Biophysical chemistry of proteins: An introduction to laboratory methods

Biophysical Chemistry of Proteins: An Introduction to Laboratory Methods

Volumn , Issue , 2011, Pages 1-510

  Buxbaum, Engelbert ^a  

^a ROSS UNIVERSITY SCHOOL OF MEDICINE   (Dominica)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84900692827     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4419-7251-4     Document Type: Book

References (450)

1. E. ABBE: Beiträge zur theorie des mikroskops und der mikroskopischen wahrnehmung. Arch. Mikr. Anat. 9 (1873) 413-420. doi: 10.1007/BF02956173
2. G. ACKERS: Analytical gel chromatography of proteins. In: Mechanisms and pathways of heterotrimeric G protein signaling, C. ANFINSEN, J. EDSALL et al., eds., vol. 24 of Adv. Protein Chem. chap. 5, pp. 343-441. (Academic, New York), 1970. ISBN 978-0120342242
3. G. ADAIR: A critical study of the direct method of measuring the osmotic pressure of hoemoglobin. Proc. R. Soc. Lond. A 108 (1925) (748) 627-637
4. G. ADAIR: The osmotic pressure of hoemoglobin in the absence of salts. Proc. R. Soc. Lond. A 108 (1925) 292-300
5. 2H solid-state NMR spectroscopy. Eur. Biophys. J. 36 (2007) 451-460. doi: 10.1007/s00249-006-0122-2
6. K. ALTLAND: IPGMaker: A program for IBM compatible personal computers to create and test recipes for immobilized pH gradients. Electrophoresis 11 (1990) 140-147. doi: 10.1002/elps.1150110207
7. H. AN, J. FROEHLICH et al.: Determination of glycosylation sites and site-specific heterogeneity in glycoproteins. Curr. Opin. Chem. Biol. 13 (2009) (4) 421-426. doi: 10.1016/j.cbpa.2009.07.022
8. K. ANDERSON, A. POTTER et al.: Protein expression changes in spinal muscular atrophy revealed with a novel antibody array technology. Brain 126 (2003) (9) 2052-2064. doi: 10.1093/brain/awg208. URL http://brain. oxfordjournals.org/cgi/reprint/126/9/2052.pdf
9. L. ANDERSSON, H. JÖRNVALL et al.: Separation of isozymes of horse liver alcohol dehydrogenase and purification of the enzyme by affinity chromatography on an immobilized AMP-analogue. Biochim. Biophys. Acta 364 (1974) 1-8. doi: 10.1016/0005-2744 (74) 90126-0
10. S. ARRHENIUS: Über die reaktionsgeschwindigkeit bei der inversion von rohrzucker durch säuren. Z. phys. Chem. 4 (1889) 226-248
11. C. ARTOM: Labeled compounds in the study of phospholipid metabolism. Methods Enzymol. 4 (1957) 809-840. doi: 10.1016/0076-6879 (57) 04081-1
12. A. ASHKIN, J. M. DZIEDZIC et al.: Observation of a single-beam gradient force optical trap for dielectric particles. Opt. Lett. 11 (1986) 288. URL http://ol.osa.org/abstract.cfm?URI=ol-11-5-288
13. K. ASLAN & C. GEDDES: New tools for rapid clinical and bioagent diagnostics: Microwaves and plasmonic nanostructures. Analyst 133 (2008) 1469-1480. doi: 10.1039/b808292h
14. S. AUDIC, F. LOPEZ et al.: SAmBa: An interactive software for optimizing the design of biological macromolecules crystallization experiments. Proteins 29 (1997) 252-257. doi: 10.1002/(SICI) 1097-0134 (199710) 29:2<252::AID- PROT12>3.0. CO;2-N
15. A. AYED, A. KRUTCHINSKY et al.: Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization timeofflight mass spectrometry. Rapid Commun. Mass Spectrom. 12 (1998) 339-344. doi: 10.1002/(SICI) 1097-0231 (19980415) 12:7<339::AID-RCM163>3.0. CO;2-6
16. P. BARTH, T. ALBER et al.: Accurate, conformation-dependent predictions of solvent effects on protein ionization constants. Proc. Natl. Acad. Sci. USA 104 (2007) 4898-4903. doi: 10.1073/pnas.0700188104
17. J. BASSHAM, A. BENSON et al.: Isotope studies in photosynthesis. J. Chem. Educ. 30 (1953) 274-283. doi: 10.1021/ed030p274
18. A. BATISTA, W. VETTER et al.: Use of focused open vessel microwave-assisted extraction as prelude for the determination of the fatty acid profile of fish - a comparison with results obtained after liquid-liquid extraction according to Bligh and Dyer. Eur. Food Res. Technol. 212 (2001) 377-384. doi: 10.1007/s002170000240
19. T. BAYBURT & S. SLIGAR: Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers. Protein Sci. 12 (2003) 2476-2481. doi: 10.1110/ps.03267503
20. H.-J. BÖCKENHAUER & D. BONGARTZ: Algorithmische grundlagen der bioinformatik. 1st edn.. (Teubner, Wiesbaden), 2003. ISBN 978-3-519-00398-8
21. J. BECHHOEFER & S. WILSON: Faster, cheaper, safer optical tweezers for the undergraduate laboratory. Am. J. Phys. 70 (2002) 393-400. doi: 10.1119/1.1445403. URL http://link.aip.org/link/?AJP/70/393/1
22. M. BELOV, M. GORSHKOV et al.: Zeptomole-sensitivity electrospray ionization - Fourier transform ion cyclotron resonance mass spectrometry of proteins. Anal. Chem. 72 (2000) 2271-2279. doi: 10.1021/ac991360b
23. A. BENSADOUN & D. WEINSTEIN: Assay of proteins in the presence of interfering materials. Anal Biochem. 70 (1976) 241-250. doi: 10.1016/S0003-2697 (76) 80064-4
24. M. BERENBAUM: What is synergy? Pharmacol. Rev. 41 (1989) 93-141. URL http://pharmrev.aspetjournals.org/cgi/reprint/41/2/93
25. M. BEREZOVSKI, M. LECHMANN et al.: Aptamer-facilitated biomarker discovery (AptaBiD). J. Am. Chem. Soc. 130 (2008) 9137-9143. doi: 10.1021/ja801951p
26. J. BERNAL & D. CROWFORD: X-ray photographs of crystalline pepsin. Nature 133 (1934) 794-795. doi: 10.1038/133794b0
27. H. BISSWANGER: Enzyme kinetics, theories and methods. 3rd edn.. (Wiley-VCH, Weinheim), 2008. ISBN 978-3527319572
28. B. BJELLQVIST, K. EK et al.: Isoelectric focusing in immobilized pH gradients: principle, methodology and some applications. J. Biochem. Biophys. Methods 6 (1982) 317-339. doi: 10.1016/0165-022X (82) 90013-6
29. G. BLACKBURN, H. SHAH et al.: Electrochemiluminescence detection for development of immunoassays and DNA probe assays for clinical diagnostics. Clin. Chem. 37 (1991) 1534. URL http://www.clinchem.org/cgi/reprint/37/9/1534.pdf
30. B. BLAGOEV, I. KRATCHMAROVA et al.: A proteomics strategy to elucidate functional protein-protein interactions. Nat. Biotechnol. 21 (2003) 315-318. doi: 10.1038/nbt790
31. E. BLIGH & W. DYER: A rapid method for total lipid extraction and purification. Can. J. Biochem. Physiol. 37 (1959) (8) 911-917. doi: 10.1139/y59-099
32. 2+ concentrations in living cells. Prog. Biophys. Mol. Biol. 40 (1982) 1-114. doi: 10.1016/0079-6107 (82) 90011-6
33. D. BOLEN: Effects of naturally occuring osmolytes on protein stability and solubility: Issues important in protein crystallization. Methods 34 (2004) 312-322. doi: 10.1016/j.ymeth.2004.03.022
34. D. BOLEN & I. BASKAKOV: The osmophobic effect: Natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310 (2001) 955-963. doi: 10.1006/jmbi.2001.4819
35. P. BOOTH & P. CURNOW: Folding scene investigation: Membrane proteins. Curr. Opin. Struct. Biol. 19 (2009) 8-13. doi: 10.1016/j.sbi.2008.12.005
36. M. BRADFORD: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principles of protein-dye binding. Anal. Biochem. 72 (1976) 248-254. doi: 10.1016/0003-2697 (76) 90527-3
37. S. BRAHMS & J. BRAHMS: Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138 (1980) 149-178. doi: 10.1016/0022-2836 (80) 90282-X
38. G. U. BUBLITZ & S. G. BOXER: STARK spectroscopy: Applications in chemistry, biology, and materials science. Annu. Rev. Phys. Chem. 48 (1997) 213-242. doi: 10.1146/annurev. physchem.48.1.213
39. K. BUCHHOLZ, V. KASCHE et al.: Biocatalysts and enzyme technology. 2nd edn.. (Wiley-VCH, Weinheim), 2005. ISBN 9-783527-304974
40. D. BUNKA & P. STOCKLEY: Aptamers come of age - at last. Nat. Rev. Microbiol. 4 (2006) 588-596. doi: 10.1038/nrmicro1458
41. E. BUXBAUM: Co-operating ATP sites in the multiple drug resistance transporter Mdr1. Eur. J. Biochem. 265 (1999) 54-63. doi: 10.1046/j.1432-1327. 1999.00643.x
42. E. BUXBAUM: Co-operative binding sites for transported substrates in the multiple drug resistance transporter Mdr1. Eur. J. Biochem. 265 (1999) 64-70. doi: 10.1046/j.1432-1327.1999.00644.x
43. E. BUXBAUM: Cationic electrophoresis and electrotransfer of membrane glycoproteins. Anal. Biochem. 314 (2003) 70-76. doi:10.1016/S0003-2697 (02) 00639-5
44. E. BUXBAUM: Introduction to protein structure and function. (Springer, New York), 2007. ISBN 978-0387-26352-6
45. E. BUXBAUM: Cationic electrophoresis and eastern blotting. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 115-128
46. +-ATPase. J. Theor. Biol. 155 (1992) 21-23. doi: 10.1016/S0022-5193 (05) 80546-6
47. E. BUXBAUM & P. WOODMAN: Binding of ATP and nucleotide analogues to Hsc70. Biochem. J. 318 (1996) 923-929. URL http://www.ncbi.nlm.nih.gov/pmc/ articles/PMC1217706/pdf/8836139.pdf
