaz F, Pucci P, Marino G (2002) Structural characterization of the M* partly folded intermediate of wild-type and P138A aspartate aminotransferase from Escherichia coli. J Biol Chem 277:17428-17437
Biscarini F, Cavallini M, Leigh DA, Leon S, Teat SJ, Wong JK, Zerbetto F (2002) The effect of mechanical interlocking on crystal packing: predictions and testing. J Am Chem Soc 124:225-233
Blanchard WC, Bacon AT (1989) Ion mobility spectrometer. US Patent 4,797,554
Blomberg A (2002) Use of two-dimensional gels in yeast proteomics. Methods Enzymol 350:559-584
Boettner M, Prinz B, Holz C, Stahl U, Lang C (2002) High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris. J Biotechnol 99:51-62
Boisvert DC, Wang J, Otwinowski Z, Horwich AL, Sigler PB (1996) The 2.4 Е crystal Structure of the bacterial chaperonin GroEL complexed with ATP gamma S Nature Struct Biol 3:170-177
Bork P (2002) Comparative analysis of protein interaction networks. Bioinformatics 18 Suppl 2:S64
Borsdorf H, Rudolph M (2001) Gas-phase ion mobility studies of constitutional isomeric hydrocarbons using different ionization techniques. Int J Mass Spectrom 208:67-72
Borsdorf H, Schelhorn H, Flachowsky J, Dцring HR, Stach J (2000) Corona discharge ion mobility spectrometry of aliphatic and aromatic hydrocarbons. Anal Chim Acta 403:235-242
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 Е. Nature 371:578-586
Brask J, Jensen KJ (2000) Carbopeptides: chemoselective ligation of peptide aldehydes to an aminooxy-functionalized D-galactose template. J Pept Sci 6:290-299
Brown DR, Wong BS, Haifiz F, Clive C, Haswell SJ, Jones IM (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem J 344:1-5
Brown DR, Hafiz F, Glasssmith LL, Wong BS, Jones IM, Clive C, Haswell SJ (2000) Consequences of manganese replacement of copper for prion protein function and proteinase resistance. EMBO J 19:1180-1186
Bruckbauer A, Ying L, Rothery AM, Korchev YE, Klenerman D (2002a) Characterization of a novel light source for simultaneous optical and scanning ion conductance microscopy. Anal Chem 74:2612-2616
Bruckbauer A, Ying L, Rothery AM, Zhou D, Shevchuk AI, Abell C, Korchev YE, Klenerman D (2002b) Writing with DNA and protein using a nanopipet for controlled delivery. J Am Chem Soc 124:8810-8811
Brunkan WB (1989) Hearing system. US Patent 4,877,027
Bryden WA (1995) Tiny-TOF-MALDI mass spectrometry for particulate drug and explosives detection. 3rd Symposium on Research & Development, Kossiakoff Center, The Johns Hopkins University
Budovich VL, Mikhailov AA, Arnold G (1999) Ion mobility spectrometer. US Patent 5,969,349
Burbaum J, Tobal GM (2002) Proteomics in drug discovery. Curr Opin Chem Biol 6:427-433
Burke JR (1992) Ion mobility detector. US Patent 5,162,649
Burton RE, Huang GS, Daugherty MA, Fullbright PW, Oas TG (1996) Microsecond protein folding through a compact transition state. J Mol Biol 263:311-322
Burton RE, Huang GS, Daugherty MA, Calderone TL, Oas TG (1997) The energy landscape of a fast-folding protein mapped by Ala(r)Gly substitutions. Nature Struct Biol 4:305-310
Bustamante C, Smith SB, Liphardt J, Smith D (2000) Single-molecule studies of DNA mechanics. Curr Opin Struct Biol 10:279-285
Butler BC, Hanchett RH, Rafailov H, MacDonald G (2002) Investigating structural changes induced by nucleotide binding to RecA using difference FTIR. Biophys J 82:2198-2210
Calvo EJ, Danilowicz C, Wolosiuk A (2002) Molecular "wiring" enzymes in organized nanostructures. J Am Chem Soc 124:2452-2453
Campbell DN, Spangler GE, Davis RC Jr, Fafaul EF, Carrico JP Jr (1991) All ceramic ion mobility spectrometer cell. US Patent 5,021,654
Canady MA, Tsuruta H, Johnson JE (2001) Analysis of rapid, large-scale protein quaternary structural changes: time-resolved X-ray solution scattering of Nudaurelia capensis Omega virus (NOmegaV) maturation. J Mol Biol 311:803-814
Canet D, Last AM, Tito P, Sunde M, Spencer A, Archer DB, Redfield C, Robinson CV, Dobson CM (2002) Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme. Nature Struct Biol 9:308-315
Carnahan BL, Tarassov AS (1995) Ion mobility spectrometer. US Patent 5,420,424
Carnahan BL, Tarassov AS (1998) Recirculating filtration system for use with a transportable ion mobility spectrometer. US Patent 5,723,861
Caroll DI (1972) Apparatus and methods for separating, detecting, and measuring trace gases. US Patent 3,668,383
Caroll DI, Cohen MJ, Wernlund RF (1971) Apparatus and methods for separating, detecting, and measuring trace gases with enhanced resolution. US Patent 3,626,180
Carrion-Vazquez M, Oberhauser AF, Fowler SB, Marszalek PE, Broedel SE, Clarke J, Fernandez JM (1999) Mechanical and chemical unfolding of a single protein: a comparison. Proc Natl Acad Sci USA 96:3694-3699
Casari G, Sippl MJ (1992) Structure-derived hydrophobic potential - hydrophobic potential derived from X-ray structures of globular proteins is able to identify native folds. J Mol Biol 224:725-732
Castellanos IJ, Cruz G, Crespo R, Griebenow K (2002) Encapsulation-induced aggregation and loss in activity of gamma-chymotrypsin and their prevention. J Control Release 81:307-319
Celis JE, Celis P, Palsdottir H, Ostergaard M, Gromov P, Primdahl H, Orntoft TF, Wolf H, Celis A, Gromova I (2002) Proteomic strategies to reveal tumor heterogeneity among urothelial papillomas. Mol Cell Proteomics 1:269-279
Chacon P, Moran F, Diaz JF, Pantos E, Andreu JM (1998) Low-resolution structures of proteins in solution retrieved from X-ray scattering with a genetic algorithm. Biophys J 74:2760-2775
Chambert R, Petit-Glatron MF (1999) Anionic polymers of Bacillus subtilis cell wall modulate the folding rate of secreted proteins. FEMS Microbiol. Lett 179:43-47
Chan HS (1998) Protein folding: matching speed and locality. Nature 392:761-763
Chan HS (1999) Folding alphabets. Nature Struct Biol 6:994-996
Chan HS (2000) Modeling protein density of states: additive hydrophobic effects are insufficient for calorimetric two-state cooperativity. Proteins 40:543-571
Chang AM, Hallen HD, Harriott L, Hess HF, Kao HL, Kwo J, Miller RE, Wolfe R, van der Ziel J, Chang TY (1992a) Scanning Hall probe microscopy. Appl Phys Lett 61:1974-1976
Chang AM, Hallen HD, Hess HF, Kao HL, Kwo J, Sudbш A, Chang TY (1992b) Scanning Hall probe microscopy of a vortex and field fluctuations in La1.85Sr0.15CO4 films. Europhys Lett 20:645-650
Chang JY, Li L, Bulychev A (2000a) The underlying mechanism for the diversity of disulfide folding pathways. J Biol Chem 275:8287-8289
Chang JY, Li L, Canals F, Aviles FX (2000b) The unfolding pathway and conformational stability of potato carboxypeptidase inhibitor. J Biol Chem 275:14205-14211
Charras GT, Horton MA (2002) Single cell mechanotransduction and its modulation analyzed by atomic force microscope indentation. Biophys J 82:2970-2981
Chen SJ, Dill KA (2000) RNA folding energy landscapes. Proc Natl Acad Sci USA 97:646-651
Chen L, Wildegger G, Kiefhaber T, Hodgson KO, Doniach S (1998) Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering. J Mol Biol 276:225-237
Chen J, Chen Y, Gong P, Jiang Y, Li YM, Zhao YF (2002a) Novel phosphoryl derivatization method for peptide sequencing by electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom 16:531-536
Chen L, Haushalter KA, Lieber CM, Verdine GL (2002b) Direct visualization of a DNA glycosylase searching for damage. Chem Biol 9:345-350
Cheng J, Wu L, Heller MJ, Sheldon E, Diver J, O'Connell JP, Smolko D, Jalali S, Willoughby D (2002) Integrated portable biological detection system. US Patent 6,403,367
Cherny DI, Jovin TM (2001) Electron and scanning force microscopy studies of alterations in supercoiled DNA tertiary structure. J Mol Biol 313:295-307
Cho SJ, Quinn AS, Stromer MH, Dash S, Cho J, Taatjes DJ, Jena BP (2002) Structure and dynamics of the fusion pore in live cells. Cell Biol Int 26:35-42
Choy WY, Mulder FA, Crowhurst KA, Muhandiram DR, Millett IS, Doniach S, Forman-Kay JD, Kay LE (2002) Distribution of molecular size within an unfolded state ensemble using small angle X-ray scattering and pulse field gradient NMR techniques. J Mol Biol 316:101-112
Christendat D, Yee A, Dharamsi A, Kluger Y, Gerstein M, Arrowsmith CH, Edwards AM (2000) Structural proteomics: prospects for high throughput sample preparation. Prog Biophys Mol Biol 73:3393-45
Clementi C, Jennings PA, Onuchic JN (2000a) How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta. Proc Natl Acad Sci USA 97:5871-5876
Clementi C, Nymeyer H, Onuchic JN (2000b) Topological and energetic factors: what determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins. J Mol Biol 298:937-953
Cobon GS, Verrills N, Papakostopoulos P, Eastwood H, Linnane AW (2002) The proteomics of aging. Biogerontology 3:133-136
Cohen MJ, Karasek FW (1970) Plasma chromatography - a new dimension for gas chromatography and mass spectrometry. J Chromatographic Sci 8:330-337
Cohen MJ, Crowe RW (1973) Apparatus and methods for detecting, separating, concentrating and measuring electronegative trace vapors. US Patent 3,742,213
Cohen MJ, Carroll DI, Wernlund RF, Kilpatrick WD (1972) Apparatus and methods for separating, concentrating, detecting, and measuring trace gases. US Patent 3,699,333
Coimbra MA, Goncalves F, Barros AS, Delgadillo I (2002) Fourier transform infrared spectroscopy and chemometric analysis of white wine polysaccharide extracts. J Agric Food Chem 50:3405-3411
Coligan JE, Dunn BM, Ploegh HL, Speicher DW, Wingfield PT (ed) (1996) Current protocols in protein science. Wiley & Sons, New York
Costantino HR, Griebenow K, Mishra P, Langer R, Klibanov AM (1995) Fourier transform infrared spectroscopic investigation of protein stability in the lyophilized form. Biochim Biophys Acta 1253:69-74
Crawford OH (1999) A fast, stochastic threading algorithm for proteins. Bioinformatics 15:66-71
Csermely P (1999) Chaperone-percolator model: a possible molecular mechanism of Anfinsen-cage-type chaperones. BioEssays 21:959-965
Cui XD, Primak A, Zarate X, Tomfohr J, Sankey OF, Moore AL, Moore TA, Gust D, Harris G, Lindsay SM (2001) Reproducible measurement of single-molecule conductivity. Science 294:571-574
Czaplewski C, Rodziewicz-Motowidlo S, Liwo A, Ripoll DR, Wawak RJ, Scheraga HA (2000) Molecular simulation study of cooperativity in hydrophobic association. Protein Sci 9:1235-1245
D'Alessio G (1999a) Evolution of oligomeric proteins - the unusual case of a dimeric ribonuclease. Eur J Biochem 266:699-708
D'Alesso G (1999b) The evolutionary transition from monomeric to oligomeric proteins: tools, the environment, hypotheses. Progress Biophys Mol Biol 72:271-298
Dammer U, Popescu O, Wagner P, Anselmetti D, Gьntherodt HJ, Misevic GN (1995) Binding strength between cell adhesion proteoglycans measured by atomic force microscopy. Science 267:1173-1175
Dammer U, Hegner M, Anselmetti D, Wagner P, Dreier M, Huber W, Gьntherodt HJ (1996) Specific antigen/antibody interactions measured by force microscopy. Biophys J 70:2437-2441
Davda J, Labhasetwar V (2002) Characterization of nanoparticle uptake by endothelial cells. Int J Pharm 233:51-59