48. M. CAFFREY: A lipids eye view of membrane protein crystallization in mesophases. Curr. Opin. Struct. Biol. 10 (2000) 486-497. URL http://www.ul.ie/~ces/PDF%20files/Lipid.pdf
49. C. CANTOR & P. SCHIMMEL: Biophysical chemistry vol 1-3. (W. H. Freeman, San Francisco), 1980
50. C. CARTER & R. SWEET (eds.): Macromolecular crystallography vol. A, vol. 276 of Methods Enzymol. (Academic, New York, London), 1997. ISBN 978-0-12-182177-7
51. N. CATSIMPOOLAS & J. KENNEY: Analytical isotachophoresis of human serum proteins with ampholine spacers. Biochim. Biophys. Acta - Protein Structure 285 (1972) 287-292. doi: 10.1016/0005-2795 (72) 90312-1
52. 2+)-ATPase. Biochim. Biophys. Acta 899 (1987) 83-92. doi: 10.1016/0005-2736 (87) 90242-2
53. R. CELIKEL, E. PETERSON et al.: Crystal structure of a therapeutic single chain antibody in complex with two drugs of abuse - methamphetamine and 3, 4-methylenedioxymethamphetamine. Protein Sci. 18 (2009) 2336-2345. doi: 10.1002/pro.244
54. B. CHANCE: The stopped-flow method and chemical intermediates in enzyme reactions - a personal essay. Photosynth. Res. 80 (2004) 387-400. doi: 10.1023/B:PRES.0000030601.50634.0c
55. A. CHANUTIN, S. LUDEWIG et al.: Studies on the calcium-protein relationship with the aid of the ultracentrifuge. J. Biol. Chem. 143 (1942) 737-751. URL http://www.jbc.org/content/143/3/763.full.pdf
56. L. CHARBONNIÈRE & N. HILDEBRANDT: Lanthanide complexes and quantum dots: A bright wedding for resonance energy transfer. Eur. J. Inorg. Chem. 2008 (2008) 3241-3251. doi: 10.1002/ejic.200800332
57. A. CHATTOPADHYAY & E. LONDON: Fluorimetric determination of critical micelle concentration avoiding interference from detergent charge. Anal. Biochem. 139 (1984) 408-412. doi: 10.1016/0003-2697 (84) 90026-5
58. J. CHERRY & A. FIDANTSEF: Directed evolution of industrial enzymes: an update. Curr. Opin. Biotechnol. 14 (2003) 438-443. doi: 10.1016/S0958-1669 (03) 00099-5
59. P. CHONG & R. HODGES: A new heterobifunctional cross-linking reagent for the study of biological interactions between proteins. I. Design, synthesis, and characterization. J. Biol. Chem. 256 (1981) 5064-5070. URL http://www.jbc.org/content/256/10/5064.full.pdf
60. A. CHRAMBACH: The practice of quantitative gel electrophoresis. (VCH, Weinheim), 1985. ISBN 978-3527260393
61. S. CHRISTENSEN, E. H. MOELLER et al.: Preliminary studies of the physical stability of a glucagon-like peptide-1 derivate in the presence of metal ions. Eur. J. Pharm. Biopharm. 66 (2006) 366-371. doi: 10.1016/j.ejpb.2006.11.019
62. W. CLELAND: Determination of equilibrium isotope effects by the equilibrium perturbation method. Methods Enzymol. 87 (1982) 641-646. doi: 10.1016/S0076-6879 (82) 87033-X
63. W. CLELAND: The use of isotope effects to determine transition-state structure for enzymatic reactions. Methods Enzymol. 87 (1982) 625-641. doi: 10.1016/S0076-6879 (82) 87033-X
64. W. CLELAND: Use of isotope effects to elucidate enzyme mechanism. CRC Crit. Rev. Biochem. 13 (1982) 385-428. doi: 10.3109/10409238209108715
65. W. CLELAND: The use of isotope effects to determine enzyme mechanism. J. Biol. Chem. 278 (2003) 51 975-51 984. doi: 10.1074/jbc. X300005200
66. M. COMISAROW & A. MARSHALL: Fourier transform ion cyclotron resonance spectroscopy. Chem. Phys. Lett. 25 (1974) (2) 282-283. doi: 10.1016/0009-2614 (74) 89137-2
67. I. H. G. S. CONSORTIUM: Initial sequencing and analysis of the human genome. Nature 409 (2001) 860-921. doi: 10.1038/35057062
68. P. COOK & W. CLELAND: Enzyme kinetics and mechanism. (Garland, New York), 2007. ISBN 978-0-8153-4140-6
69. R. COPELAND: Enzymes. A practical Introduction to structure, mechanism and data analysis. 2nd edn.. (Wiley-VCH, New York), 2000. ISBN 978-0471359296
70. L. CRAIG: Identification of small amounts of organic compounds by distribution studies. J. Biol. Chem. 155 (1944) 519-534. URL http://www.jbc.org/content/155/2/519.full.pdf
71. T. CREIGHTON: Electrophoretic analysis of the unfolding of proteins by urea. J. Mol. Biol. 129 (1979) 235-264. doi: 10.1016/0022-2836 (79) 90279-1
72. L. CUMMINGS, M. SNYDER et al.: Protein chromatography on hydroxyapatite columns. Methods Enzymol. 463 (2009) 387-404. doi: 10.1016/S0076-6879 (09) 63024-X
73. J. DABAN, S. BARTOLOMREA et al.: Use of the hydrophobic probe nile red for the fluorescent staining of protein bands in sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 199 (1991) 169-174. doi: 10.1016/0003-2697 (91) 90085-8
74. M. DAS, T. MIYAKAWA et al.: Specific radiolabeling of a cell surface receptor for epidermal growth factor. Proc. Natl. Acad. Sci. USA 74, (1977) 2790-2794. URL http://www.pnas.org/content/74/7/2790.full.pdf
75. B. DAVIS: Disc electrophoresis - II Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121 (1964) 404-427. doi: 10.1111/j.1749-6632. 1964.tb14213.x. URL http://www.pipeline.com/~lenornst/DiscEle2.pdf
76. A. DERFUS, W. CHAN et al.: Probing the cytotoxicity of semiconductor quantum dots. Nano Lett. 4 (2004) (1) 11-18. doi: 10.1021/nl0347334. URL http://homepages.wmich.edu/~sobare/courses/Nano%20Lett%202004-4-11.pdf
77. P. DEVINE & J. WARREN: Glycoprotein detection on immobilon PVDF transfer membrane using the periodic acid/SCHIFF reagent. Biotechniques 8 (1990) 492-495
78. R. DISCIPIO: Preparation of colloidal gold particles of various sizes using sodium borohydride and sodium cyanoborohydride. Anal. Biochem. 236 (1996) 168-170. doi: 10.1006/abio.1996.0146
79. E. DOLK, M. VAN der VAART et al.: Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. Appl. Environ. Microbiol. 71 (2005) 442-450. doi: 10.1128/AEM.71.1.442-450.2005
80. A. DOUNCE, R. WITTER et al.: A method for isolating intact mitochondria and nuclei from the same homogenate, and the influence of mitochondrial destruction on the properties of cell nuclei. J. Biophys. Biochem. Cytol. 1 (1955) 139-153. doi: 10.1083/jcb.1.2.139
81. D. DRAPER & P. VON HIPPEL: Measurements of macromolecule binding constants by a sucrose gradient band. Biochemistry 18 (1979) 753-760. doi: 10.1021/bi00572a003
82. R. DUGGLEBY: Regression analysis of nonlinear ARRHENIUS plots: An empirical model and a computer program. Comput. Biol. Med. 14 (1984) 447-455. doi: 10.1016/0010-4825 (84) 90045-3
83. R. DUGGLEBY: Quantitative analysis of the time courses of enzyme-catalyzed reactions. Methods 24 (2001) 168-174. doi: 10.1006/meth.2001. 1177
84. S. DUNN: Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on western blots by monoclonal antibodies. Anal. Biochem. 157 (1986) 144-153. doi: 10.1016/0003-2697 (86) 90207-1
85. J.-L. EISELÉ & J. ROSENBUSCH: Crystallization of porin using short chain phospholipids. J. Mol. Biol. 206 (1989) 209-212. doi: 10.1016/0022-2836 (89) 90533-0
86. E. ELSON & D. MAGDE: Fluorescence correlation spectroscopy. I. Conceptual basis and theory. Biopolymers 13 (1974) 1-27. doi: 10.1002/bip. 1974.360130102
87. H. ENGELHARDT & J. PLITZKO: 3D-Structuren prokaryotischer organellen. BIOspektrum 12 (2006) 477-478. URL http://www.biospektrum.de/blatt/ dbspdf&id=932616
88. J. F. ENGELHART: Commentatio de vera materiae sanguini purpureum colorem impertientis natura. (Dieterich, Göttingen), 1825
89. E. ENGVALL & P. PERLMAN: Enzyme-linked immunosorbent assay of immunoglobulin G. Immunochemistry 8 (1971) 871-874. doi: 10.1016/0019-2791 (71) 90454-X
90. L. ERIKS, J. MAYOR et al.: A strategy for identification and quantification of detergents frequently used in the purification of membrane proteins. Anal. Biochem. 323 (2003) 234-241. doi: doi:10.1016/j.ab.2003.09.002
91. S. ERIKSSON, I. CARAS et al.: Direct photoaffinity labeling of an allosteric site on subunit protein Ml of mouse ribonucleotide reductase by dTTP. Proc. Natl. Acad. Sci. USA 79 (1982) 81-85. URL http://www.pnas.org/content/79/ 1/81.full.pdf+html
92. L. ESTELA & T. HEINRICHS: Evaluation of the counterimmunoelectrophoretic (CIE) procedure in a clinical laboratory setting. Am. J. Clin. Pathol. 70 (1978) 329-343
93. S. FAHAM & J. BOWIE: Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316 (2002) 1-6. doi: 10.1006/jmbi.2001.5295
94. G. FAIRBANKS, T. STECK et al.: Electrophoretic analysis of themajor polypeptides of the human erythrocyte membrane. Biochemistry 10 (1971) 2606-2617. doi: 10.1021/bi00789a030
95. A. FELINGER: Data analysis and signal processing in chromatography. (Elsevier, Amsterdam), 1998. ISBN 978-0-444-82066-2