Davies DK (1994) Pulsed ionization ion mobility sensor. US Patent 5,300,773
Dawson RMC, Elliott DC, Elliott WH, Jones KM (1969) Data for biochemical research. Oxford University Press, 2nd Ed,
de Cock H, Brandenburg K, Wiese A, Holst O, Seydel U (1999) Non-lamellar structure and negative charges of lipopolysaccarides required for efficient folding of outer membrane protein PhoE of Escherichia coli. J Biol Chem 274:5114-5119
Demers LM, Ginger DS, Park SJ, Li Z, Chung SW, Mirkin CA (2002) Direct patterning of modified oligonucleotides on metals and insulators by dip-pen nanolithography. Science 296:1836-1838
Dempsey BR, Economou A, Dunn SD, Shilton BH (2002) The ATPase domain of SecA can form a tetramer in solution. J Mol Biol 315:831-843
de Paris R, Strunz T, Oroszlan K, Gьntherodt HJ, Hegner M (2000) Force spectroscopy and dynamics of the biotin-avidin bond studied by scanning force microscopy. Single Mol 1:285-290
Desmeules P, Grandbois M, Bondarenko VA, Yamazaki A, Salesse C (2002) Measurement of membrane binding between recoverin, a calcium-myristoyl switch protein, and lipid bilayers by AFM-based force spectroscopy. Biophys J 82:3343-3350
Dierksen K, Typke D, Hegerl R, Koster AJ, Baumeister W (1992) Towards automatic electron tomography. Ultramicroscopy 40:71-87
Dill KA, Fiebig KM, Chan HS (1993) Cooperativity in protein folding kinetics. Proc Natl Acad Sci USA 90:1942-1946
Ding FX, Schreiber D, VerBerkmoes NC, Becker JM, Naider F (2002) The chain length dependence of helix formation of the second transmembrane domain of a G protein-coupled receptor of Saccharomyces cerevisiae. J Biol Chem 277:14483-14492
Djuricic D, Hill HA, Lo KK, Wong LL (2002) A scanning tunneling microscopy (STM) investigation of complex formation between cytochrome P450cam and putidaredoxin. J Inorg Biochem 88:362-367
Dong A, Malecki JM, Lee L, Carpenter JF, Lee JC (2002) Ligand-induced conformational and structural dynamics changes in Escherichia coli cyclic AMP receptor protein. Biochemistry 41:6660-6667
Dцring HR, Arnold G, Adler J, Rцbel T, Riemenschneider J (1999) Photo-ionization ion mobility spectrometry. US Patent 5,968,837
Doyle R, Simons K, Qian H, Baker D (1997) Local interactions and the optimization of protein folding. Proteins 29:282-291
Drablos F (1999) Clustering of non-polar contacts in proteins. Bioinformatics 15:501-509
Duarte IF, Barros A, Delgadillo I, Almeida C, Gil AM (2002) Application of FTIR spectroscopy for the quantification of sugars in mango juice as a function of ripening. J Agric Food Chem 50:3104-3111
Duncan MD, Bashkansky M, Reintjes j (1998) Subsurface defect detection in materials using optical coherence tomography. Optics Express 2:540-545
Durbin SD, Carlson WE (1992) Lysozyme crystal growth studied by atomic force microscopy. J Cryst Growth 122:71-79
Durbin SD, Carson WE, Saros MT (1993) In situ studies of protein crystal growth by atomic force microscopy. J Phys D Appl Phys 26:B128-B132
Dwek MV, Rawlings SL (2002) Current perspectives in cancer proteomics. Mol Biotechnol 22:139-152
Dworzanski JP, McClennen WH, Cole PA, Thornton SN, Meuzelaar HLC, Arnold NS, Snyder AP (1997) Field-portable, automated pyrolysis/GC/IMS system for rapid biomarker detection in aerosols: a feasibility study. Field Anal Chem Technol 1:295-305
Dzwolak W, Kato M, Taniguchi Y (2002) Fourier transform infrared spectroscopy in high-pressure studies on proteins. Biochim Biophys Acta 1595:131-144
Edwards AM, Arrowsmith CH, des Pallieres B (2000) Proteomics: New tools for a new era. Modern Drug Discovery 5:35-44
Edwards AM, Kus B, Jansen R, Greenbaum D, Greenblatt J, Gerstein M (2002) Bridging structural biology and genomics: assessing protein interaction data with known complexes. Trends Genet 18:529-536
Efimov AV (1998) A structural tree for protein containing S-like beta-sheets. FEBS Lett 437:246-250
Efimov AV (1999) Complementary packing of alpha-helices in proteins. FEBS Lett 463:3-6
Egawa A, Chiba N, Homma K, Chinone K, Muramatsu H (1999) High-speed scanning by dual feedback control in SNOM/AFM. J Microsc 194:325-328
Egea PF, Rochel N, Birck C, Vachette P, Timmins PA, Moras D (2001) Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR. J Mol Biol 307:557-576
Eiceman GA, Karas Z (1994) Ion Mobility Spectrometry. CRC Press, Boca Raton
Eiceman GA, Ferris MJ, Anderson GK, Danen WC, Tiee JJ (1988) Laser desorption and ionization of solid polycyclic aromatic hydrocarbons in air with analysis by ion mobility spectrometry. Anal Lett 21:539-552
Eiceman GA, Tadjikov B, Krylov E, Nazarov EG, Miller RA, Westbrook J, Funk P (2001) Miniature radio-frequency mobility analyzer as a gas chromatographic detector for oxygen-containing volatile organic compounds, pheromones and other insect attractants. J Chromatogr A 917:205-217
El Khattabi M, Ockhuijsen C, Bitter W, Jaeger KE, Tommassen J (1999) Specifity of the lipase-specific foldases of gram-negative bacteria and the role of the membrane anchor. Mol Gen Genet 261:770-776
Ellis RJ, Hartl FU (1999) Principles of protein folding in the cellular environment. Curr Opin Struct Biol 9:102-110
Eve JK, Patel N, Luk SY, Ebbens SJ, Roberts CJ (2002) A study of single drug particle adhesion interactions using atomic force microscopy. Int J Pharm 238:17-27
Facci P, Alliata D, Cannistraro S (2001) Potential-induced resonant tunneling through a redox metalloprotein investigated by electrochemical scanning probe microscopy. Ultramicroscopy 89:291-298
Fagas G, Cuniberti G, Richter K (2002) Molecular wire-nanotube interfacial effects on electron transport. Ann N Y Acad Sci 960:216-224
Favier AL, Schoehn G, Jaquinod M, Harsi C, Chroboczek J (2002) Structural studies of human enteric adenovirus type 41. Virology 293:75-85
Fermi G, Perutz MF, Shaanan B, Fourme R (1984) The crystal structure of human deoxyheamoglobin at 1.74 Е resolution. J Mol Biol 175:159-174
Fernandez M, Keyrilainen J, Serimaa R, Torkkeli M, Karjalainen-Lindsberg ML, Tenhunen M, Thomlinson W, Urban V, Suortti P (2002) Small angle X-ray scattering studies of human breast tissue samples. Phys Med Biol 47:577-592
Fersht AR (1995a) Characterizing transition states in protein folding - an essential step in the puzzle. Curr Opin Struct Biol 5:79-84
Fersht AR (1995b) Optimization of rates of protein folding - the nucleation-condensation mechanism and its implications. Proc Natl Acad Sci USA 92:10869-10873
Fersht AR, Matouschek A, Serrano L (1992) The folding of an enzyme. 1. Theory of protein engineering analysis of stability and pathway of protein folding. J Mol Biol 224:771-782
Fetler L, Tauc P, Baker DP, Macol CP, Kantrowitz ER, Vachette P (2002) Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase. Protein Sci 11:1074-1081
Fetterolf DD, Clark TD (1993) Detection of trace explosive evidence by ion mobility spectrometry. J Forensic Sci 38:28-39
Feughelman M, Lyman DJ, Willis BK (2002) The parallel helices of the intermediate filaments of alpha-keratin. Int J Biol Macromol 30:95-96
Figeys D (2002a) Proteomics approaches in drug discovery. Anal Chem 74:412A-419A
Figeys D (2002b) Adapting arrays and lab-on-a-chip technology for proteomics. Proteomics 2:373-382
Figeys D (2002c) Functional proteomics: mapping protein-protein interactions and pathways. Curr Opin Mol Ther 4:210-215
Florin EL, Moy VT, Gaub HE (1994) Adhesion forces between individual ligand-receptor pairs. Science 264:415-417
Florin EL, Pralle A, Horber JK, Stelzer EH (1997) Photonic force microscope based on optical tweezers and two-photon excitation for biological applications. J Struct Biol 119:202-211
Forge V, Hoshino M, Kuwata K, Arai M, Kuwajima K, Batt CA, Goto Y (2000) Is folding of beta-lactoglobulin non-hierarchic? Intermediate with native-like beta-sheet and non-native alpha-helix. J Mol Biol 296:1039-1051
Freeman R, Goodfellow M, Gould FK, Hudson SJ, Lightfoot NF (1990) Pyrolysis mass spectrometry (Py-MS) for the rapid epidemiological typing of clinically significant bacterial pathogens. J Med Microbiol 32:283-286
Freeman R, Sisson PR, Heatherington CS (1995) Pyrolysis mass spectrometry. Methods Mol Biol 46:97-105
Freeman R, Sisson PR, Barer MR, Ward AC, Lightfoot NF (1997) A highly discriminatory method for the direct comparison of two closely related bacterial populations by pyrolysis mass spectrometry. Zentralbl Bakteriol 285:285-290
Frey AH (1961) Auditory system response to modulated electromagnetic energy. Aerospace Med 32:1140-1142
Frey AH (1962) Human auditory system response to modulated electromagnetic energy. J Appl Physiol 17:689-692
Frey AH (1993) Electromagnetic field interactions with biological systems. FASEB Journal 7:272-281
Frey AH, Messener R (1973) Human perception of illumination with pulsed UHF electromagnetic energy. Science 181:356-358
Frey AH, Corin E (1979) Holographic assessment of a hypothesized microwave hearing mechanism. Science 206:232-234
Frey TG, Mannella CA (2000) The internal structure of mitrochondria. Trends Biochem Sci 25:319-324
Fringeli UP, Goette J, Reiter G, Siam M, Baurecht D (1998) Structural investigation of oriented membrane assemblies by FTIR-ATR spectroscopy. AIP Conf Proc 430:729-747
Fritz J, Baller MK, Lang HP, Rothuizen H, Vettiger P, Meyer E, Gьntherodt HJ, Gerber C, Gimzewski JK (2000) Translating biomolecular recognition into nanomechanics. Science 288:316-318
Frolow F, Kalb AJ, Yariv J (1994) Structure of a unique, twofold symmetrical haem-binding site. Nature Struct Biol 1:453-460
Furuike S, Ito T, Yamazaki M (2001) Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy. FEBS Lett 498:72-75
Gaietta G, Deerinck TJ, Adams SR, Bouwer J, Tour O, Laird DW, Sosinsky GE, Tsien RY, Ellisman MH (2002) Multicolor and electron microscopic imaging of connexin trafficking. Science 296:503-507
Gaigneaux A, Ruysschaert JM, Goormaghtigh E (2002) Infrared spectroscopy as a tool for discrimination between sensitive and multiresistant K562 cells. Eur J Biochem 269:1968-1973
Gall J (1994) Method and system for altering consciousness. US Patent 5,289,438; and references therein
Gallagher T, Alexander P, Bryan P, Gilliland GL (1994) Two crystal structures of the B1 immunoglobin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33:4721-4729
Gallardo K, Job C, Groot SP, Puype M, Demol H, Vandekerckhove J, Job D (2002) Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds. Plant Physiol 129:823-837
Galzitskaya OV, Surin AK, Nakamura H (2000) Optimal region of average sidechain entropy for fast protein folding. Protein Sci 9:580-586
Gao H, Oberringer M, Englisch A, Hanselmann RG, Hartmann U (2001) The scanning near-field optical microscope as a tool for proteomics. Ultramicroscopy 86:145-150
Garcia P, Serrano L, Durand D, Rico M, Bruix M (2001) NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation. Protein Sci 10:1100-1112
Garcia-Hernandez E, Hernandez-Arana A (1999) Structural basis of lectin-carbohydrate affinities: comparison with protein-folding energetics. Protein Sci 8:1075-1086