96. H. FENTON: Oxidation of tartaric acid in presence of iron. J. Chem. Soc. Trans. 65 (1894) 899-910. doi: 10.1039/CT8946500899
97. K. FERGUSON: Starch gel electrophoresis: application to the classification of pituitary proteins and peptides. Metabolism 13 (1964) 985-1002. URL http://www.his.com/~djt/FergusonKA-Metabolism-October-1964.pdf
98. 2+ reverse staining method for the detection and quantification of proteins in polyacrylamide gels. Anal. Biochem. 213 (1993) 206-212. doi: 10.1006/abio.1993.1410
99. A. FERSHT, A. MATOUSCHEK et al.: Physical-organic molecular biology: Pathway and stability of protein folding. Pure Appl. Chem. 63 (1991) 187-194. URL http://www.iupac.org/publications/pac/1991/pdf/6302x0187.pdf
100. S. FINET, D. VIVARÈS et al.: Controlling biomolecular crystallization by understanding the distinct effects of PEGs and salts on solubility. Methods Enzymol. 368 (2003) 105-129. doi: 10.1016/S0076-6879 (03) 68007-9
101. H. FISCHER, I. POLIKARPOV et al.: Average protein density is a molecular-weight-dependent function. Protein Sci. 13 (2004) 2825-2828. doi:10.1110/ps.04688204
102. N. FITZKEE, P. FLEMMING et al.: Are proteins made from a limited parts list? Trends Biochem. Sci. 30 (2005) 73-80. doi: 10.1016/j.tibs.2004.12.005
103. S. FLEISCHER & M. KERVINA: Subcellular fractionation of rat liver. Methods Enzymol. 31 (1974) 6-41. doi: 10.1016/j.tibs.2004.12.005
104. J. FLOSSDORF & U. SÜSSENBACH: Bestimmung des partiellen spezifischen volumens von gelöst-stoffen in lösungen unbekannter konzentration. Die Makromolekulare Chemie 179 (1978) 1061-1068. doi: 10.1002/macp. 1978.021790420
105. J. FOLCH, M. LEES et al.: A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226 (1957) 497-509. http://www.jbc.org/content/226/1/497.full.pdf+html?sid=1a04415e-c1d6- 406a-ab02-70674cab2d2f
106. P. FREDERIX, T. AKIYAMA et al.: Atomic force bioanalytics. Curr. Opin. Chem. Biol. 7 (2003) 641-647. doi: 10.1016/j.cbpa.2003.08.010
107. T. FöRSTER: Zwischenmolekulare energiewanderung und fluoreszenz. Ann. Phys. 437 (1948) 55-75. doi: 10.1002/andp. 19484370105
108. Y. FUJIKI, A. HUBBARD et al.: Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J. Cell Biol. 93 (1982) 97-102. URL http://jcb.rupress.org/cgi/reprint/93/1/97
109. S. C. GAD (ed.): Handbook of Pharmaceutical Biotechnology. (Wiley Interscience, Hoboken, NJ), 2007. ISBN 978-0471213864
110. Z. GANIM, H. CHUNG et al.: Amide I two-dimensional infrared spectroscopy of proteins. Acc. Chem. Res. 41 (2008) 432-441. doi: 10.1021/ar700188n
111. P. GAST, P. HEMELRIJK et al.: Determination of the number of detergent molecules associated with the reaction center protein isolated from the photosynthetic bacterium Rhodopseudomonas viridis. FEBS Lett. 337 (1994) 39-42. doi: 10.1016/0014-5793 (94) 80625-X
112. A.-C. GAVIN, M. BöSCHE et al.: Functional organisation of the yeast proteome by systematic analysis of protein complexes. Nature 415 (2002) 141-147. doi: 10.1038/415141a
113. A. GEORGE & W. WILSON: Predicting protein crystallization from dilute solution property. Acta Crystallogr. D 50 (1994) 361-365. doi: 10.1107/S0907444994001216
114. R. GILBERT, P. FUCINI et al.: Three-dimensional structures of translating ribosomes by cryo-EM. Mol. Cell 14 (2004) 57-66. doi: 10.1016/S1097-2765 (04) 00163-7
115. S. GILL & P. VON HIPPEL: Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326. doi: 10.1016/0003-2697 (89) 90602-7
116. R. GIVENS, G. TIMBERLAKE et al.: A photoactivated diazopyruvoyl cross-linking agent for bonding tissue containing type-I collagen. Photochem. Photobiol. 78 (2003) 23-29
117. R. GLASER: Biophysics: An Introduction. 5th edn.. (Springer, Berlin), 2000. ISBN 978-3540670889
118. M. GOLDBERG & A. CHAFFOTTE: Undistorted structural analysis of soluble proteins by attenuated total reflectance infrared spectroscopy. Protein Sci. 14 (2005) 2781-2792. doi: 10.1110/ps.051678205
119. L. GOLDSCHMIDT, D. R. COOPER et al.: Toward rational protein crystallization: A Web server for the design of crystallizable protein variants. Protein Sci. 16 (2007) 1569-1576. doi: 10.1110/ps.072914007
120. D. GOOD & J. COON: Advancing proteomics with ion/ion chemistry. Biotechniques 40 (2006) 783-789. doi: 10.2144/000112194
121. V. GOODFELLOW, M. SETTINERI et al.: p-Nitrophenyl 3-diazopyruvate and diazopyruvamides, a new family of photoactivatable cross-linking bioprobes. Biochemistry 28 (1989) 6346-6360. doi: 10.1021/bi00441a030
122. B. GOODSON: Nuclear magnetic resonance of laser-polarised noble gases in molecules, materils and organisms. J. Magn. Reson. 155 (2002) 157-216. doi: 10.1006/jmre.2001.2341
123. S. GORDO & E. GIRALT: Knitting and untying the protein network: Modulation of protein ensembles as a therapeutic strategy. Protein Sci. 18 (2009) 481-493. doi: 10.1002/pro.43
124. P. GRABAR & C. WILLIAMS: Méthode permettant l'étude conjuguée des propriétés électrophorétiques et immunochimiques d'un mélange de protéines. Application au sérum sanguin. Biochim. Biophys. Acta 10 (1953) 193-194. doi: 10.1016/0006-3002 (53) 90233-9
125. K. GRAHAM & J. SHIVELY: Improved initial yields in C-terminal sequence analysis by thiohydantoin chemistry using purified diphenylphosphoryl isothiocyanate: NMR evidence for a reaction intermediate in the coupling reaction. Anal. Biochem. 307 (2002) 202-211. doi: 10.1016/0003-2697 (89) 90602-7
126. M. GREASER & C. WARREN: Efficient electroblotting of very large proteins using a vertical agarose electrophoresis system. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 221-227
127. W. GRECO, G. BRAVO et al.: The search for synergy: A critical review from a response surface perspective. Pharmacol. Rev. 47 (1995) 331-385. URL http://pharmrev.aspetjournals.org/cgi/reprint/47/2/331
128. D. GREENBAUM, C. COLANGELO et al.: Comparing protein abundance and mRNA expression levels on a genomic scale. Genome Biol. 4 (2003) 117. URL http://genomebiology.com/2003/4/9/117
129. W. GRIFFIN: Classification of surface-active agents by "HLB". J. Soc. Cosmet. Chem. 1 (1949) 311
130. W. GRIFFIN: Calculation of HLB values of non-ionic surfactants. J. Soc. Cosmet. Chem. 5 (1954) 249
131. B. GRIFFITH & A. DOYLE: Cell culture: Essential techniques. (J. Wiley & Sons, New York), 1997. doi: 978-0471970576
132. G. GRIMSLEY, J. SCHOLTZ et al.: A summary of the measured pK values of the ionizable groups in folded proteins. Protein Sci. 18 (2009) 247-251. doi: 10.1002/pro.19
133. E. GROSS & B. WITKOP: Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. J. Am. Chem. Soc. 83 (1961) 1510-1511. doi: 10.1021/ja01467a052
134. D. GUTMANN, E. MIZOHATA et al.: A high-throughput method for protein solubility screening: The ultracentrifugation dispersity sedimentation assay. Protein Sci. 16 (2007) 1422-1428. doi: 10.1110/ps.072759907
135. S. GYGI, B. RIST et al.: Quantitative analysis of complex protein mixtures using isotopecoded affinity tags. Nat. Biotechnol. 17 (1999) 994-999. doi: 10.1038/13690
136. S. GYGI, Y. ROCHON et al.: Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol. 19 (1999) 1720-1730. URL http://www.ncbi.nlm.nih.gov/ pmc/articles/PMC83965
137. J. HAJDU: Single molecule X-ray diffraction. Curr. Opin. Struct. Biol. 10 (2000) 569. doi: 10.1016/S0959-440X (00) 00133-0
138. A. VON HALL, M. HAMACHER et al.: 5 Jahre human brain proteom project. BIOspektrum 12 (2006) 727-730. URL http://www.biospektrum.de/blatt/ dbspdf&id=932513
139. O. P. HAMILL, A. MARTY et al.: Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflügers Arch. 1981 (391) 85-100. doi: 10.1007/BF00656997
140. K. HANCOCK & V. TSANG: India ink staining of proteins on nitrocellulose paper. Anal. Biochem. 133 (1983) 157-162. doi: 10.1016/0003-2697 (83) 90237-3
141. Q. HANLEY, K. LIDKE et al.: Fluorescence lifetime imaging in an optically sectioning programmable array microscope (PAM). Cytometry 67 A (2005) 112-118. doi: 10.1002/cyto.a.20177
142. Q. HANLEY, P. MURRAY et al.: Microspectroscopic fluorescence analysis with prism-based imaging spectrometers: Review and current studies. Cytometry 69 A (2006) 759-766. doi: 10.1002/cyto.a.20265
143. K. HANNIG: New aspects in preparative and analytical continuous free-flow cell electrophoresis. Electrophoresis 3 (1982) 235-243. doi: 10.1002/elps.1150030502
144. E. HARDY & L. CASTELLANOS-SERRA: "Reverse-staining" of biomolecules in electrophoresis gels: Analytical and micropreparative applications. Anal. Biochem. 328 (2004) 1-13. doi: 10.1016/j.ab.2004.02.017