Gaub HE, Fernandez JM (1998) The molecular elasticity of individual proteins studied by AFM-related techniques. AvH Magazin 71:11-18
Genick UK, Borgstahl GEO, Ng K, Ren Z, Pradervand C, Burke PM, Srajer V, Teng TY, Schildkamp W, McRee DE, Moffat K, Getzoff ED (1997) Structure of a protein photocycle intermediate by millisecond time-resolved crystallography. Science 275:1471-1475
Gera JF, Hazbun TR, Fields S (2002) Array-based methods for identifying protein-protein and protein-nucleic acid interactions. Methods Enzymol 350:499-512
Ghirlanda G, Lear JD, Ogihara NL, Eisenberg D, DeGrado WF (2002) A hierarchic approach to the design of hexameric helical barrels. J Mol Biol 319:243-253
Giessibl FJ, Hembacher S, Bielefeldt H, Mannhart J (2000) Subatomic features on the Silicon(111)-(7x7) surface observed by atomic force microscopy. Science 289:422-426
Gilardi G, Fantuzzi A, Sadeghi SJ (2001) Engineering and design in the bioelectrochemistry of metalloproteins. Curr Opin Struct Biol 11:491-499
Goebel J, Breit U (2000) Ion mobility spectrometer. US Patent 6,049,076
Goldbeck RA, Thomas YG, Chen E, Esquerra RM, Kliger DS (1999) Multiple pathways on a protein-folding energy landscape: kinetic evidence. Proc Natl Acad Sci USA 96:2782-2787
Goldsbury C, Aebi U, Frey P (2001) Visualizing the growth of Alzheimer's A beta-amyloid-like fibrils. Trends Mol Med 7:582
Goodacre R (1994) Characterisation and quantification of microbial systems using pyrolysis mass spectrometry: introducing neural networks to analytical pyrolysis. Microbiology Europe 2:16-22
Goodacre R, Kell DB (1996) Pyrolysis mass spectrometry and its applications in biotechnology. Curr Opin Biotechnol 7:20-28
Goodacre R, Howell SA, Noble WC, Neal MJ (1996) Sub-species discrimination, using pyrolysis mass spectrometry and self-organising neural networks, of Propionibacterium acnes isolated from normal human skin. Zentralbl Bakteriol 284:501-515
Goodacre R, Rooney PJ, Kell DB (1998a) Discrimination between methicillin-resistant and methicillin-susceptible Staphylococcus aureus using pyrolysis mass spectrometry and artificial neural networks. J Antimicrob Chemother 41:27-34
Goodacre R, Timmins EM, Burton R, Kaderbhai N, Woodward AM, Kell DB, Rooney PJ (1998b) Rapid identification of urinary tract infection bacteria using hyperspectral whole-organism fingerprinting and artificial neural networks. Microbiology 144:1157-1170
Goodacre R, Shann B, Gilbert RJ, Timmins EM, McGovern AC, Alsberg BK, Kell DB, Logan NA (2000) Detection of the dipicolinic acid biomarker in Bacillus spores using Curie point pyrolysis mass spectrometry and Fourier transform infrared spectroscopy. Anal Chem 72:119-127
Goodfellow M, Freeman R, Sisson PR (1997) Curie point pyrolysis mass spectrometry as a tool in clinical microbiology. Zentralbl Bakteriol 285:133-156
Gordon L, Mobley PW, Pilpa R, Sherman MA, Waring AJ (2002) Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using 13C-enhanced Fourier transform infrared spectroscopy. Biochim Biophys Acta 1559:96-120
Goto Y, Aimoto S (1991) Anion and pH-dependent conformational transition of an amphiphilic polypeptide. J Mol Biol 218:387-396
Goto Y, Hoshino M, Kuwata K, Batt CA (1999) Folding of beta-lactoglobulin, a case of the inconsistency of local and non-local interactions. In: Kuwajima K and Arai M (ed) Old and New Views of Protein Folding. Elsevier, Amsterdam, 3-11
Govindarajan S, Goldstein RA (1995) Optimal local propensities for model proteins. Proteins 22:413-418
Grabner B, Landis WJ, Roschger P, Rinnerthaler S, Peterlik H, Klaushofer K, Fratzl P (2001) Age- and genotype-dependence of bone material properties in the osteogenesis imperfecta murine model (oim). Bone 29:453-457
Grandori R, Matecko I, Mьller N (2002) Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry. J Mass Spectrom 37:191-196
Grantcharova VP, Riddle DS, Baker D (2000) Long-range order in the src SH3 folding transition state. Proc Natl Acad Sci USA 97:7084-7089
Grayhack EJ, Phizicky EM (2001) Genomic analysis of biochemical function. Curr Opin Chem Biol 5:34-39
Griffin TJ, Goodlett DR, Aebersold R (2001) Advances in proteome analysis by mass spectrometry. Curr Opin Biotechnol 12:607-612
Grigoriev IV, Rakhmaninova AB, Mironov AA (1998) Simulated annealing for alpha-helical protein folding: searches in vicinity of the "molten globule" state. J Biomol Struct Dyn 16:115-121
Grigoriev IV, Mironov AA, Rakhmaninova AB (1999) Refinement of helix boundaries in alpha-helical globular proteins (in Russian). Mol Biol (Moscow) 33:206-214
Griko YV (2000) Energetic basis of structural stability in the molten globule state of beta-lactalbumin. J Mol Biol 297:1259-1268
Gromiha MM, Selvaraj S (1997) Influence of medium and long range interactions in different structural classes of globular proteins. J Biol Phys 23:151-162
Gromiha MM, Selvaraj S (1999) Importance of long-range interactions in protein folding. Biophys Chem 77:49-68
Gross M (1996) Linguistic analysis of protein folding. FEBS Lett 390:249-252
Gruebele M (1999) The fast protein-folding problem. Annu Rev Phys Chem 50:485-516
Gunning AP, Wilde PJ, Clark DC, Morris VJ, Parker ML, Gunning PA (1996) Atomic force microscopy of interfacial protein films. J Colloid Interface Sci 183:600-602
Gursky O (1999) Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and trimethylamine-N-oxide. Prot Sci 8:2055-2064
Gursky O, Alehkov S (2000) Temperature-dependent beta-sheet formation in beta-amyloid Abeta(1-40) peptide in water: uncoupling beta-structure folding from aggregation. Biochim Biophys Acta 1476:93-102
Gutsche I, Holzinger J, RцЯle M, Heumann H, Baumeister W, May RP (2000a) Conformational rearrangements of an archaeal chaperonin upon ATPase cycling. Curr Biol 10:405-408
Gutsche I, Mihalache O, Hegerl R, Typke D, Baumeister W (2000b) ATPase cycle controls the conformation of an archaeal chaperonin as visulaized by cryo-electron microscopy. FEBS Lett 477:278-282
Haas J, Lehr CM (2002) Developments in the area of bioadhesive drug delivery systems. Expert. Opin Biol Ther 2:287-298
Haider M, Uhlemann S, Schwan E, Rose H, Kabius B, Urban K (1998) Electron microscopy image enhanced. Nature 392:768-769
Hamada D, Kuroda Y, Tanaka T, Goto Y (1995) High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein. J Mol Biol 254:737-746
Hansma PK, Drake B, Marti O, Gould SAC, Prater CB (1989) The scanning ion-conductance microscope. Science Reports 243:641-643
Hardesty B, Tsalkova T, Kramer G (1999) Co-translational folding. Curr Opin Struct Biol 9:111-114
Hдusler G, Lindner MW (1998) "Coherence radar" and "Spectral radar"-New tools for dermatological diagnosis. J Biomed Opt 3:21-31
Heimel J, Fischer UC, Fuchs H (2001) SNOM/STM using a tetrahedral tip and a sensitive current-to-voltage converter. J Microsc 202:53-59
Heinemann U, Frevert J, Hofmann K, Illing G, Maurer C, Oschkinat H, Saenger W (2000) An integrated approach to structural genomics. Prog Biophys Mol Biol 73:347-362
Heinemann U, Illing G, Oschkinat H (2001) High-throughput three-dimensional protein structure determination. Curr Opin Biotechnol 12:348-354
Helyer RJ, Kelley T, Berkeley RC (1997) Pyrolysis mass spectrometry studies on Bacillus anthracis, Bacillus cereus and their close relatives. Zentralbl Bakteriol 285:319-328
Henderson R (1996) Lecture "Resolution limits of microscopes", Laboratory of Molecular Biology, Cambridge
Henderson E, Haydon PG, Sakaguchi DS (1992) Actin filament dynamics in living glial cells imaged by atomic force microscopy. Science 257:1944-1946
Hertadi R, Ikai A (2002) Unfolding mechanics of holo- and apocalmodulin studied by the atomic force microscope. Protein Sci 11:1532-1538
Heyes CD, Wang J, Sanii LS, El-Sayed MA (2002) Fourier transform infrared study of the effect of different cations on bacteriorhodopsin protein thermal stability. Biophys J 82:1598-1606
Hilario J, Kubelka J, Syud FA, Gellman SH, Keiderling TA (2002) Spectroscopic characterization of selected beta-sheet hairpin models. Biopolymers 67:233-236
Hildebrand G, Kunze S, Driver M (2001) Blood cell adhesion on sensor materials studied by light, scanning electron, and atomic-force microscopy. Ann Biomed Eng 29:1100-1105
Hill HH, Siems WF, St Louis RW, McMinn DG (1990) Ion mobility spectrometry. Anal Chem 62:1201-1209
Hodneland CD, Lee YS, Min DH, Mrksich M (2002) Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands. Proc Natl Acad Sci USA 99:5048-5052
Honda S, Kobayashi N, Munekata E, Uedaira H (1999) Fragment reconstitution of a small protein: folding energetics of the reconstituted immunoglobulin binding domain B1 of stretococcal protein G. Biochemistry 38:1203-1213
Honda S, Kobayashi N, Munekata E (2000) Thermodynamics of a beta-hairpin structure: evidence for cooperative formation of folding nucleus. J Mol Biol 295:269-278
Hoover DM, Ludwig ML (1997) A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 Е resolution. Protein Sci 6:2525-2537
Horiuchi Y, Yagi K, Hosokawa T, Yamamoto N, Muramatsu H, Fujihira M (1999) Imaging of various surface properties of fluorescently labelled phospholipid Langmuir-Blodgett films with a combined scanning probe microscope. J Microsc 194:467-471
Hornemann S, Glockshuber R (1998) A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH. Proc Natl Acad Sci USA 95:6010-6014
Howald L, Lьthl R, Meyer E, Gьntherodt HJ (1995) Atomic-force microscopy on the Si(111)-(7x7) surface. Phys Rev B Condens Matter 51:5484-5487
Huang CY, Getahun Z, Zhu Y, Klemke JW, DeGrado WF, Gai F (2002) Helix formation via conformation diffusion search. Proc Natl Acad Sci USA 99:2788-2793
Hubbard MJ (2002) Functional proteomics: The goalposts are moving. Proteomics 2:1069-1078
Hung K, Sun X, Ding H, Kalafatis M, Simioni P, Guo B (2002) A matrix-assisted laser desorption/ionization time-of-flight based method for screening the 1691 G ( A mutation in the factor V gene. Blood Coagul Fibrinolysis 13:117-122
Igartua M, Saulnier P, Heurtault B, Pech B, Proust JE, Pedraz JL, Benoit JP (2002) Development and characterization of solid lipid nanoparticles loaded with magnetite. Int J Pharm 233:149-157
Ikarashi Y, Itoh K, Maruyama Y (1991) Application of FRIT fast atom bombardment liquid chromatography / mass spectrometry for the determination of acetylcholine levels in rat brain regions. Biol Mass Spectrom. 20:21-25
Ikeda S, Morris VJ (2002) Fine-stranded and particulate aggregates of heat-denatured whey proteins visualized by atomic force microscopy. Biomacromolecules 3:382-389
Irbдck A, Peterson C, Potthast F, Sandelin E (1999) Design of sequences with good folding properties in coarse-grained protein models. Structure Fold Des 7:347-360
Ironside JW (1998) Prion diseases in man. J Pathol 186:227-234
Ishizawa F, Misawa S (1990) Capillary column pyrolysis - gas chromatography of hair: a short study in personal identification. J Forensic Sci Soc 30:201-209
Ito Y, Bleloch AL, Brown LM (1998) Nanofabrication of solid-state Fresnel lenses for electron optics. Nature 394:49-52