145. P. HARE, D. VON ENDT et al.: Protein and amino acid diagenesis dating. In: Chronometric dating in archaeology, R. TAILOR & M. AITKEN, eds., vol. 2 of Adv. archaeology mus. sci. (Springer, New York). ISBN 978-0-306-45715-9, 1997 pp. 261-296
146. E. HARLOW & D. LANE: Antibodies - A Laboratory Manual. 1 edn.. (Cold Spring Harbor Laboratory, Cold Spring Harbor), 1988. ISBN 978-0879694145
147. H. HARTRIDGE & F. ROUGHTON: A method of measuring the velocity of very rapid chemical reactions. Proc. R. Soc. Lond. A 104 (1923) 376-394. doi: 10.1098/rspa.1923.0116
148. L. HAYFLICK & P. S. MOORHEAD: The serial cultivation of human diploid cell strains. Exp. Cell Res. 25 (1961) 585-621. doi: 10.1016/0014-4827 (61) 90192-6
149. J. HEDRICK & A. SMITH: Size and charge isomer separation and estimation of molecular weights of protein by disk gel electrophoresis. Arch. Biochem. Biophys. 126 (1968) 155-64. doi: 10.1016/0003-9861 (68) 90569-9
150. H. HEERKLOTZ & J. SEELIG: Correlation of membrane/water partition coefficients of detergents with the cmc. Biophys. J. 78 (2000) 2435-2440. doi: 10.1016/S0006-3495 (00) 76787-7
151. M. HEGRENESS, N. SHORESH et al.: Accelerated evolution of resistance in multidrug environments. Proc. Natl. Acad. Sci. USA 105 (2008) 13 977-13 981. doi: 10.1073/pnas.0805965105
152. A. HELENIUS & K. SIMONS: Solubilization of membranes by detergents. Biochim. Biophys. Acta 415 (1975) 29-79. doi: 10.1016/0304-4157 (75) 90016-7
153. P. HELFMAN & J. BADA: Aspartic acid racemization in tooth enamel from living humans. Proc. Natl. Acad. Sci. USA 72 (1975) 2891-2894. URL http://www.pnas.org/content/72/8/2891.full.pdf
154. S. HELL & J. WICHMANN: Breaking the diffraction resolution limit by stimulated emission: Stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 19 (1994) 780-782. doi: 10.1364/OL.19.000780
155. R. HENDERSON, J. BALDWIN et al.: Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 899-929. doi: 10.1016/S0022-2836 (05) 80271-2
156. P. HENGEN: Chemoluminescent detection methods. Trends Biochem. Sci. 22 (1997) 313-314. doi:10.1016/S0968-0004 (97) 01095-5
157. A. HENKEL & S. BIEGER: Quantification of proteins dissolved in an electrophoresis sample buffer. Anal. Biochem. 223 (1995) 329-331. doi: 10.1006/abio.1994.1595
158. S. HENNING, J. PETER-KATALINIC et al.: Structure analysis of N-glycoproteins. In: Mass Spectrometry of Proteins and Peptides, L. PAŠA-TOLIC & M. LIPTON, eds., vol. 492 of Methods Mol. Biol., 2nd edn., pp. 181-200. (Humana, Dordrecht). ISBN 978-1-934115-48-0, 2009 doi: 10.1007/978-1-59745-493-3
159. G. HERMANSON: Bioconjugate techniques. 2nd edn.. (Academic, Amsterdam), 2008. ISBN 978-0-12-370501-3
160. J. HEUKESHOVEN & R. DERNICK: Improved silver staining procedure for fast staining in phastsystem development unit I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9 (1988) 28-32. doi: 10.1002/elps.1150090106
161. A. HINCHLIFFE: Molecular modelling for beginners. 2nd edn.. (Wiley, Chichester), 2008. ISBN 978-0470513149
162. T. HISABORI, K. INOUE et al.: Two-dimensional gel electrophoresis of membrane-bound protein complexes, including photosystem I, of tylacoid membranes in the presence of sodium oligooxyethylene alkyl ether sulfate/dimethyl dodecylamine oxide and sodium dodecyl sulfate. J. Biochem. Biophys. Methods 22 (1991) 253-260. doi: 10.1016/0165-022X (91) 90073-6
163. L. HJELMELAND & A. CHRAMBACH: Formation of natural pH gradients in sequential moving boundary systems with solvent counterions I. Theory. Electrophoresis 4 (83) 20-26. doi: 10.1002/elps.1150040104
164. S. HJERTÉN, L. ÖFVERSTEDT et al.: Free displacement electrophoresis (isotachophoresis): An absolute determination of the KOHLRAUSCHfunctions and their use in interaction studies. J. Chromatogr. A 194 (1980) 1-10. doi: 10.1016/S0021-9673 (00) 81044-4
165. H.-D. HöLTJE, W. SIPPL et al.: Molecular Modeling: Basic Principles and Applications. 3rd edn.. (Wiley, Weinheim), 2008. ISBN 978-3527315680
166. F. HOFMEISTER: Zur lehre der wirkung von salzen. Arch. Exp. Pathol. Pharmakol. 24 (1888) 247-260. doi: 10.1007/BF01838161
167. K. VAN HOLDE, W. JOHNSON et al.: Principles of physical biochemistry. 2 edn.. (Pearson, Upper Saddle River, NJ), 2006. ISBN 0-13-046427-9
168. P. HOLLOWAY: A simple procedure for the removal of Triton-X100 from protein samples. Anal. Biochem. 53 (1973) 304-308. doi: 10.1016/0003-2697 (73) 90436-3
169. F. HOPPE-SEYLER & K. BUTZ: Peptide aptamers: Powerful new tools for molecular medicine. J. Mol. Med. 78 (2000) 426-430. doi: 10.1007/s0010900000140
170. C. HUANG: Determination of the binding stoichiometry by the continuous variation method: The JOB-plot. Methods Enzymol. 87 (1982) 509-525. doi: 10.1016/S0076-6879 (82) 87029-8
171. W. HUEMOELLER & H. TIEN: A simple setup for black lipid membrane experiments. J. Chem. Educ. 47 (1970) 469-470. doi: 10.1021/ed047p469
172. P. HUGHES, D. MARSHALL et al.: The costs of using unauthenticated, over-passaged cell lines: how much more data do we need? Biotechniques 43 (2007) 575-586. doi: 10.2144/000112598
173. J. HUMMEL & W. DREYER: Measurment of protein-binding phenomena by gel filtration. Biochim. Biophys. Acta 63 (1962) 530-532. doi: 10.1016/0006-3002 (62) 90124-5
174. S. JACKSON: How do small single-domain proteins fold? Fold Des 3 (1998) R81-R91. doi: doi:10.1016/S1359-0278 (98) 00033-9
175. N. JAIN & I. ROY: Effect of trehalose on protein structure. Protein Sci. 18 (2009) 24-36. doi: 10.1002/pro.3
176. P. JOB: Recherches sur la formation de complexes minéraux en solution, et sur leur stabilité. Ann. Chim. (Paris) 9 (1928) 113-203
177. J. JOHNSON, R. YOST et al.: Tandem-in-space and tandem-in-time mass spectrometry: triple quadrupoles and quadrupole ion traps. Anal. Chem. 62 (1990) (20) 2162-2172. doi: 10.1021/ac00219a003
178. S. JOHNSON & A. BANGHAM: Potassium permeability of single compartment liposomes with and without valinomycin. Biochim. Biophys. Acta 193 (1969) 82-91. doi: 10.1016/0005-2736 (69) 90061-3
179. G. JONES & M. DOLE: The viscosity of aqueous solutions of strong electrolytes with special reference to barium chloride. J. Am. Chem. Soc. 51 (1929) 2950-2964. doi: 10.1021/ja01385a012
180. N. JONES & P. PEVZNER: An introduction to bioinformatics algorithms. (MIT, Cambridge, London), 2004. ISBN 978-0-262-10106-6
181. J. JØRGENSEN & K. LUKACS: Zone electrophoresis in open-tubular glass capillaries. Anal. Chem. 53 (1981) 1298-1302. doi: 10.1021/ac00231a037
182. T. JOVIN: Multiphasic zone electrophoresis. I. Steady-state moving-boundary systems formed by different electrolyte combinations. Biochemistry 12 (1973) 871-879. doi: 10.1021/bi00729a014
183. T. JOVIN: Multiphasic zone electrophoresis. II. Design of integrated discontinuous buffer systems for analytical and preparative fractionation. Biochemistry 12 (1973) 879-890. doi: 10.1021/bi00729a015
184. T. JOVIN: Multiphasic zone electrophoresis. III. Further analysis and new forms of discontinuous buffer systems. Biochemistry 12 (1973) 890-898. doi:10.1021/bi00729a016
185. T. JOVIN: Multiphasic zone electrophoresis. IV Design and analysis of discontinuous buffer systems with a digital computer. Ann. NY Acad. Sci. 209 (1973) 477-496. doi: 10.1111/j.1749-6632.1973.tb47551.x
186. J. KALINICH & D. MCCLAIN: An in vitro method for radiolabeling proteins with 35S. Anal. Biochem. 205 (1992) 208-212. doi: 10.1016/0003-2697 (92) 90425-7
187. E. KALTSCHMIDT & H. G. WITTMANN: Ribosomal proteins. VII: Two-dimensional polyacrylamide gel electrophoresis for fingerprinting of ribosomal proteins. Anal. Biochem. 36 (1970) 401-412. doi: 10.1016/0003-2697 (70) 90376-3
188. A. KAPANIDIS, N. LEE et al.: Fluorescence-aided molecule sorting: Analysis of structure and interactions by alternating-laser excitation of single molecules. Proc. Natl. Acad. Sci. USA 101 (2004) 8936-8941. doi: 10.1073pnas.0401690101
189. K. KARLSSON, B. SAMUELSSON et al.: The lipid composition of the salt (rectal) gland of spiny dogfish. Biochim. Biophys. Acta 337 (1974) 365-376. doi: 10.1016/0005-2760 (74) 90111-8
190. V. KASCHE & R. ZöLLNER: Tris (hydroxymethyl) methylamine is acylated when it reacts with acyl-chymotrypsin. Hoppe Seylers Z. physiol. Chem. 363 (1982) 531-534
191. S. VAN KASTERENA, S. CAMPBELLB et al.: Glyconanoparticles allow pre-symptomatic in vivo imaging of brain disease. Proc. Natl. Acad. Sci. USA 106 (2009) 18-23. doi: 10.1073/pnas.0806787106
192. A. KATDARE & M. CHAUBAL (eds.): Excipient Development for Pharmaceutical, Biotechnology, and Drug Delivery Systems. (Informa HealthCare), 2006. ISBN 978-0849327063
193. S. KELLY, T. JESS et al.: How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751 (2005) 119-139. doi: 10.1016/j.bbapap. 2005.06.005
194. T. KERPPOLA: Visualization of molecular interactions by fluorescence complementation. Nature Rev. Mol. Cell Biol. 7 (2006) 449-456. doi: 10.1038/nrm1929
195. F. KIENBERGER, G. KADA et al.: Single molecule studies of antibody-antigen interaction strength versus intra-molecular antigen stability. J. Mol. Biol. 347 (2005) 597-606. doi: 10.1016/j.jmb.2005.01.042
196. H. KIM, D. BYRNE et al.: Perceiving mitosis in eukaryotic cells. In Vitro Cell. Dev. Biol. Plant 24 (1988) 100-107. doi: 10.1007/BF02623886
197. M.-S. KIM, J. SONG et al.: Determining protein stability in cell lysates by pulse proteolysis and western blotting. Protein Sci. 18 (2009) 1051-1059. doi: 10.1002/pro.115
198. M. KIMBER et al.: Data mining crystallization data bases: Knowledge-based approaches to optimize protein crystal screens. Proteins 51 (2003) 562-568. URL http://papers.gersteinlab.org/e-print/xtalmine/reprint.pdf
199. M. KINTER & N. SHERMAN: Protein sequencing and identification using tandem mass spectrometry. (Wiley Interscience, New York), 2000. ISBN 978-0471322498
200. M. KLAPPER & I. KLOTZ: Acylation with dicarboxylic acid anhydrides. Methods Enzymol. 25 (1972) 531-552. doi: 10.1016/S0076-6879 (72) 25050-9
201. B. KLEINE, G. LöFFLER et al.: Reduced chemical and radioactive liquid waste during electrophoresis using polymerized electrode gels. Electrophoresis 13 (1992) 73-75. doi: 10.1002/elps.1150130114
202. J. KLOSE & U. KOBALZ: Two-dimensional electrophoresis of proteins: An updated protocoll and implications for functional analysis of genomes. Electrophoresis 16 (1995) 1034-1059. doi: 10.1002/elps.11501601175
203. F. KOHLRAUSCH: Über concentrations-verschiebungen durch electrolyse im inneren von lösungen und lösungsgemischen. Ann. Phys. Chem. 62 (1897) 209-239. doi: 10.1002/andp. 18972981002
204. J. KOHN: A cellulose acetate supporting medium for zone electrophoresis. Clin. Chim. Acta 2 (1957) 297-303. doi: 10.1016/0009-8981 (57) 90005-0
205. B. KOLAKOWSKI & L. KONERMANN: From small-molecule reactions to protein folding: Studying biochemical kinetics by stopped-flow electrospray mass spectrometry. Anal. Biochem. 292 (2001) 107-114. doi: 10.1006/abio.2001.5062
206. A. KOLLER, M. WASHBURN et al.: Proteomic survey of metabolic pathways in rice. Proc. Natl. Acad. Sci. USA 99 (2002) (18) 11 969-11 974. doi: 10.1073/pnas.172183199. URL http://www.pnas.org/content/99/18/11969.full. pdf+html
207. J. KOST: Blotting from phastgel to membranes by ultrasound. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 173-179
208. M. KOSZELAK-ROSENBLUM, A. KROL et al.: Determination and application of empirically derived detergent phase boundaries to effectively crystallize membrane proteins. Protein Sci. 18 (2009) 1828-1839. doi: 10.1002/pro183
209. U. KRAGH-HANSEN, M. LE MAIRE et al.: The mechanism of detergent solubilization of liposomes and protein containing membranes. Biophys. J. 75 (1998) 2932-2946. doi: 10.1016/S0006-3495 (98) 77735-5
210. S. KRAJEWSKI, J. ZAPATA et al.: Detection of multiple antigens on western blots. Anal. Biochem. 236 (1996) 221-228. doi: 10.1006/abio.1996.0160
211. O. KRATKY, H. LEOPOLD et al.: The determination of the partial specific volume by the mechanical oscillator technique. Methods Enzymol. 27 (1973) 98-110. doi: 10.1016/S0006-3495 (98) 77735-5
212. E. KREYSZIG: Statistische Methoden und ihre Anwendungen. 7th edn.. (Vandenhoeck & Ruprecht, Göttingen), 1979. ISBN 978-3-525-40717-2
213. A. KROGH, B. LARSSON et al.: Predicting transmembrane protein topology with a hidden MARKOW model: Application to complete genomes. J. Mol. Biol. 305 (2001) 567-580. doi: 10.1006/jmbi.2000.4315
214. J. KUIPER, R. PLUTA et al.: A method for site-specific labelling of multiple protein thiols. Protein Sci. 18 (2009) 1033-1041. doi: 10.1002/pro.113
215. B. KURIEN & R. SCOFIELD: Non-electrophoretic bi-directional transfer of a single SDSPAGE gel with multiple antigens to obtain 12 immunoblots. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 55-65
216. K. KURIHARA & K. SUZUKI: Theoretical undestanding of an absorption-based surface plasmon resonance sensor based on KRETSCHMANNS theory. Anal. Chem. 74 (2002) 696-701. doi: 10.1021/ac010820+
217. J. KYTE & R. DOOLITTLE: A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105. doi: 10.1016/0022-2836 (82) 90515-0
218. U. LAEMLI: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685. doi: 10.1038/227680a0
219. J. LAKOWICZ: Principles of fluorescence spectroscopy. 3rd edn.. (Kluwer, New York), 2006. ISBN 978-0387312781
220. A. LAMANDA, A. ZAHN et al.: Improved ruthenium (II) tris (bathophenantroline disulfonate) staining and destaining protocol for a better signal-to-background ratio and improved baseline resolution. Proteomics 4 (2004) 599-608. doi: 10.1002/pmic.200300587
221. J. LANDRY & S. DELHAYE: A simple and rapid procedure for hydrolyzing minute amounts of proteins with alkali. Anal. Biochem. 243 (1996) 191-194. doi: 10.1006/abio.1996.0503
222. T. LAUE, A. HAZARD et al.: Direct determination of macromolecular charge by equilibrium electrophoresis. Anal. Biochem. 182 (1989) 377-382. doi: 10.1016/0003-2697 (89) 90611-8
223. R. LAUGHLIN: The Aqueous Phase Behavior of Surfactants. 2nd edn.. (Elsevier, Amsterdam), 1996. ISBN 9780124377608
224. C. LAURELL: Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal. Biochem. 15 (1966) 45-52. doi:10.1016/0003-2697 (66) 90246-6
225. M. LAURIERE: A semidry electroblotting system efficiently transfers both high- and lowmolecularweight proteins separated by SDS-PAGE. Anal. Biochem. 212 (1993) 206-211. doi: 10.1006/abio.1993.1313
226. J. LAZAR & F. TAUB: A highly sensitive method for detecting peroxidase in situ hybridization or immunohistochemical assays. In: Non-radioactive labeling and detection of biomolecules, C. KESSLER, ed., pp. 135-142. (Springer, Berlin), 1992
227. H. LÜDI & W. HASSELBACH: Excimer formation of ATPase from sarcoplasmic reticulum labeled with N-(3-pyrene) maleimide. Eur. J. Biochem. 130 (1983) 5-8. doi: 10.1111/j.1432-1033.1983.tb07108.x
228. A. LEACH: Molecular Modelling: Principles and Applications. 2nd edn.. (Prentice Hall, New York), 2001. ISBN 978-0582382107
229. J. LEBOWITZ, M. LEWIS et al.: Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci. 11 (2002) 2067-2079. doi: 10.1110/ps.0207702
230. S. LEE, J. STEVENS et al.: A liquid gelatin blocking reagent for western blotting with chemiluminescent detection. Biotechniques 17 (1994) 60-62
231. P. LEMEY, M. SALEMI et al.: The Phylogenetics Handbook: A Practical Approach to DNA and Protein Phylogeny. 2nd edn.. (Cambridge University Press, Cambridge), 2009. ISBN 978-0521730716
232. S. LEVEY & E. JENNINGS: The use of control charts in the clinical laboratory. Am. J. Clin. Pathol. 20 (1950) 1059-1066. doi: 10.1016/0009-8981 (60) 90150-9
233. H. LEVY, P. LEBER et al.: Inactivation of myosin by 2, 4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds. J. Biol. Chem. 238 (1963) 3654-3659. URL http://www.jbc.org/cgi/reprint/238/11/3654.pdf
234. L. LEWIS, M. ROBSON et al.: Interference with spectrophotometric analysis of nucleic acids and proteins by leaching of chemicals from plastic tubes. Biotechniques 48 (2010) 297-302. doi: 10.2144/000113387
235. T. LIEBERMANN & W. KNOLL: Surface-plasmon field-enhanced fluorescence spectroscopy. Colloids Surf A 171 (2000) 115-130. doi: 10.1016/S0927-7757 (99) 00550-6
236. H. LINDLEY: A new synthetic substrate for trypsin and its application to the determination of the amino-acid sequence of proteins. Nature 178 (1956) 647-648. doi: 10.1038/178647a0
237. A. LINK, J. ENG et al.: Direct analysis of protein complexes using mass spectrometry. Nat. Biotechnol. 17 (1999) (7) 676-682. doi: 10.1038/10890. URL http://www.worldinfocus.net/Papers/Proteomics/mudpit.pdf
238. T. LIU, E. DIEMANN et al.: Self-assembly in aqueous solution of wheel-shaped Mo154 oxide clusters into vesicles. Nature 426 (2003) 59-62. doi: 10.1038/nature02036
239. P. LOLL, M. ALLAMAN et al.: Assessing the role of detergent-detergent interactions in membrane protein crystallization. J. Cryst. Growth 232 (2001) 432-438. doi: 10.1016/S0022-0248 (01) 01076-4