Ito T, Ota K, Kubota H, Yamaguchi Y, Chiba T, Sakuraba K, Yoshida M (2002) Roles for the two-hybrid system in exploration of the yeast protein interactome. Mol Cell Proteomics 1:561-566
Itoh H, Ogura M, Komatsuda A, Wakui H, Miura AB, Tashima Y (1999) A novel chaperone-activity-reducing mechanism of the 90-kDa molecular chaperone HSP90. Biochem J 343:697-703
Itzhaki LS, Otzen DE, Fersht AR (1995) The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol 254:260-288
Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999) Structure of the E. coli fumarate reductase respiratory complex. Science 284:1961-1966
Jackson SE (1998) How do small single-domain proteins fold? Fold Des 3:R81-R91
Jдger D, Jungblut PR, Mьller-Werdan U (2002) Separation and identification of human heart proteins. J Chromatogr B Analyt Technol Biomed Life Sci 771:131-153
Jain KK (2002) Recent advances in oncoproteomics. Curr Opin Mol Ther 4:203-209
Jeney S, Florin EL, Horber JK (2001) Use of photonic force microscopy to study single-motor-molecule mechanics. Methods Mol Biol 164:91-108
Jйsior JC, Filhol A, Tranqui D (1994) FoldIt (light) - an interactive program for Macintosh computers to analyze and display Protein Data Bank coordinate files. J Appl Cryst 27:1075
Jйsior JC (2000) Hydrophilic frameworks in proteins? J Protein Chem 19:93-103
Jiang M, Nцlting B, Stayton PS, Sligar SG (1996) Surface-linked molecular monolayers of an engineered myoglobin: structure, stability, and function. Langmuier 12:1278-1283
Jiao Y, Cherny DI, Heim G, Jovin TM, Schaffer TE (2001) Dynamic interactions of p53 with DNA in solution by time-lapse atomic force microscopy. J Mol Biol 314:233-243
Jimenez CR, Eyman M, Lavina ZS, Gioio A, Li KW, van der Schors RC, Geraerts WP, Giuditta A, Kaplan BB, van Minnen J (2002) Protein synthesis in synaptosomes: a proteomics analysis. J Neurochem 81:735-744
Kaji N, Ueda M, Baba Y (2001) Direct measurement of conformational changes on DNA molecule intercalating with a fluorescence dye in an electrophoretic buffer solution by means of atomic force microscopy. Electrophoresis 22:3357-3364
Kamatari YO, Ohji S, Konno T, Seki Y, Soda K, Kataoka M, Akasaka K (1999) The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent. Protein Sci 8:873-882
Kandori H, Shimono K, Shichida Y, Kamo N (2002) Interaction of Asn105 with the retinal chromophore during photoisomerization of pharaonis phoborhodopsin. Biochemistry 41:4554-4559
Karasek FW (1970) Plasma chromatograph. Research/Development 21:34-37
Karl M (1994) Ion mobility spectrometer drift chamber. US Patent 5,280,175
Karplus M, Weaver DL (1994) Protein folding dynamics: the diffusion-collision model and experimental data. Protein Sci 3:650-668
Katakuse I, Matsuo T, Matsuda H, Shimonishi Y, Hong YM, Izumi Y (1982) Sequence determination of a peptide with 55 amino acid residues by Edman degradation and field desorption mass spectrometry. Biomed Mass Spectrom 9:64-68
Katou H, Hoshino M, Kamikubo H, Batt CA, Goto Y (2001) Native-like beta-hairpin retained in the cold-denatured state of bovine beta-lactoglobulin. J Mol Biol 310:471-484
Kawata Y, Kawagoe M, Hongo K, Mikuya T, Higurashi T, Mizobata T, Nagai J (1999) Functional communications between the apical and equatorial domains of GroEL through the intermediate domain. Biochemistry 38:15731-15740
Keller RA (1975) Plasma chromatograph, an atmospheric pressure chemical ionization drift-time spectrometer. Am Lab 7:35-44
Keller T, Miki P, Regenscheit P, Dirnhofer R, Schneider A, Tsuchihashi H (1998) Detection of designer drugs in human hair by ion mobility spectrometry. Forensic Sci Int 94:55-63
Kellermayer MS, Smith SB, Bustamante C, Granzier HL (2001) Mechanical fatigue in repetitively stretched single molecules of titin. Biophys J 80:852-863
Kendrew JC, Dickerson RE, Strandberg BE, Hart RJ, Davies DR, Phillips DC, Shore VC (1960) Structure of myoglobin: a three-dimensional Fourier synthesis at 2 Е resolution. Nature 185:422-427
Kenyon RG, Ferguson EV, Ward AC (1997) Application of neural networks to the analysis of pyrolysis mass spectra. Zentralbl Bakteriol 285:267-277
Kersten B, Burkle L, Kuhn EJ, Giavalisco P, Konthur Z, Lueking A, Walter G, Eickhoff H, Schneider U (2002) Large-scale plant proteomics. Plant Mol Biol 48:133-141
Kharakoz DP (1989) Volumetric properties of proteins and their analogs in diluted water solutions. 1. Partial volumes of amino acids at 15-55 oC. Biophys Chem 34:115-125
Kharakoz DP (1991) Volumetric properties of proteins and their analogs in diluted water solutions. 2. Partial adiabatic compressibilities of amino acids at 15-70 oC. J Phys Chem 95:5634-5642
Kharakoz DP (1997) Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry 36:10276-10285
Khomutov GB, Belovolova LV, Gubin SP, Khanin VV, Obydenov AY, Sergeev-Cherenkov AN, Soldatov ES, Trifonov AS (2002) STM study of morphology and electron transport features in cytochrome c and nanocluster molecule monolayers. Bioelectrochemistry 55:177-181
Kienzl E, Jellinger K, Stachelberger H, Linert W (1999) Iron as catalyst for oxidative stress in the pathogenesis of Parkinson's disease? Life Sci 65:1973-1976
Kim Y, Prestegard JH (1990) Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins 8:377-385
Kim JM, Ohtani T, Sugiyama S, Hirose T, Muramatsu H (2001) Simultaneous topographic and fluorescence imaging of single DNA molecules for DNA analysis with a scanning near-field optical/atomic force microscope. Anal Chem 73:5984-5991
Kinney JH, Pople JA, Marshall GW, Marshall SJ (2001) Collagen orientation and crystallite size in human dentin: a small angle X-ray scattering study. Calcif Tissue Int 69:31-37
Kintz P, Cirimele V, Sengler C, Mangin P (1995) Testing human hair and urine for anhydroecgonine methyl ester, a pyrolysis product of cocaine. J Anal Toxicol 19:479-482
Kizil R, Irudayaraj J, Seetharaman K (2002) Characterization of irradiated starches by using FT-Raman and FTIR spectroscopy. J Agric Food Chem 50:3912-3918
Klade CS (2002) Proteomics approaches towards antigen discovery and vaccine development. Curr Opin Mol Ther 4:216-223
Kline AD, Braun W, Wьthrich K (1988) Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry. J Mol Biol 204:675-724
Kneipp J, Beekes M, Lasch P, Naumann D (2002) Molecular changes of preclinical scrapie can be detected by infrared spectroscopy. J Neurosci 22:2989-2997
Koga N, Takada S (2001) Roles of native topology and chain-length scaling in protein folding: a simulation study with a Go-like model. J Mol Biol 313:171-180
Kohno M, Enatsu M, Yoshiizumi M, Kugimiya W (1999) High-level expression of Rhizopus niveus lipase in the yeast Saccharomyces cerevisiae and structural properties of the expressed enzyme. Protein Expr Purif 15:327-335
Kojima M, Tanokura M, Maeda M, Kimura K, Amemiya Y, Kihara H, Takahashi K (2000) pH-dependent unfolding of aspergillopepsin II studied by small angle X-ray scattering. Biochemistry 39:1364-1372
Konan YN, Gurny R, Allemann E (2002) Preparation and characterization of sterile and freeze-dried sub-200 nm nanoparticles. Int J Pharm 233:239-252
Koradi R, Billeter M, Wьthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 14:51-55
Korchev YE, Bashford CL, Milovanovic M, Vodyanoy I, Lab MJ (1997) Scanning ion conductance microscopy of living cells. Biophys J 73:653-658
Korchev YE, Gorelik J, Lab MJ, Sviderskaya EV, Johnston CL, Coombes CR, Vodyanoy I, Edwards CR (2000a) Cell volume measurement using scanning ion conductance microscopy. Biophys J 78:451-457
Korchev YE, Raval M, Lab MJ, Gorelik J, Edwards CR, Rayment T, Klenerman D (2000b) Hybrid scanning ion conductance and scanning near-field optical microscopy for the study of living cells. Biophys J 78:2675-2679
Koshland DE Jr, Hamadani K (2002) Proteomics and models for enzyme cooperativity. J Biol Chem 277:46841-46844
Kцster H (2001a) DNA sequencing by mass spectrometry. US Patent 6,194,144
Kцster H (2001b) DNA sequencing by mass spectrometry. US Patent 6,225,450
Kotiaho T, Lauritsen FR, Degn H, Paakkanen H (1995) Membrane inlet ion mobility spectrometer for on-line measurement of ethanol in beer and in yeast fermentation. Anal Chim Acta 309:317-325
Kramer G, Kudlicki W, McCarthy D, Tsalkova T, Simmons D, Hardesty B (1999) N-terminal and C-terminal modifications affect folding, release from the ribosomes and stability of in vitro synthesed proteins. Int J Biochem Cell Biol 31:231-241
Kraulis PJ (1991) MOLSRCIPT - a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950
Krautbauer R, Pope LH, Schrader TE, Allen S, Gaub H (2002) Discriminating small molecule DNA binding modes by single molecule force spectroscopy. FEBS Lett 510:154-158
Kukar T, Eckenrode S, Gu Y, Lian W, Megginson M, She JX, Wu D (2002) Protein microarrays to detect protein-protein interactions using red and green fluorescent proteins. Anal Biochem 306:50-54
Kuwajima K, Yamaya H, Sugai S (1996) The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J Mol Biol 264:806-822
Kuznetsov YG, Malkin AJ, Lucas RW, McPherson A (2000) Atomic force microscopy studies of icosahedral virus crystal growth. Colloids Surf B Biointerfaces 19:333-346
Lasch P, Pacifico A, Diem M (2002) Spatially resolved IR microspectroscopy of single cells. Biopolymers 67:335-338
Laurell T, Marko-Varga G (2002) Miniaturisation is mandatory unravelling the human proteome. Proteomics 2:345-351
Lawrence AH, Barbour RJ, Sutcliffe R (1991) Identification of wood species by ion mobility spectrometry. Anal Chem 63:1217-1221
Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP (1992) Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. Science 258:987-991
Leasure CS, Fleischer ME, Anderson GK, Eiceman GA (1986) Photoionization in air with ion mobility spectrometry using a hydrogen discharge lamp. Anal Chem 58:2142-2147
Leaves NI, Sisson PR, Freeman R, Jordens JZ (1997) Pyrolysis mass spectrometry in epidemiological and population genetic studies of Haemophilus influenzae. J Med Microbiol 46:204-207
Lee DS, Wu C, Hill HH (1998) Detection of carbohydrates by electrospray ionization / ion mobility spectrometry following microbore high-performance liquid chromatography. J Chromatogr 822:1-9
Lee KA, Craven KB, Niemi GA, Hurley JB (2002a) Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation. Protein Sci 11:862-874
Lee KB, Park SJ, Mirkin CA, Smith JC, Mrksich M (2002b) Protein nanoarrays generated by dip-pen nanolithography. Science 295:1702-1705
Lee SW, Mao CB, Flynn CE, Belcher AM (2002c) Ordering of quantum dots using genetically engineered viruses. Science 296:892-895
Leonhardt JW (1996) New detectors in environmental monitoring using tritium sources. J Radioanlyt Nucl Chem 206:333-339
Leonhardt JW, Rohrbeck W, Bensch H (2001) A high resolution IMS for environmental studies. Supplement to the catalogue for the IMS supplied by the IUT Institute for Environmental Technologies Ltd, Berlin
Li T, Talvenheimo J, Zeni L, Rosenfeld R, Stearns G, Arakawa T (2002) Changes in protein conformation and dynamics upon complex formation of brain-derived neurotrophic factor and its receptor: investigation by isotope-edited Fourier transform IR spectroscopy. Biopolymers 67:10-19
Lim SO, Park SJ, Kim W, Park SG, Kim HJ, Kim YI, Sohn TS, Noh JH, Jung G (2002) Proteome analysis of hepatocellular carcinoma. Biochem Biophys Res Commun 291:1031-1037
Lin JC (1978) Microwave Auditory Effects and Applications. Charles C Thomas, Publisher, Springfield, IL, USA
Lin JC (1989) Electromagnetic Interaction with Biological Systems. Plenum Press, New York
Lin JC (ed) (2000) Advances in Electromagnetic Fields in Living Systems. Vol 3. Kluwer/Plenum, New York
Lin H, Cornish VW (2002) Screening and selection methods for large-scale analysis of protein function. Angew Chem Int Ed Engl 2002 41:4402-4425
Linderoth NA, Simon MN, Russel M (1997) The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science 278:1635-1638
Lindqvist M, Graslund A (2001) An FTIR and CD study of the structural effects of G-tract length and sequence context on DNA conformation in solution. J Mol Biol 314:423-432
Lindsay SM, Thundat T, Nagahara L, Knipping U, Rill RL (1989) Images of DNA double helix in water. Science 244:1063-1064
Liphardt J, Onoa B, Smith SB, Tinoco I Jr, Bustamante C (2001) Reversible unfolding of single RNA molecules by mechanical force. Science 292:733-737
Liu M, Barth A (2002) Mapping nucleotide binding site of calcium ATPase with IR spectroscopy: effects of ATP gamma-phosphate binding. Biopolymers 67:267-270
Liu H, Berger SJ, Chakraborty AB, Plumb RS, Cohen SA (2002) Multidimensional chromatography coupled to electrospray ionization time-of-flight mass spectrometry as an alternative to two-dimensional gels for the identification and analysis of complex mixtures of intact proteins. J Chromatogr B Analyt Technol Biomed Life Sci 782:267-289
Lowery OM (1992) Silent subliminal presentation system. US Patent 5,159,703
Lubman DM, Kronick MN (1982) Plasma chromatography with laser-produced ions. Anal Chem 54:1546-1551
Lubman DM, Kronick MN (1983) Multiwavelength-selective ionization of organic compounds in an ion mobility spectrometer. Anal Chem 55:867-873
MacBeath G (2002) Protein microarrays and proteomics. Nat Genet 32 Suppl 2:526-532
Magee JG, Goodfellow M, Sisson PR, Freeman R, Lightfoot NF (1997) Differentiation of Mycobacterium senegalense from related non-chromogenic mycobacteria using pyrolysis mass spectrometry. Zentralbl Bakteriol 285:278-284
Malins DC, Hellstrom KE, Anderson KM, Johnson PM, Vinson MA (2002) Antioxidant-induced changes in oxidized DNA. Proc Natl Acad Sci USA 99:5937-5941
Malkin AJ, Land TA, Kuznetsov YG, McPherson A, DeYoreo JJ (1995) Investigation of virus crystal growth mechanisms by in situ atomic force microscopy. Phys Rev Lett 75:2778-2781
Malkin AJ, Plomp M, McPherson A (2002) Application of atomic force microscopy to studies of surface processes in virus crystallization and structural biology. Acta Crystallogr D Biol Crystallogr 58:1617-1621
Man WJ, White IR, Bryant D, Bugelski P, Camilleri P, Cutler P, Heald G, Lord PG, Wood J, Kramer K (2002) Protein expression analysis of drug-mediated hepatotoxicity in the Sprague-Dawley rat. Proteomics 2:1577-1585
Maret W, Heffron G, Hill HA, Djuricic D, Jiang LJ, Vallee BL (2002) The ATP/metallothionein interaction: NMR and STM. Biochemistry 41:1689-1694
Marple VA, Chein CM (1980) Virtual impactors: a theroretical study. Environmental Sci Technol 14:976-985
Marple VA, Olson BA, Miller NC (1998) The role of inertial particle collectors in evaluating pharmaceutical aerosol delivery systems. J Aerosol Med 11 Suppl 1:S139-S153
Martin SJ, Butler MA, Frye GC, Schubert WK (1998) Ion mobility spectrometer using frequency-domain separation. US Patent 5,789,745
Martzen MR, McCraith SM, Spinelli SL, Torres FM, Fields S, Grayhack EJ, Phizicky EM (1999) A biochemical genomics approach for identifying genes by the activity of their products. Science 286:1153-1155
Maruyama T, Nakajima M, Ichikawa S, Sano Y, Nabetani H, Furusaki S, Seki M (2001) Small angle X-ray scattering analysis of stearic acid modified lipase. Biosci Biotechnol Biochem 65:1003-1006
Mathur AB, Collinsworth AM, Reichert WM, Kraus WE, Truskey GA (2001) Endothelial, cardiac muscle and skeletal muscle exhibit different viscous and elastic properties as determined by atomic force microscopy. J Biomech 34:1545-1553
Matsko N, Klinov D, Manykin A, Demin V, Klimenko S (2001) Atomic force microscopy analysis of bacteriophages PhiKZ and T4. J Electron Microsc (Tokyo) 50:417-422
Matsuda H (1976) Double focusing mass spectrometers of second order. Atomic Masses and Fundamental Constants 5:185-191
Matsuda H (1981) Mass spectrometers of high transmission and high resolving power. Nucl Instr Meth 187:127-136
Matsuda H, Naito M, Takeuchi M (1974) Advanced virtual image double focussing mass spectrometer. Adv Mass Spectrom 6:407-412
Matz G, Schrцder W (1996) Fast GC/MS field screening for excavation and bioredmediation of contaminated soil. Field Anal Chem Technol 1:77-85
Matz G, Schrцder W (1997) Fast detection of wood preservatives on waste wood with GC/MS, GC/ECD and ion mobility spectrometry. Conference "Field analytical methods for hazardous wastes and toxic chemicals", Las Vegas
Matz LM, Hill HH (2001) Evaluation of opiate separation by high-resolution electrospray ionization-ion mobility spectrometry / mass spectrometry. Anal Chem 73:1664-1669
Mayor U, Johnson CM, Daggett V, Fersht AR (2000) Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc Natl Acad Sci USA 97:13518-13522
McCraith S, Holtzman T, Moss B, Fields S (2000) Genome-wide analysis of vaccinia virus protein-protein interactions. Proc Natl Acad Sci USA 97:4879-4884
McPherson A, Malkin AJ, Kuznetsov YG (2000) Atomic force microscopy in the study of macromolecular crystal growth. Annu Rev Biophys Biomol Struct 29:361-410
McPherson A, Malkin AJ, Kuznetsov YG, Plomp M (2001) Atomic force microscopy applications in macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 57:1053-1060
Megerle CA, Cohn DB (2000) Ion mobility sensors and spectrometers having a corona discharge ionization source. US Patent 6,100,698
Meixner AJ, Kneppe H (1998) Scanning near-field optical microscopy in cell biology and microbiology. Cell Mol Biol 44:673-688
Meland BC (1980) Apparatus for electrophysiological stimulation. US Patent 4,227,516
Merkel R, Nassoy P, Leung A, Ritchie K, Evans E (1999) Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397:50-53
Mezzetti A, Nabedryk E, Breton J, Okamura MY, Paddock ML, Giacometti G, Leibl W (2002) Rapid-scan Fourier transform infrared spectroscopy shows coupling of Glu-L212 protonation and electron transfer to Q(B) in Rhodobacter sphaeroides reaction centers. Biochim Biophys Acta 1553:320-330
Michener CM, Ardekani AM, Petricoin EF 3rd, Liotta LA, Kohn EC (2002) Genomics and proteomics: application of novel technology to early detection and prevention of cancer. Cancer Detect Prev 26:249-255
Miki A, Keller T, Regenscheit P, Dirnhofer R, Tatsuno M, Katagi M, Nishikawa M, Tsuchihashi H (1997) Application of ion mobility spectrometry to the rapid screening of methamphetamine incorporated in hair. J Chromatogr B 692:319-328
Miki A, Tatsuno M, Katagie M, Nishikawa M, Tsuchihashi H (1998) Analysis of illicit drugs by ion mobility spectrometry. J Toxicol - Toxin Rev 17:93-93
Miller LD, Putthanarat S, Eby RK, Adams WW (1999) Investigation of the nanofibrillar morphology in silk fibers by small angle X-ray scattering and atomic force microscopy. Int J Biol Macromol 24:159-165
Mills G, Zhou H, Midha A, Donaldson L, Weaver JMR (1998) Scanning thermal microscopy using batch fabricated thermocouple probes. Appl Phys Lett 72:2900-2902
Mills G, Weaver JMR, Harris G, Chen W, Carrejo J, Johnson L, Rogers B (1999) Detection of subsurface voids using scanning thermal microscopy. Ultramicroscopy 80:7-11
Mirny L, Shakhnovich E (2001) Protein folding theory: from lattice to all-atom models. Annu Rev Biophys Biomol Struct 30:361-396
Mitsuoka Y, Niwa T, Ichihara S, Kato K, Muramatsu H, Nakajima K, Shikida M, Sato K (2001) Microfabricated silicon dioxide cantilever with subwavelength aperture. J Microsc 202:12-15
Mo W, Karger BL (2002) Analytical aspects of mass spectrometry and proteomics. Curr Opin Chem Biol 6:666-675
Mollica V, Borassi A, Relini A, Cavalleri O, Bolognesi M, Rolandi R, Gliozzi A (2001) An atomic force microscopy investigation of protein crystal surface topography. Eur Biophys J 30:313-318
Moritz R, Reinstadler D, Fabian H, Naumann D (2002) Time-resolved FTIR difference spectroscopy as tool for investigating refolding reactions of ribonuclease T1 synchronized with trans (r) cis prolyl isomerization. Biopolymers 67:145-155
Morris VJ, Kirby AR, Gunning AP (1999) Using atomic force microscopy to probe food biopolymer functionality. Scanning 21:287-292
Morrison RS, Kinoshita Y, Johnson MD, Uo T, Ho JT, McBee JK, Conrads TP, Veenstra TD (2002) Proteomic analysis in the neurosciences. Mol Cell Proteomics 1:553-560
Morton CJ, Pugh DJR, Brown ELJ, Kahmann JD, Renzoni DAC, Campbell ID (1996) Solution structure and peptide binding of the SH3 domain from human Fyn. Structure 4:705-714
Mui C, Han JH, Wang GT, Musgrave CB, Bent SF (2002) Proton transfer reactions on semiconductor surfaces. J Am Chem Soc 124:4027-4038
Muсoz V, Eaton WA (1999) A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc Natl Acad Sci USA 96:11311-11316
Muramatsu H, Homma K, Chiba N, Yamamoto N, Egawa A (1999) Dynamic etching method for fabricating a variety of tip shapes in the optical fiber probe of a scanning near-field optical microscope. J Microsc 194:383-387
Muroga Y (2001) Derivation of the small angle X-ray scattering functions for local conformations of polypeptide chains in solution. Biopolymers 59:320-329
Natsume T, Yamauchi Y, Nakayama H, Shinkawa T, Yanagida M, Takahashi N, Isobe T (2002) A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics. Anal Chem 74:4725-4733
Nemeth-Cawley JF, Rouse JC (2002) Identification and sequencing analysis of intact proteins via collision-induced dissociation and quadrupole time-of-flight mass spectrometry. J Mass Spectrom 37:270-282
Niggemann M, Steipl B (2000) Exploring local and nonlocal interactions for protein stability by structural motif engineering. J Mol Biol 296:181-195
Nilges M, Macias MJ, O'Donoghue SI, Oschkinat H (1997) Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. J Mol Biol 269:408-422
Nilsson CL (2002) Bacterial proteomics and vaccine development. Am J Pharmacogenomics 2:59-65
Nilsson T, Bassani MR, Larsen TO, Montanarella L (1996) Classification of species in the genus Penicillium by Curie point pyrolysis / mass spectrometry followed by multivariate analysis and artificial neural networks. J Mass Spectrom 31:1422-1428
Noinville S, Revault M, Baron MH (2002) Conformational changes of enzymes adsorbed at liquid-solid interface: relevance to enzymatic activity. Biopolymers 67:323-326
Nölting B (1991) Development of a novel spectrometer for the simultaneous measurement of absorption and circular dichroism (in German). PhD thesis, University of Bochum.