240. A. LOMANT & G. FAIRBANKS: Chemical probes of extended biological structures: Synthesis and properties of the cleavable protein cross-linking reagent 35S-dithiobis (succinimidyl propionate). J. Mol. Biol. 104 (1976) 243-261. doi: 10.1016/0022-2836 (76) 90011-5
241. J. LOO: Studying non-covalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16 (1997) 1-23. doi: 10.1002/(SICI) 1098-2787 (1997) 16:1<1::AID-MAS1>3.0. CO;2-L
242. M. LOPEZ, W. PATTON et al.: Effect of various detergents on protein migration in the second dimension of two-dimensional gels. Anal. Biochem. 199 (1991) (1) 35-44. doi: 10.1016/0003-2697 (91) 90266-V
243. O. LOWRY, N. ROSEBROUGH et al.: Protein measurement with the FOLIN phenol reagent. J. Biol. Chem. 193 (1951) 265-275. URL http://www.jbc.org/content/193/ 1/265.full.pdf+html
244. C. LÓPEZ, M. FLEISSNER et al.: Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Sci. 18 (2009) 1637-1652. doi: 10.1002/pro180
245. P. LU, C. VOGEL et al.: Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat. Biotechnol. 25 (2006) 117-124. doi: doi:10.1038/nbt1270
246. G. LUBEC, M. WENINGER et al.: Racemization and oxidation studies of hair protein in the Homo tirolensis. FASEB J. 8 (1994) (14) 1166-1169. URL http://www.fasebj.org/cgi/reprint/8/14/1166.pdf
247. M. LUCKEY: Membrane Structural Biology: With Biochemical and Biophysical Foundations. (Cambridge University Press, Cambridge; New York), 2008. ISBN 9780521856553
248. R. LUNDBLAD & C. NOYES: Chemical reagents for protein modification. 3rd edn.. (CRC, Boca Raton), 2005. ISBN 0-8493-1983-8
249. M. LUNDER, T. BRATKOVIC et al.: Ultrasound in phage display: A new approach to nonspecific elution. Biotechniques 44 (2008) 893-900. doi: 10.2144/000112759
250. A. LUSTIG, A. ENGEL et al.: Molecular weight determination of membrane proteins by sedimentation equilibrium at the sucrose or nycodenz-adjusted density of the hydrated detergent micelle. Biochim. Biophys. Acta 1464 (2000) 199-206. doi: 10.1016/S0005-2736 (99) 00254-0
251. G. MACBATH: Protein microarrays and proteomics. Nat. Genet. Suppl. 32 (2002) 526-532. doi: 10.1038/ng1037
252. D. MAGDE & E. ELSON: Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 13 (1974) 29-61. doi: 10.1002/bip. 1974.360130103
253. M. LE MAIRE, P. CHAMPEIL et al.: Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta 1508 (2000) 86-111. doi: 10.1016/S0304-4157 (00) 00010-1
254. M. LE MAIRE, J. MØLLER et al.: Protein-protein contacts in solubilized membrane proteins, as detected by cross-linking. Anal. Biochem. 362 (2007) 168-171. doi: 10.1016/j.ab.2006.11.025
255. K. MANDAL, B. PENTELUTE et al.: Racemic crystallography of synthetic protein enantiomeres used to determine the X-ray structure of plectasin by direct methods. Protein Sci. 18 (2009) 1146-1154. doi: 10.1002/pro.127
256. M. MANNING: Use of infrared spectroscopy to monitor protein structure and stability. Expert Rev. Proteomics 2 (2005) (5) 731-743. doi:10.1586/14789450.2. 5.731
257. J. MARGOLIS & K. KENRICK: Polyacrylamide gel electrophoresis in a continuous molecular sieve gradient. Anal. Biochem. 25 (1968) 347-362. doi: 10.1016/0003-2697 (68) 90109-7
258. R. MARTIN & B. AMES: A method for determining the sedimentation behaviour of enzymes: Applicaton to protein mixtures. J. Biol. Chem. 236 (1961) 1372-1379. http://www.jbc.org/content/236/5/1372.full.pdf+html?sid=49a396bd- 5a66-45a8-b0fd-cdae82b24c59
259. A. MARTONOSI (ed.): The enzymes of biological membranes, vol. 3. (Plenum, New York, London), 1985. ISBN 978-0306414534
260. J. MATHER & P. ROBERTS: Introduction to cell and tissue cultrure: Theory and techniques. (Plenum, New York), 1998. ISBN 978-0306458590
261. A. MATOUSCHEK & A. FERSHT: Protein engineering in analysis of protein folding pathways and stability. Methods Enzymol. 202 (1991) 82-112. doi: 10.1016/0076-6879 (91) 02008-W
262. P. MATSUDAIRA: Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262 (1987) 10 035-10 038. URL http://www.jbc.org/cgi/reprint/262/21/10035.pdf
263. K. MATSUO, Y. MATSUSHIMA et al.: Vacuum-ultraviolet circular dichroism of amino acids as revealed by synchrotron radiation spectrophotometer. Chem. Lett. 31 (2002) 826-827. http://home.hiroshima-u.ac.jp/x070010/HiSOR-HSRC-BL15.files/ VUVCD%20amino%20acids.pdf
264. T. MATSUYA, N. HOSHINO et al.: Design of lanthanide complex probes for highly sensitive time-resolved fluorometric detection methods and its application to biochemical, environmental and clinical analyses. Curr. Anal. Chem. 2 (2006) 397-410. doi: 10.2174/157341106778520526
265. C. MATTHEWS: Effect of point mutations on the folding of globular proteins. Methods Enzymol. 154 (1987) 498-511. doi: 10.1016/0076-6879 (87) 54092-7
266. G. MAYER, B. LUDWIG et al.: Studying membrane proteins in detergent solution by analytical ultracentrifugation: Different methods for density matching. Prog. Colloid Polym. Sci. 113 (1999) 176-181. doi: 10.1007/3-540-48703-4 25
267. C. MCCUDDEN & V. KRAUS: Biochemistry of amino acid racemization and clinical application to musculoskeletal disease. Clin. Biochem. 39 (2006) 1112-1130. doi: 10.1016/j.clinbiochem.2006.07.009
268. L. MCINTOSH, G. HAND et al.: The pKaof the general acid/base carboxyl group of a glycosidase cycles during catalysis: A 13C-NMR study of bacillus circulans xylanase. Biochemistry 35 (1996) 9958-9966. doi: 10.1021/bi9613234. URL http://startrek.ccs.yorku.ca/~pjohnson/publications/bio03.pdf
269. A. MCPHERSON: Crystallization of biological macromolecules. (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY), 1999. ISBN 978-0879695279
270. W. MELCHIOR & D. FAHRNEY: Ethoxyformylation of proteins. Biochemistry 9 (1970) 251-258. doi: 10.1021/bi00804a010
271. T. MENGUY, S. CHENEVOIS et al.: Ligand binding to macromolecules or micelles: Use of centrifugal ultrafiltration to measure low-affinity binding. Anal. Biochem. 264 (1998) 141-148. doi: 10.1006/abio.1998.2854
272. C. MERRIL, D. GOLDMAN et al.: Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins. Science 211 (1981) 1437-1438. doi: 10.1126/science.6162199
273. M. MESELSON & W. STAHL: The replication of DNA in Escherischia coli. Proc. Natl. Acad. Sci. USA 44 (1958) 671-682. URL http://www.pnas.org/content/ 44/7/671.full.pdf+html
274. X. MICHALET, F. PINAUD et al.: Quantum dots for live cells, in vivo imaging and diagnostics. Science 307 (2005) 538-544. doi: 10.1126/science. 1104274
275. M. DE MICHELIS & R. SPANSWICK: HC-pumping driven by the vanadate-sensitive ATPase in membrane vesicles from corn root. Plant Physiol. 81 (1986) 542-547. URL http://www.plantphysiol.org/cgi/reprint/81/2/542
276. G. A. MILLICAN: Photoelectric methods of measuring the velocity of rapid reactions. III. A portable micro-apparatus applicable to an extended range of reactions. Proc. R. Soc. Lond. A 155 (1936) 277-292. doi: 10.1098/rspa.1936.0099
277. I. MILLS, T. CVITA et al.: Quantities, units and symbols in physical chemistry. 2nd edn.. (Blackwell, Oxford), 1993. ISBN 0-632-03583-8. http://old.iupac.org/publications/books/gbook/index.html
278. L. MITIC, V. UNGER et al.: Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Protein Sci. 12 (2003) 217-218. doi: 10.1110/ps.0233903
279. M. MIYAGI & K. C. S. RAO: Proteolytic 18O-labeling strategies for quantitative proteomics. Mass Spectrom. Rev. 26 (2007) 121-136. doi: 10.1002/mas.20116
280. B. MÜLLER, E. ZAYCHIKOV et al.: Pulsed interleaved excitation. Biophys J. 89 (2005) 3508-3522. doi: 10.1529/biophysj.105.064766
281. K. MONKOS: Concentration and temperature dependence of viscosity in lysozyme aqueous solution. Biochim. Biophs. Acta 1339 (1997) 304-310. doi: 10.1016/S0167-4838 (97) 00013-7
282. M. MONTAL & P. MUELLER: Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc Natl. Acad. Sci. USA 69 (1972) 3561-3566. http://www.pnas.org/content/69/12/3561.full.pdf
283. N. MORGNER, H.-D. BARTH et al.: A new way to detect noncovalently bonded complexes of biomolecules from liquid micro-droplets by laser mass spectrometry. Aust. J. Chem. 59 (2006) 109-114. doi: 10.1071/CH05285
284. K. MOSBACH: Separation of isozymes. Methods Enzymol. 34 (1974) 595-598. doi: 10.1016/S0076-6879 (74) 34079-7
285. P. MUELLER, D. RUDIN et al.: Reconstitution of cell membrane structure in vitro and its transformation into an excitable system. Nature 194 (1962) 979-980. doi: 10.1038/194979a0
286. th edition from 1968, the last one edited by ROMEIS, is an encyclopedic laboratory handbook.)