Nölting B (1998) Structural resolution of the folding pathway of a protein by correlation of Phi-values with inter-residue contacts. J Theor Biol 194:419-428
Nölting B (1999a) Analysis of the folding pathway of chymotrypsin inhibitor by correlation of Phi-values with inter-residue contacts. J Theor Biol 197:113-121
Nölting B (1999b) Protein Folding Kinetics: Biophysical Methods. Springer, Berlin Heidelberg New York
Nölting B (2002) Thought transmission (in German). Patent application
Nölting B, Andert K (2000) Mechanism of protein folding. Proteins 41:288-298. Препринт: http://www.pitb.de/nolting/prot00/index.html
Nölting B, Golbik R, Fersht AR (1995) Submillisecond events in protein folding. Proc Natl Acad Sci USA 92:10668-10672. Свободно доступна на сайте автора: http://www.pitb.de/nolting/pnas95.pdf
Nölting B, Golbik R, Neira JL, Soler-Gonzalez AS, Schreiber G, Fersht AR (1997a) The folding pathway of a protein at high resolution from microseconds to seconds. Proc Natl Acad Sci USA 94:826-830. Свободно доступна на сайте автора:
http://www.pitb.de/nolting/pnas97.pdf
Nölting B, Golbik R, Soler-Gonzбlez AS, Fersht AR (1997b) Circular dichroism of denatured barstar shows residual structure. Biochemistry 36:9899-9905
Nölting B, Schälike W, Hampel P, Grundig F, Gantert S, Sips N, Bandlow W, Qi PX (2003) Structural determinants of the rate of protein folding. J Theor Biol 223: 299‑307.
Norledge B, Mayr EM, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HPC (1996) The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins. Nature Struct Biol 3:267-274
Nyman TA (2001) The role of mass spectrometry in proteome studies. Biomol Eng 18:221-227
Odom TW, Huang JL, Lieber CM (2002) Single-walled carbon nanotubes: from fundamental studies to new device concepts. Ann N Y Acad Sci 960:203-215
Oesterhelt F, Oesterhelt D, Pfeiffer M, Engel A, Gaub HE, Mьller DJ (2000) Unfolding pathways of individual bacteriorhodopsins. Science 288:143-146
Ogden ID, Strachan NJC (1993) Enumeration of Escherichia coli in cooked and raw meats by ion mobility spectrometry. J Applied Bacteriology 74:402-405
Orengo CA, Jones DT, Thornton JM (1994) Protein superfamilies and domain superfolds. Nature 372:631-634
Oroudjev E, Soares J, Arcdiacono S, Thompson JB, Fossey SA, Hansma HG (2002) Segmented nanofibers of spider dragline silk: atomic force microscopy and single-molecule force spectroscopy. Proc Natl Acad Sci USA 99:6460-6465
Oubridge C, Ito N, Evans PR, Teo CH, Nagai K (1994) Crystal structure at 1.92 Е resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372:432-438
Panick G, Malessa R, Winter R, Rapp G, Frye KJ, Royer CA (1998) Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small angle X-ray scattering and Fourier transform infrared spectroscopy. J Mol Biol 275:389-402
Panick G, Malessa R, Winter R (1999a) Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FTIR spectroscopy and small angle X-ray scattering. Biochemistry 38:6512-6519
Panick G, Vidugiris GJ, Malessa R, Rapp G, Winter R, Royer CA (1999b) Exploring the temperature-pressure phase diagram of staphylococcal nuclease. Biochemistry 38:4157-4164
Park SJ, Taton TA, Mirkin CA (2002) Array-based electrical detection of DNA with nanoparticle probes. Science 295:1503-1506
Pastore A, Saudek V, Ramponi G, Williams RJP (1992) Three-dimensional structure of acylphosphatase refinement and structure analysis. J Mol Biol 224:427-440
Pereira RS (2001) Atomic force microscopy as a novel pharmacological tool. Biochem Pharmacol 62:975-983
Perez J, Defrenne S, Witz J, Vachette P (2000) Detection and characterization of an intermediate conformation during the divalent ion-dependent swelling of tomato bushy stunt virus. Cell Mol Biol 46:937-948
Perkins WD (1986) Fourier transform infrared spectroscopy. J Chem Education 63:A5-A10
Perkins G, Renken C, Martone ME, Young SJ, Ellisman M, Frey TG (1997a) Electron tomography of neuronal mitochondria: three-dimensional structure and organization of cristae and membrane contacts. J Struct Biol 119:260-272
Perkins G, Renken CW, Song JY, Frey TG, Young SJ, Lamont S, Martone ME, Lindsey S, Ellisman MH (1997b) Electron tomography of large, multicomponent biological structures. J Struct Biol 120:219-227
Perutz MF, Rossmann MG, Cullis AF, Muirhead G, Will G, North AT (1960) Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5 Е resolution, obtained by X-ray analysis. Nature 185:416-422
Petsko GA, Ringe D (2000) Observation of unstable species in enzyme-catalyzed transformations using protein crystallography. Curr Opin Chem Biol 4:89-94
Philippsen A, Im W, Engel A, Schirmer T, Roux B, Mьller DJ (2002) Imaging the electrostatic potential of transmembrane channels: atomic probe microscopy of OmpF porin. Biophys J 82:1667-1676
Phillips J, Gormally J (1992) The laser desorption of organic molecules in ion mobility spectrometry. Int J Mass Spectrom Ion Processes 112:205-214
Phillips GN Jr, Arduini RM, Springer BA, Sligar SG (1990) Crystal structure of myoglobin from a synthetic gene. Proteins 7:358-365
Phizicky EM, Martzen MR, McCraith SM, Spinelli SL, Xing F, Shull NP, Van Slyke C, Montagne RK, Torres FM, Fields S, Grayhack EJ (2002) Biochemical genomics approach to map activities to genes. Methods Enzymol 350:546-559
Pillutla RC, Goldstein NI, Blume AJ, Fisher PB (2002) Target validation and drug discovery using genomic and protein-protein interaction technologies. Expert Opin Ther Targets 6:517-531
Plaxco KW, Simons KT, Baker D (1998) Contact order, transition state placement and the refolding rates of single-domain proteins. J Mol Biol 277:985-994
Pohl DW, Denk W, Lanz M (1984) Optical stethoscopy: image recording with resolution lamda/20. Appl Phys Lett 44:651-653
Powell KD, Wales TE, Fitzgerald MC (2002) Thermodynamic stability measurements on multimeric proteins using a new H/D exchange- and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry-based method. Protein Sci 11:841-851
Pralle A, Florin EL (2002) Cellular membranes studied by photonic force microscopy. Methods Cell Biol 68:193-212
Prechtel K, Bausch AR, Marchi-Artzner V, Kantlehner M, Kessler H, Merkel R (2002) Dynamic force spectroscopy to probe adhesion strength of living cells. Phys Rev Lett 89:028101-1-4
Preston R (1998) The bioweaponeers. The New Yorker, March 9:52-65
Prokop A, Holland CA, Kozlov E, Moore B, Tanner RD (2001) Water-based nanoparticulate polymeric system for protein delivery. Biotechnol Bioeng 75:228-232
Prusiner SB (ed) (1999) Prion Biology and Diseases. Cold Spring Harbor Monograph Series, No 38.
Purves RW, Barnett DA, Ells B, Guevremont R (2000) Investigation of bovine ubiquitin conformers separated by high-field asymmetric waveform ion mobility spectrometry: cross section measurements using energy-loss experiments with a triple quadrupole mass spectrometer. J Am Soc Mass Spectrom 11:738-745
Ranson NA, White HE, Saibil HR (1998) Chaperonins. Biochem J 333:233-242
Razatos A (2001) Application of atomic force microscopy to study initial events of bacterial adhesion. Methods Enzymol 337:276-285
Reimers JR, Shapley WA, Lambropoulos N, Hush NS (2002) An atomistic approach to conduction between nanoelectrodes through a single molecule. Ann N Y Acad Sci 960:100-130
Renfrey S, Featherstone J (2002) Structural proteomics. Nat Rev Drug Discov 1:175-176
Richards FM (1974) The interpretation of protein structures: Total volume, group volume distributions and packing density. J Mol Biol 82:1-14
Riddle DS, Grantcharova VP, Santiago JV, Alm E, Ruczinski I, Baker D (1999) Experiment and theory highlight role of native state topology in SH3 folding. Nature Struct Biol 6:1016-1024
Riedel M, Mьller B, Wintermantel E (2001) Protein adsorption and monocyte activation on germanium nanopyramids. Biomaterials 22:2307-2316
Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-1112
Riek R, Hornemann S, Wider G, Billeter M, Glockshuber R, Wьthrich K (1996) NMR structure of the mouse prion protein domain PrP(121-321). Nature 382:180-182
Riek R, Wider G, Billeter M, Hornemann S, Glockshuber R, Wьthrich K (1998) Prion protein NMR structure and familial human spongiform encephalopathies. Proc Natl Acad Sci USA 95:11667-11672
Riekel C, Vollrath F (2001) Spider silk fibre extrusion: combined wide- and small angle X-ray microdiffraction experiments. Int J Biol Macromol 29:203-210
Rinaldi R, Branca E, Cingolani R, Di Felice R, Calzolari A, Molinari E, Masiero S, Spada G, Gottarelli G, Garbesi A (2002) Biomolecular electronic devices based on self-organized deoxyguanosine nanocrystals. Ann N Y Acad Sci 960:184-192
Rinia HA, Boots JW, Rijkers DT, Kik RA, Snel MM, Demel RA, Killian JA, van der Eerden JP, de Kruijff B (2002) Domain formation in phosphatidylcholine bilayers containing transmembrane peptides: specific effects of flanking residues. Biochemistry 41:2814-2824
Rinnerthaler S, Roschger P, Jakob HF, Nader A, Klaushofer K, Fratzl P (1999) Scanning small angle X-ray scattering analysis of human bone sections. Calcif Tissue Int 64:422-429
Riske KA, Amaral LQ, Lamy-Freund MT (2001) Thermal transitions of DMPG bilayers in aqueous solution: SAXS structural studies. Biochim Biophys Acta 1511:297-308
Rohlff C, Southan C (2002) Proteomic approaches to central nervous system disorders.Curr Opin Mol Ther 4:251-258
Roseman A, Chen S, White H, Braig K, Saibil HR (1996) The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87:241-251
Russell R, Millett IS, Doniach S, Herschlag D (2000) Small angle X-ray scattering reveals a compact intermediate in RNA folding. Nature Struct Biol 7:367-370
Rye HS, Roseman AM, Chen S, Furtak K, Fenton WA, Saibil HR, Horwich AL (1999) GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97:325-338
Saibil H (2000a) Molecular chaperones: containers and surfaces for folding, stabilizing or unfolding proteins. Curr Opin Struct Biol 10:251-258
Saibil HR (2000b) Conformational changes studied by cryo-electron microscopy. Nature Struct Biol 7:711-714
Sandhu KK, McIntosh CM, Simard JM, Smith S, Rotello VM (2002) Gold nanoparticle-mediated transfection of mammalian cells. Bioconjug Chem 13:3-6
Sanger F (1988) Sequences, sequences, and sequences. Annu Rev Biochem 57:1-28
Sanger F, Nicklen S, Coulson AR (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463-5467
Sano Y, Inoue H, Hiragi Y (1999) Differences of reconstitution process between tobacco mosaic virus and cucumber green mottle mosaic virus by synchrotron small angle X-ray scattering using low-temperature quenching. J Protein Chem 18:801-805
Sato M, Hida M, Nagase H (2001) Analysis of pyrolysis products of dimethylamphetamine. J Anal Toxicol 25:304-309
Saurina J, Hernandez-Cassou S (1999) Flow-injection and stopped-flow completely continuous flow spectrometric determination of aniline and cyclohexylamine. Anal Chim Acta 396:151-159
Scheuring S, Stahlberg H, Chami M, Houssin C, Rigaud JL, Engel A (2002) Charting and unzipping the surface layer of Corynebacterium glutamicum with the atomic force microscope. Mol Microbiol 44:675-684
Schindelin H, Marahiel MA, Heinemann U (1993) Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 364:164-168
Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG (2000) The catalytic pathway of cytochrome P450cam at atomic resolution. Science 287:1615-1622
Schmid MB (2002) Structural proteomics: the potential of high-throughput structure determination. Trends Microbiol. 10(Suppl):S27-31
Schmitke JL, Stern LJ, Klibanov AM (1997) The crystal structure of subtilisin Carlsberg in anhydrous dioxane and its comparison with those in water and acetonitrile. Proc Natl Acad Sci USA 94:4250-4255
Schmitke JL, Stern LJ, Klibanov AM (1998) Comparison of X-ray crystal structures of an acyl-enzyme intermediate of subtilisin Carlsberg formed in anhydrous acetonitrile and in water. Proc Natl Acad Sci USA 95:12918-12923
Schnurpfeil R, Klepel S (2000) Radioactivity ion sources for miniaturized ion mobility spectrometers. US Patent 6,064,070
Schцn JH, Meng H, Bao Z (2001a) Self-assembled monolayer organic field-effect transistors. Nature 413:713-716
Schцn JH, Meng H, Bao Z (2001b) Self-assembled monolayer organic field-effect transistors. Nature 414:470-470
Schцnbrunn E, Svergun DI, Amrhein N, Koch MH (1998) Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA). Eur J Biochem 15:406-412
Schrцder W, Matz G, Kubler J (1998) Fast detection of preservatives on waste wood with GC/MS, GC-ECD and ion-mobility spectrometry. Field Anal Chem Technol 2:287-297
Schurmann G, Noell W, Staufer U, de Rooij NF (2000) Microfabrication of a combined AFM-SNOM sensor. Ultramicroscopy 82:33-38
Schwartz DE, Mancinelli RL, White MR (1995) Search for life on Mars: evaluation of techniques. Adv Space Res 15:193-197
Schweitzer-Stenner R (2002) Dihedral angles of tripeptides in solution directly determined by polarized Raman and FTIR spectroscopy. Biophys J 83:523-532
Schwesinger F, Ros R, Strunz T, Anselmetti D, Gьntherodt HJ, Honegger A, Jermutus L, Tiefenauer L, Plьckthun A (2000) Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates. Proc Natl Acad Sci USA 97:9972-9977
Scott DJ, Grossmann JG, Tame JR, Byron O, Wilson KS, Otto BR (2002) Low resolution solution structure of the Apo form of Escherichia coli haemoglobin protease Hbp. J Mol Biol 315:1179-1187
Seeman NC, Belcher AM (2002) Emulating biology: building nanostructures from the bottom up. Proc Natl Acad Sci USA 99:6451-6455
Segel DJ, Eliezer D, Uversky V, Fink AL, Hodgson KO, Doniach S (1999) Transient dimer in the refolding kinetics of cytochrome c characterized by small angle X-ray scattering. Biochemistry 38:15352-15359
Sekatskii SK, Dietler G (1999) Near-field optical excitation as a dipole-dipole energy transfer process. J Microsc 194:255-259
Seong GH, Kobatake E, Miura K, Nakazawa A, Aizawa M (2002) Direct atomic force microscopy visualization of integration host factor-induced DNA bending structure of the promoter regulatory region on the Pseudomonas TOL plasmid. Biochem Biophys Res Commun 291:361-366
Service RF (2001) Breakthrough of the year. Molecules get wired. Science 294:2442-2443
Service RF (2002) Analytical chemisty - new test could speed bioweapon detection. Science 295:1447-1447
Shakhnovich EI (1997) Theoretical studies of protein-folding thermodynamics and kinetics. Curr Opin Struct Biol 7:29-40
Shakhnovich E, Abkevich V, Ptitsyn O (1996) Conserved residues and the mechanism of protein folding. Nature 379:96-98
Shevchenko A, Chernushevic I, Shevchenko A, Wilm M, Mann M (2002) "De novo" sequencing of peptides recovered from in-gel digested proteins by nanoelectrospray tandem mass spectrometry. Mol Biotechnol 20:107-118
Shilton B, Svergun DI, Volkov VV, Koch MH, Cusack S, Economou A (1998) Escherichia coli SecA shape and dimensions. FEBS Lett 436:277-282
Shimonishi Y, Hong YM, Kitagishi T, Matsuo T, Matsuda H, Katakuse I (1980) Sequencing of peptide mixtures by Edman degradation and field-desorption mass spectrometry. Eur J Biochem 112:251-264
Shumate CB, Hill HH (1989) Coronaspray nebulization and ionization of liquid samples for ion mobility spectrometry. Anal Chem 61:601-606
Simpson AA, Tao YZ, Leiman PG, Badasso MO, He Y, Jardine PJ, Olson NH, Morais MC, Grimes S, Anderson DL, Baker TS, Rossmann MG (2000) Structure of the bacteriophage Phi29 DNA packaging motor. Nature 408:745-750
Sisson PR, Freeman R, Magee JG, Lightfoot NF (1991) Differentiation between mycobacteria of the Mycobacterium tuberculosis complex by pyrolysis mass spectrometry. Tubercle 72:206-209
Smith DE, Tans SJ, Smith SB, Grimes S, Anderson DL, Bustamante C (2001) The
bacteriophage straight Phi29 portal motor can package DNA against a large internal force. Nature 413:748-752
Smith SB, Cui Y, Bustamante C (1996) Overstreaching B-DNA: the elastic resonse of individual double-stranded and single-stranded DNA molecules. Science 271:795-799
Smith GB, Eiceman GA, Walsh MK, Critz SA, Andazola E, Ortega E, Cadena F (1997) Detection of Salmonella typhimurium by hand-held ion mobility spectrometer: a quantitative assessment of response characteristics. Field Anal Chem Technol 1:213-226
Snabe T, Petersen SB (2002) Application of infrared spectroscopy (attenuated total reflection) for monitoring enzymatic activity on substrate films. J Biotechnol 95:145-155
Snow CD, Nguyen H, Pande VS, Gruebele M (2002) Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420:102-106
Snyder AP, McClennen WH, Dworzanski JP, Meuzelaar HL (1990) Characterization of underivatized lipid biomarkers from microorganisms with pyrolysis short-column gas chromatography / ion trap mass spectrometry. Anal Chem 62:2565-2573
Snyder AP, Miller M, Shoff DB, Eiceman GA, Blyth DA, Parsons JA (1991a) Enzyme-substrate assay for the qualitative detection of microorganisms by ion mobility spectrometry. J Microbiol Methods 14:21-32
Snyder AP, Shoff DB, Eiceman GA, Blyth DA, Parsons JA (1991b) Detection of bacteria by ion mobility spectrometry. Anal Chem 63:526-529
Snyder AP, Harden CS, Brittain AH, Kim MG, Arnold NS, Meuzelaar HLC (1993) Portable hand-held gas chromatography / ion mobility spectrometry device. Anal Chem 65:299-306
Snyder AP, Blyth DA, Parsons JA (1996a) Ion mobility spctrometry as an immunoassay detection technique. J Microbiol Methods 27:81-88
Snyder AP, Thornton SN, Dworzanski JP, Meuzelaar HLC (1996b) Detection of picolinic acid biomarker in Bacillus spores using a potentially field-portable pyrolysis gas chromatography / ion mobility spectrometer. Field Anal Chem Technol 1:49-59
Snyder AP, Maswadeh WM, Parson JP, Tripathi A, Meuzelaar HLC, Dworzanski J, Kim MG (1999) Field detection of Bacillus spore aerosols with stand-alone pyrolysis gas chromatography / ion mobility spectrometry. Field Anal Chem Technol 3:315-326
Snyder AP, Maswadeh WM, Tripathi A, Dworzanski JP (2000) Detection of gram-negative Erwinia herbicola outdoor aerosols with pyrolysis gas chromatography / ion mobility spectrometry. Field Anal Chem Technol 4:111-126
Snyder AP, Tripathi A, Maswadeh WM, Ho J, Spence M (2001) Field detection and identification of a bioaerosol suite by pyrolysis / gas chromatography / ion mobility spectrometry. Field Anal Chem Technol 5:190-204
Spangler GE (1982) Membrane interface for ion mobility detector cells. US Patent 4,311,669
Spangler GE (1992a) Preconcentrator for ion mobility spectrometer. US Patent 5,083,019
Spangler GE (1992b) Space charge effects in ion mobility spectrometry. Anal Chem 64:1312-1312
Spangler GE, Carrico JP (1983) Membrane inlet for ion mobility spectrometry (plasma chromatography). Int J Mass Spectrom Ion Phys 52:267-287
Spangler GE, Roehl JE, Patel GB, Dorman A (1994) Photoionization ion mobility spectrometer. US Patent 5,338,931
Srajer V, Teng TY, Ursby T, Pradervand C, Ren Z, Adachi SI, Schildkamp W, Bourgeois D, Wulff M, Moffat K (1996) Photolysis of the carbon monoxide complex of myoglobin: nanosecond time-resolved crystallography. Science 274:1726-1729
Stachelberger H (2001) personal communication.