287. E. MULLER & T. DAVIS: Protein localization by cell imaging. In: Proteomics for biological discovery, T. VEENSTRA & J. Y. III, eds.. (Wiley, Hoboken, NJ). ISBN 978-0-471-16005-2, 2006 pp. 137-155
288. S. MUYLDERMANS, C. CAMBILLAU et al.: Recognition of antigens by single-domain antibody fragments: The superfluous luxury of paired domains. Trends Biochem. Sci. 26 (2001) 230-235. doi: 10.1016/S0968-0004 (01) 01790-X
289. L. NANNINGA & W. MOMMAERTS: Studies on the formation of an enzyme-substrate complex between myosin and adenosinetriphosphate. Proc. Natl. Acad. Sci. USA 46 (1960) (8) 1155. http://www.ncbi.nlm.nih.gov/pmc/articles/ PMC223016/pdf/pnas00207-0149.pdf
290. A. VON NEUHOFF: Die kolloidale coomassie-blau-färbung von proteinen und peptiden in polyacrylamid-gelen: Schnell, untergrundfrei und mit nanogramm-empfindlichkeit. Biol. Chem. Hoppe Seyler 371 (1990) 10-11
291. S. NEWSTEAD, S. FERRANDON et al.: Rationalizing '-helical membrane protein crystallization. Protein Sci. 17 (2008) 466-472. doi: 10.1110/ps.073263108
292. N. NIRMALAN, P. HARNDEN et al.: Mining the archival formalin-fixed paraffin embedded tisue proteome: Opportuniuties and challenges. Mol. Biosyst 4 (2008) 712-720. doi: 10.1039/b800098k
293. T. NISHIBU, K. HIRAYASU et al.: Quantitative filtration-blotting of protein in the presence of sodium dodecyl sulfate and its use for protein assay. Anal. Biochem. 319 (2003) 88-95. doi: 10.1016/S0003-2697 (03) 00255-0
294. H. NISHIZAWA, N. KITA et al.: Determination of molecular weights of native proteins by polyacrylamide gradient gel electrophoresis. Electrophoresis 9 (1989) 803-806. doi: 10.1002/elps.1150091203
295. M. ÜNLÜ, M. MORGAN et al.: Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18 (1997) 2071-2077. doi: 10.1002/elps.1150181133
296. U. NUBER (ed.): DNA Microarrays. (Taylor & Francis, New York), 2005. ISBN 978-0415358668
297. P. O'FARRELL, H. GOODMAN et al.: High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12 (1977) 1133-1142. doi: 10.1016/0092-8674 (77) 90176-3
298. G. OGG: A Practical Guide to Quality Management in Clinical Trial Research. (Informa HealthCare, Boca Raton), 2005. ISBN 978-0849397226
299. K. OIWA, J. ECCLESTON et al.: Comparative single-molecule and ensemble myosin enzymology: Sulfoindocyanine ATP and ADP derivatives. Biophys. J. 78 (2000) 3048-3071. doi: 10.1016/S0006-3495 (00) 76843-3
300. I. OLSEN & H. WIKER: Diffusion blotting for rapid production of multiple identical imprints from sodium dodecylsulfate polyacrylamide gel electrophoresis on a solid support. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 35-38
301. S. OPELLA & F. MARASSI: Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104 (2004) 3587-3606. doi: 10.1021/cr0304121
302. V. ORLANDO, H. STRUTT et al.: Analysis of chromatin structure by in vivo formaldehyde cross-linking. Methods 11 (1997) 205-214. doi: 10.1006/meth.1996. 0407
303. L. ORNSTEIN: Disk electrophoresis: I. Background and theory. Ann. N. Y. Acad. Sci. 121 (1962) 321-351. doi: 10.1111/j.1749-6632.1964.tb14207.x
304. B. ORSI & K. TIPTON: Kinetic analysis of progress curves. Methods Enzymol. 63 (1979) 159-183. doi: 10.1016/0076-6879 (79) 63010-0
305. J. ORTH, I. PREUSS et al.: Pasteurella multocida toxin activation of heterotrimeric Gproteins by deamination. Proc. Natl. Acad. Sci. USA 106 (2009) 7179-7184. doi: 10.1073/pnas.0900160106
306. C. OSTERMEIER, A. HARRENGA et al.: Structure at 2.7 °A resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv fragment. Proc. Natl. Acad. Sci. USA 94 (1997) 10 547-10 553. http://www.pnas.org/content/94/20/10547. full.pdf+html
307. O. OUCHTERLONY: Antigen-antibody reactions in gels. Acta Pathol. Microbiol. Scand. 26 (1949) 507. doi: 10.1111/j.1600-0463.2007.apm 678a.x
308. W. OUTLAW, JR., S. SPRINGER et al.: Histochemical technique: A general method for quantitative enzyme assays of single cell 'extracts' with a time resolution of seconds and a reading precision of femtomoles. Plant Physiol. 77 (1985) 659-666. doi: 10.1104/pp. 77.3.659
309. W. OUTLAW, JR. & S. ZHANG: Single-cell dissection and microdroplet chemistry. J. Exp. Bot. 52 (2001) 605-614. doi: 10.1093/jexbot/52.356.605
310. C. PACE: Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131 (1986) 266-280. doi: 10.1016/0076-6879 (86) 31045-0
311. D. PANTAZATOS, J. KIM et al.: Rapid refinement of crystallographic protein construct, definition employing enhanced hydrogen/deuterium exchange MS. Proc. Natl. Acad. Sci. USA 101 (2004) 751-756. http://www.pnas.org/content/101/ 3/751.full.pdf+html
312. J. PARK, M. MABUCHI et al.: Visualization of unstained protein bands on PVDF. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 527-531
313. M. PARKANY: Quality Assurance and Total Quality Management for Analytical Laboratories. (Royal Society of Chemistry, London), 1993. ISBN 978-0851867052
314. M. PASCHKA & W. HöHNE: A twin-arginine translocation (Tat)-mediated phage display system. Gene 350 (2005) 79-88. doi: 10.1016/j.gene.2005.02.005
315. L. PATTHY & E. L. SMITH: Reversible modification of arginine residues. Application to sequence studies by restriction of tryptic hydrolysis to lysine residues. J. Biol. Chem. 250 (1975) (2) 557-564. http://www.jbc.org/ cgi/reprint/250/2/557.pdf
316. C. PAWELETZ, L. CHARBONNEAU et al.: Reverse phase protein microarrays which capture disease progression show activation of pro-survival pathways at the cancer invasion front. Oncogene 20 (2001) 1981-1989. doi: 10.1038/sj.onc.1204265
317. R. PEARLMAN & Y. WANG: Formulation, characterization, and stability of protein drugs: Case histories. (Springer, New York), 1996. ISBN 978-0306453328
318. M. PEDERSEN, N. SORENSEN et al.: Effect of different hapten-carrier conjugation ratios and molecular orientations on antibody affinity against a peptide antigen. J. Immunol. Methods 311 (2006) 198-206. doi: 10.1016/j.jim.2006.02.008
319. T. PEDERSON: Turning a PAGE: The overnight sensation of SDS-polycrylamide gel electrophoresis. FASEB J. 22 (2008) 949-953. doi: 10.1096/fj.08-0402ufm
320. J. PENG, D. SCHWARTZ et al.: A proteomics approach to understanding protein ubiquitination. Nat. Biotechnol. 21 (2003) 921-926. http://www.fbmc. fcen. uba.ar/~3-2-2005/SEM6JM2007.pdf
321. D. PERKINS, D. PAPPIN et al.: Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567. doi: 10.1002/(SICI) 1522-2683 (19991201) 20:18<3551::AID- ELPS3551>3.0. CO;2-2
322. S. PERKINS: Protein volumes and hydration effects. J. Biochem. 157 (1986) 169-180. doi: 10.1111/j.1432-1033.1986.tb09653.x
323. F. PERRIN: Polarisation de la lumière de fluorecence. Vie moyenne des molécules dans létat excité. J. Phys. Series VI, 7 (1926) 390-401. doi: 10.1051/jphysrad:01926007012039000
324. K. PETERS & G. SNYDER: Time-resolved photoacoustic calorimetry: probing the energetics and dynamics of fast chemical and biochemical reactions. Science 241 (1988) 1053-1057. doi: 10.1126/science.3045967
325. M. PETOUKHOV, N. EADY et al.: Addition of missing loops and domains to protein models by X-ray solution scattering. Biophys. J. 83 (2002) 3113-3125. doi: 10.1016/S0006-3495 (02) 75315-0
326. E. PETRICOIN, A. ARDEKANI et al.: Use of proteomic patterns in serum to identify ovarian cancer. Lancet 359 (2002) 572-577. doi: 10.1016/S0140-6736 (02) 07746-2
327. G. PFENNIG, H. KLEVE-HEBENIUS et al.: Karlsruher nuklidkarte. 7th edn.. (Forschungszentrum Karlsruhe, Karlsruhe), 2006. ISBN 978-3921879184
328. A. PITRE, Y. PAN et al.: On the use of ratio standard curves to accurately quantitate relative changes in protein levels by western blot. Anal. Biochem. 361 (2007) 305-307. doi: 10.1016/j.ab.2006.11.008
329. J. PITTS: Crystallization by centrifugation. Nature 355 (1992) 117. doi: 10.1038/355117a0
330. B. PLAPP: Application of affinity labeling for studying structure and function of enzymes. Methods Enzymol. 87 (1982) 469-499. doi: 10.1016/S0076-6879 (82) 87027-4
331. J. PODUSLO: Glycoprotein molecular-weight estimation using sodium dodecyl sulfate-pore gradient electrophoresis: Comparison of tris-glycine and tris-borate-EDTA buffer systems. Anal. Biochem. 114 (1981) 131-139. doi: 10.1016/0003-2697 (81) 90463-2
332. A. POLLARD & C. HERON: Archaeological Chemistry. 2nd edn.. (RSC, Cambridge, UK), 2008. ISBN 978-0-85404-262-3
333. R. POLLET, B. HAASE et al.: Macromolecular characterization by sedimentation equilibrium in the preparative ultracentrifuge. J. Biol. Chem. 254 (1979) 30-33. http://www.jbc.org/content/254/1/30.full.pdf+html?sid=31e44cff- cf18-49d6-93a4-7d116b4ef52e
334. C. POOLE: Electron spin resonance: A comprehensive treatise on experimental techniques. 2nd edn.. (Wiley, New York), 1983. ISBN 978-0471046783
335. J. PORATH & P. FLODIN: Gel filtration: a method for desalting and group separation. Nature 183 (1959) 1657-1659. doi: 10.1038/1831657a0
336. V. POTTER & C. ELVEHJEM: A modified method for the study of tissue oxidations. J. Biol. Chem. 114 (1936) 495-504. http://www.jbc.org/content/114/2/ 495.full.pdf+html?sid=49ae7180-3734-425c-8084-8372de3a0269
337. W. PRESS, B. FLANNERY et al.: Numerical recipes in Pascal: The art of scientific computing. (Cambridge University Press, Cambridge), 1989. ISBN 978-0521375160
338. T. RABILLOUD, V. GIRARDOT et al.: One- and two-dimensional histone separation in acidic gels: Usefulness of methylene blue-driven photopolymerization. Electrophoresis 17 (1996) 67-73. doi: 10.1002/elps. 1150170112
339. T. RABILLOUD, J.-M. STRUB et al.: A comparison between sypro ruby and ruthenium (II) tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels. Proteomics 1 (2001) 699-704. http://www.uhkt.cz/ files/proteomika/sypro versus ruthenium.pdf
340. M. RADIN: Extraction of tissue lipids with a solvent of low toxicity. Methods Enymol. 72 (1981) 5-7. doi: 10.1016/S0076-6879 (81) 72003-2
341. R. RAGONE, F. FACCHIANO et al.: Flexibility plot of proteins. Protein Eng. 2 (1989) (7) 497-504. doi: 10.1093/protein/2.7.497
342. K. RAINES, S. SALHA et al.: Three-dimensional structure determination from a single view. Nature 463 (2010) 214-217. doi: 10.1038/nature08705
343. T. RATLIFF: The laboratory quality assurance system: A manual of quality procedures and forms. 3rd edn.. (Wiley-Interscience, Hoboken, NJ), 2003. ISBN 978-0471269182