Stagljar I, Fields S (2002) Analysis of membrane protein interactions using yeast-based technologies. Trends Biochem Sci 27:559-63
Steinfeld JI, Wormhoudt J (1998) Explosives detection: a challenge for physical chemistry. Annu Rev Phys Chem 49:203-232
Stephenson JL, McLuckey SA, Reid GE, Wells JM, Bundy JL (2002) Ion/ion chemistry as a top-down approach for protein analysis. Curr Opin Biotechnol 13:57-64
St Louis RH, Hill HH (1990) Ion mobility spectrometry in analytical chemistry. CRC Crit Rev Anal Chem 21:321-355
Stцckle RM, Fokas C, Deckert V, Zenobi R, Sick B, Hecht B, Wild UP (1999a) High quality near-field optical probes by tube etching. Appl Phys Lett 75:160-162
Stцckle RM, Schaller N, Deckert V, Fokas C, Zenobi R (1999b) Brighter near-field optical probes by means of improving the optical destruction threshold. J Microsc 194:378-382
Stocklin PL (1989) Hearing device. US Patent 4,858,612
Stoeva S, Idakieva K, Betzel C, Genov N, Voelter W (2002) Amino acid sequence and glycosylation of functional unit RtH2-e from Rapana thomasiana (gastropod) hemocyanin. Arch Biochem Biophys 399:149-158
Stone E, Gillig KJ, Ruotolo B, Fuhrer K, Gonin M, Schultz A, Russell DH (2001) Surface-induced dissociation on a MALDI ion mobility / orthogonal time-of-flight mass spectrometer: sequencing peptides from an "in-solution" protein digest. Anal Chem 73:2233-2238
Strachan NJC, Nicholson FJ, Ogden ID (1995) An automated sampling system using ion mobility spectrometry for the rapid detection of bacteria. Anal Chim Acta 313:63-67
Strunz T, Oroszlan K, Schдfer R, Gьntherodt HJ (1999) Dynamic force spectroscopy of single DNA molecules. Proc Natl Acad Sci USA 96:11277-11282
Sultana S, Magee JT, Duerden B (1995) Analysis of Bacteroides species by pyrolysis mass spectrometry. Clin Infect Dis 20 Suppl 2:S122-S127
Swedberg SA, Kaltenbach P, Witt KE, Bek F, Mittelstadt LS (1996) Fully integrated iniaturized planar liquid sample handling and analysis device. US Patent 5,571,410
Swedberg SA, Brennen RA (2001) Device for high throughput sample processing, analysis and collection, and methods of use thereof. US Patent 6,240,790
Synge EH (1928) A suggested method for extending microscopic resolution into the ultra-microscopic region. Phil Mag 6:356-362
Talapatra A, Rouse R, Hardiman G (2002) Protein microarrays: challenges and promises. Pharmacogenomics 3:527-536
Tanaka S, Scheraga HA (1975) Model of protein folding: Inclusion of short-, medium-, and long-range interactions. Proc Natl Acad Sci USA 72:3802-3806
Tanaka S, Scheraga HA (1977) Hypothesis about the mechanism of protein folding. Macromolecules 10:291-304
Taylor J, Goodacre R, Wade WG, Rowland JJ, Kell DB (1998) The deconvolution of pyrolysis mass spectra using genetic programming: application to the identification of some Eubacterium species. FEMS Microbiol Lett 160:237-246
Taylor SJ (1996) Introduction of samples into an ion mobility spectrometer. US Patent 5,574,277
Taylor SJ, Turner RB (1999) Ion mobility spectrometers. US Patent 5,952,652
Tcherkasskaya O, Uversky VN (2001) Denatured collapsed states in protein folding: example of apomyoglobin. Proteins 44:244-254
Tilleman K, Van den Haute C, Geerts H, van Leuven F, Esmans EL, Moens L (2002) Proteomics analysis of the neurodegeneration in the brain of tau transgenic mice. Proteomics 2:656-665
Timmins EM, Goodacre R (1997) Rapid quantitative analysis of binary mixtures of Escherichia coli strains using pyrolysis mass spectrometry with multivariate calibration and artificial neural networks. J Appl Microbiol 83:208-218
Tiner WJS, Potaman VN, Sinden RR, Lyubchenko YL (2001) The structure of intramolecular triplex DNA: atomic force microscopy study. J Mol Biol 314:353-357
Toledo-Crow R, Yang PC, Chen Y, Vaez-Iravani M (1992) Near-field differential scanning optical microscope with atomic force regulation. Appl Phys Lett 60:2957-2959
Torres J, Briggs JA, Arkin IT (2002) Multiple site-specific infrared dichroism of CD3-zeta, a transmembrane helix bundle. J Mol Biol 316:365-374
Tripathi A, Maswadeh WM, Snyder AP (2001) Optimization of quartz tube pyrolysis atmospheric pressure ionization mass spectrometry for the generation of bacterial biomarkers. Rapid Commun Mass Spectrom 15:1672-1680
Trudel E, Gallant J, Mons S, Mioskowski C, Lebeau L, Jeuris K, Foubert P, De Schryver F, Salesse C (2001) Design of functionalized lipids and evidence for their binding to photosystem II core complex by oxygen evolution measurements, atomic force microscopy, and scanning near-field optical microscopy. Biophys J 81:563-571
Turner DR (1983) Etch procedure for optical fibers. US Patent 4,469,554
Turner BR (1993) Ion mobility detector. US Patent 5,227,628
Unger R, Moult J (1996) Local interactions dominate folding in a simple protein model. J Mol Biol 259:988-994
Valle F, Dietler G, Londei P (2001) Single-molecule imaging by atomic force microscopy of the native chaperonin complex of the thermophilic archaeon Sulfolobus solfataricus. Biochem. Biophys Res Commun 288:258-262
van den Berg B, Wain R, Dobson CM, Ellis RJ (2000) Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J 19:3870-3875
van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J (1991) Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex. Science 252:839-842
van Kempen TA, Powers WJ, Sutton AL (2002) Technical note: Fourier transform infrared (FTIR) spectroscopy as an optical nose for predicting odor sensation. J Anim Sci 80:1524-1527
van Nuland NAJ, Hangyi IW, van Schaik RC, Berendsen HJC, van Gunsteren WF, Scheek RM, Robillard GT (1994) The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. J Mol Biol 237:544-559
Veerman JA, Otter AM, Kuipers L, van Hulst NF (1998) High definition aperture probes for near-field optical microscopy fabricated by focused ion beam milling. Appl Phys Lett 72:3115-3117
Vendrell J, Billeter M, Wider G, Aviles FX, Wьthrich K (1991) The NMR structure of the activation domain isolated from porcine procarboxypeptidase B. EMBO J 10:11-15
Vijay-Kumar S, Bugg CE, Cook WJ (1987) Structure of ubiquitin refined at 1.8 Е resolution. J Mol Biol 194:531-544
Voigt J, Schrцtter T (1999) Phonon assisted exciton transitions on LHC-II complexes - a long wavelength absorption mechanism by cooperative action of photons and protein vibrations. Zeitschrift Phys Chem 211:181-191
Volz K, Matsumura P (1991) Crystal structure of Escherichia coli CheY refined at 1.7 Е resolution. J Biol Chem 266:15511-15519
von Ardenne M (1940) Elektronen-Ьbermikroskopie, Springer, Berlin
Vora KN, Carrico JP Sr, Spangler GE, Campbell DN, Martin CE (1987) Ion mobility spectrometer. US Patent 4,712,008
Vytvytska O, Nagy E, Bluggel M, Meyer HE, Kurzbauer R, Huber LA, Klade CS (2002) Identification of vaccine candidate antigens of Staphylococcus aureus by serological proteome analysis. Proteomics 2:580-590
White HE, Chen S, Roseman AM, Yifrach O, Horovitz A, Saibil H (1997) Structural basis of allosteric changes in the GroEL mutant Arg197(r)Ala. Nature Struct Biol 4:690-694
Whitelegge JP, le Coutre J (2002) Proteomics. Making sense of genomic information for drug discovery. Am J Pharmacogenomics 1:29-35
Wikstrцm M, Sjцbring U, Drakenberg T, Forsйn S, Bjцrck L (1995) Mapping of the immunoglobulin light chain-binding site of protein L. J Mol Biol 250:128-133
Williams S, Causgrove TP, Gilmanshin R, Fang KS, Callender RH, Woodruff WH, Dyer RB (1996) Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry 35:691-697
Williams JC, Zeelen JP, Neubauer G, Vriend G, Backmann J, Michels PA, Lambeir AM, Wierenga RK (1999) Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Eng 12:243-250
Williams BH, Hathout Y, Fenselau C (2002) Structural characterization of lipopeptide biomarkers isolated from Bacillus globigii. J Mass Spectrom 37:259-264
Williamson RL, Miles MJ (1996) Melt-drawn scanning near-field optical microscopy probe profiles. J Appl Phys 80:4804-4812
Williamson RL, Brereton LJ, Antognozzi M, Miles MJ (1998) Are artefacts in scanning near-field optical microscopy related to the misuse of shear force? Ultramicroscopy 71:165-175
Wilmot CM, Pearson AR (2002) Cryocrystallography of metalloprotein reaction intermediates. Curr Opin Chem Biol 6:202-207
Wolynes PG, Luthey-Schulten Z, Onuchic JN (1996) Fast folding experiments and the topography of protein-folding energy landscapes. Chem Biol 3:425-432
Wu C, Hill HH, Gamerdinger AP (1998a) Electrospay ionization / ion mobility spectrometry as a field monitoring method for the detection of atrazine in natural water. Field Anal Chem Technol 2:155-161
Wu C, Siems WF, Asbury GR, Hill HH (1998b) Electrospray ionization high-resolution ion mobility spectrometry / mass spectrometry. Anal Chem 70:4929-4938
Wu C, Siems WF, Klasmeier J, Hill HH (2000) Separation of isomeric peptides using electrospray ionization/high-resolution ion mobility spectrometry. Anal Chem 72:391-395
Wuite GJL, Smith SB, Young M, Keller D, Bustamante C (2000) Single-molecule studies of the effect of template tension on T7 DNA polymerase activity. Nature 404:103-106
Wynne SA, Crowther RA, Leslie AGW (1999) The crystal structure of the human hepatitis B virus capsid. Mol Cell 3:771-780
Xu L, Frederik P, Pirollo KF, Tang WH, Rait A, Xiang LM, Huang W, Cruz I, Yin Y, Chang EH (2002) Self-assembly of a virus-mimicking nanostructure system for efficient tumor-targeted gene delivery. Hum Gene Ther 13:469-481
Yamasaki R, Hoshino M, Wazawa T, Ishii Y, Yanagida T, Kawata Y, Higurashi T, Sakai K, Nagai J, Goto Y (1999) Single molecular observations of the interaction of GroEL with substrate proteins. J Mol Biol 292:965-972
Yarmush ML, Jayaraman A (2002) Advances in proteomic technologies. Annu Rev Biomed Eng 4:349-373
Ying LM, Bruckbauer A, Rothery AM, Korchev YE, Klenerman D (2002) Programmable delivery of DNA through a nanopipet. Anal Chem 74:1380-1385
Yip CM (2001) Atomic force microscopy of macromolecular interactions. Curr Opin Struct Biol 11:567-572
Zal F, Chausson F, Leize E, van Dorsselaer A, Lallier FH, Green BN (2002) Quadrupole time-of-flight mass spectrometry of the native hemocyanin of the deep-sea crab Bythograea thermydron. Biomacromolecules 3:229-231
Zhang J, Oettmeier W, Gennis RB, Hellwig P (2002a) FTIR spectroscopic evidence for the involvement of an acidic residue in quinone binding in cytochrome bd from Escherichia coli. Biochemistry 41:4612-4617
Zhang ZL, Pang DW, Zhang RY, Yan JW, Mao BW, Qi YP (2002b) Investigation of DNA orientation on gold by EC-STM. Bioconjug Chem 13:104-109
Zheng W, Doniach S (2002) Protein structure prediction constrained by solution X-ray scattering data and structural homology identification. J Mol Biol 316:173-187
Zheng PP, Kros JM, Sillevis-Smitt PA, Theo M Luider Fn FM (2003) Proteomics in primary brain tumors. Front Biosci 8:D451-463
Zhou Y, Karplus M (1999) Interpreting the folding kinetics of helical proteins. Nature 401:400-403
Zhou H, Midha A, Mills G, Thoms S, Murad SK, Weaver JMR (1998) Generic scanned-probe microscope sensors by combined micromachining and electron-beam lithography. J Vacuum Sci Technol B 16:54-58
Zhou H, Mills G, Chong BK, Midha A, Donaldson L, Weaver JMR (1999) Recent progress in the functionalization of atomic force microscope probes using electron-beam nanolithography. J Vacuum Sci Technol A 17:2233-2239
Zocchi G (2001) Force measurements on single molecular contacts through evanescent wave microscopy. Biophys J 81:2946-2953