344. H. RATTLE: An NMR Primer for life scientists. (Partnership Press, Fareham (GB)), 1995. ISBN 978-0951643631
345. F. RAUSHEL & J. VILLAFRANCA: Positional isotope exchange. Crit. Rev. Biochem. Mol. Biol. 23 (1988) 1-26. doi: 10.3109/10409238809103118
346. S. RAYMOND & L. WEINTRAUB: Acrylamide gel as a supporting medium for zone electrophoresis. Science 130 (1959) 711. doi: 10.1126/science.130.3377.711
347. J. REIG & D. KLEIN: Submicron quantities of unstained proteins are visualized on polyvinylidene difluoride membranes by transillumination. Appl. Theor. Electrophor. 1 (1988) 59-60
348. C. RETAMAL & J. BABUL: Determination of the molecular weight of proteins by electrophoresis in slab gels with a transverse pore gradient of cross-linked polyacrylamide in the absence of denaturing agents. Anal. Biochem. 175 (1988) 544-547. doi: 10.1016/0003-2697 (88) 90581-7
349. J. REYNOLDS & C. TANFORD: Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding. Proc. Natl. Acad. Sci. USA 73 (1976) 4467-4470. http://www.pnas.org/content/73/12/4467.full.pdf+html
350. G. RHODES: Crystallography made crystal clear. 3rd edn.. (Academic, Amsterdam), 2006. ISBN 978-0-12-587073-3
351. J. RIGAUD: Membrane proteins: Functional and structural studies using reconstituted proteoliposomes and 2-D crystals. Braz. J. Med. Biol. Res. 35 (2002) 753-766. doi: 10.1590/S0100-879X2002000700001. http://www.scielo.br/pdf/ bjmbr/v35n7/4512.pdf
352. J. RIGAUD, M. CHAMI et al.: Use of detergents in two-dimensional crystallization of membrane proteins. Biochim. Biophys. Acta 1508 (2000) 112-128. doi: 10.1016/S0005-2736 (00) 00307-2
353. J.-L. RIGAUD, D. LEVY et al.: Detergent removal by non-polar polystyrene beads. Eur. Biophys. J. 27 (1998) 305-319. doi: 10.1007/s002490050138
354. m of MICHAELIS-MENTEN kinetics curves. J. Theor. Biol. 178 (1996) 239-254. doi: 10.1006/jtbi.1996.0023
355. H. ROGNIAUX, S. SANGLIER et al.: Mass spectrometry as a novel approach to probe cooperativity in multimeric enzymatic systems. Anal. Biochem. 291 (2001) 48-51. doi: 10.1006/abio.2000.4975
356. G. ROUSER & S. FLEISCHER: Isolation, characterisation and determination of polar lipids of mitochondria. Methods Enzymol. 10 (1967) 385-406. doi: 10.1016/0076-6879 (67) 10072-4
357. A. SADRA, T. CINEK et al.: Multiple probing of an immunoblot membrane using a nonblock technique: Advantages in speed and sensitivity. Anal. Biochem. 278 (2000) 235-237. doi: 10.1006/abio.1999.4453
358. Z. SALAMON, H. MACLEOD et al.: Surface plasmon resonance spectroscopy as a tool for investigating the biochemical and biophysical properties of membrane protein systems. I: Theoretical principles. Biochim. Biophys. Acta 1331 (1997) 117-129. doi: 10.1016/S0304-4157 (97) 00004-X
359. Z. SALAMON, H. MACLEOD et al.: Surface plasmon resonance spectroscopy as a tool for investigating the biochemical and biophysical properties of membrane protein systems. II: Application to biological systems. Biochim. Biophys. Acta 1331 (1997) 131-152. doi: 10.1016/S0304-4157 (97) 00003-8
360. J. SAMBROOK & D. RUSSEL: Molecular cloning: A laboratory manual. 3rd edn.. (Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y.), 2001. ISBN 978-0879695774
361. C. SANDERS & R. PROSSER: Bicelles: a model membrane system for all seasons. Structure 6 (1998) 1227-1234. doi: 10.1016/S0969-2126 (98) 00123-3
362. C. SANNY & J. PRICE: Analysis of antibody-antigen interactions using size exclusion high-performance (pressure) chromatography. Anal. Biochem. 246 (1997) 7-14. doi: 10.1006/abio.1996.9995
363. T. SANO, C. SMITH et al.: Immuno-PCR: very sensitive antigen detection by means of specific antibody-DNA conjugates. Science 258 (1992) 120-122. doi: 10.1126/science.1439758
364. M. SARGENT: Fiftyfold amplification of the LOWRY protein assay. Anal. Biochem. 163 (1987) 476-481. doi: 10.1016/0003-2697 (87) 90251-X
365. G. SAUERBREY: Verwendung von schwingquarzen zur wägung dünner schichten und zur mikrowägung. Z. Phys. A Hadrons Nucl. 155 (1959) 206. doi: 10.1007/BF01337937
366. H. SCHÄGGER: Tricine-SDS-PAGE. Nat. Protoc. 1 (2006) 16-22. doi: 10.1038/nprot.2006.4
367. H. SCHÄGGER, W. CRAMER et al.: Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217 (1994) 220-230. doi: 10.1006/abio.1994.1112
368. H. SCHÄGGER & G. VON JAGOW: Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100 kDalton. Anal. Biochem. 166 (1987) 368-379. doi: 10.1016/0003-2697 (87) 90587-2
369. S. SCHRIER, A. ZACHOWSKI et al.: Mechanisms of amphipath-induced stomatocytosis in human erythrocytes. Blood 79 (1992) 782-786. http://bloodjournal.hematologylibrary.org/cgi/reprint/79/3/782.pdf
370. P. SCHUCK: Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and LAMM equation modeling. Biophys. J. 78 (2000) 1606-1619. http://www.pubmedcentral.nih.gov/picrender.fcgi?artid= 1300758&blobtype=pdf
371. E. SCRIVEN (ed.): Azides and nitrenes. (Academic, New York), 1984. ISBN 978-0126334807
372. I. SEGEL: Enzyme Kinetics. (Wiley, New York), 1975, reprinted 1993. ISBN 978-0471303091
373. W. SHEWHART: Economic Control of Quality of Manufactured Product. (D. van Nostrand, New York), 1931. ISBN 0-87389-076-0
374. A. SHIOI, M. HARADA et al.: Protein extraction in a tailored reversed micellar system containing nonionic surfactants. Langmuir 13 (1997) 609-616. doi: 10.1021/la960250m
375. K. SHIRAHAMA, K. TSUJII et al.: Free boundary electrophoresis of sodium dodecyl sulphate-protein polypeptide complexes with special reference to SDS-polyacrylamide gel electrophoresis. J. Biochem. 75 (1974) 309-319
376. G. SIEGEL & T. DESMOND: Effects of tetradecyl sulfate on electrophoretic resolution of kidney Na; K-ATPase catalytic subunit isoforms. J. Biol. Chem. 264 (1989) 4751-4754. http://www.jbc.org/content/264/9/4751.full. pdf
377. K. SIMONS & E. IKONEN: Functional rafts in cell membranes. Nature 387 (1997) 569-572. doi: 10.1038/42408
378. S. SINGER & G. NICOLSON: The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-731. doi: 10.1126/science.175.4023.720
379. A. SIVASHANMUGAM, V. MURRAY et al.: Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci. 18 (2009) 936-948. doi: 10.1002/pro.102
380. G. SMITH: Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface. Science 228 (1985) 1315-1317. doi: 10.1126/science.4001944
381. I. SMITH, R. CROMIE et al.: Seeing gel wells well. Anal. Biochem. 169 (1988) 370-371. doi: 10.1016/0003-2697 (88) 90297-7
382. P. SMITH, R. KROHN et al.: Measurement of protein using bicinchonic acid. Anal. Biochem. 150 (1985) 76-85. doi: 10.1016/0003-2697 (85) 90442-7
383. P. SNEATH & R. SOKAL: The principles and practice of numerical taxonomy. (Freeman, San Francisco), 1973. ISBN 9780716706977
384. A. SOLOVYOVA, P. SCHUCK et al.: Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents. Biophys. J. 81 (2001) 1868-1880. doi: 10.1016/S0006-3495 (01) 75838-9
385. L. SONG & J. GOUAUX: Membrane protein crystallization: Application of sparse matrices to the '-hemolysin heptamer. Methods Enzymol. 276 (1997) 60-74. doi: 10.1016/S0076-6879 (97) 76050-6
386. T. SPANDE, B. WITKOP et al.: Selective cleavage and modification of peptides and proteins. Adv. Protein Chem. 24 (1970) 97-260
387. V. SPASSOV & L. YAN: A fast and accurate computatioal approach for protein ionization. Protein Sci. 17 (2008) 1955-1970. doi: 10.1110/ps.036335.108
388. B. SPENGLER, M. KARAS et al.: Excimer laser desorption mass spectrometry of biomolecules at 248 and 193 nm. J. Phys. Chem. 91 (1987) (26) 6502-6506. doi: 10.1021/j100310a016
389. I. STEINBERG & H. SCHACHMAN: Ultracentrifugation with absoption optics. Analysis of interacting systems involving macromolecules and small molecules. Biochemistry 5 (1966) 3728-3747. doi: 10.1021/bi00876a003
390. N. STELLWAGEN: Apparent pore size of polyacrylamide gels. Electrophoresis 19 (1998) 1542-1547. doi: 10.1002/elps.1150191004
391. A. STENSBALLE, O. JENSEN et al.: Electron capture dissociation of singly and multiply phosphorylated peptides. Rapid Commun. Mass Spectrom. 14 (2000) (19) 1793-1800. http://www.bmms.uu.se/pubs/article003.pdf
392. T. STEPHENS, C. BUNDE et al.: Mechanism of action in thalidomide teratogenesis. Biochem. Pharmacol. 59 (2000) 1489-1499. doi:10.1016/S0006-2952 (99) 00388-3
393. M. SUCHANEK, A. RADZIKOWSKA et al.: Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. Nat. Methods 2 (2005) 261-267. doi: 10.1038/NMETH752
394. I. SUYDAM, C. SNOW et al.: Electric fields at the active site of an enzyme: Direct comparison of experiment with theory. Science 313 (2006) 200-204. doi: 10.1126/science.1127159
395. T. SVEDBERG & K. PEDERSEN: The ultracentrifuge. (Oxford University Press, Oxford), 1940. ISBN 978-0384588905
396. D. SVERGUN: Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886. doi: 10.1016/S0006-3495 (99) 77443-6
397. M. SWANN, L. PEEL et al.: Dual-polarization interferometry: An analytical technique to measure changes in protein structure in real time, to determine the stoichiometry of binding events, and to differentiate between specific and nonspecific interactions. Anal. Biochem. 329 (2004) 190-198. doi: 10.1016/j.ab.2004.02.019
398. G. TAGUCHI: Introduction to quality engineering. (Asian Productivity Organisation UNIPUB, Tokyo), 1986. ISBN 978-9283310846
399. G. TAGUCHI: System of experimental design. (Asian Productivity Organisation UNIPUB/Kraus Intern. Publications, New York), 1987. ISBN 978-0527916213
400. K. TAKAHASHI: The Reaction of Phenylglyoxal with Arginine Residues in Proteins. J. Biol. Chem. 243 (1968) (23) 6171-6179. http://www.jbc.org/cgi/ reprint/243/23/6171.pdf
401. K. TAKAHASHI: Specific Modification of Arginine Residues in Proteins with Ninhydrin. J. Biochem. (Tokyo) 80 (1976) (5) 1173-1176. http://jb. oxfordjournals.org/cgi/content/abstract/80/5/1173
402. K. TAKEO: Affinity electrophoresis: Principles and application. Electrophoresis 5 (1984) 187-195. doi: 10.1002/elps.1150050402
403. T. TAKI, T. GONZALEZ et al.: TLC blot (far-eastern blot) and its applications. In: Protein blotting and detection - Methods and protocols, B. KURIEN & R. SCOFIELD, eds., vol. 536 of Methods Mol. Biol. (Humana, Dordrecht). ISBN 978-1-934115-73-2, 2009 pp. 545-556
404. Z. TAKÁTS, J. WISEMAN et al.: Mass spectrometry sampling under ambient conditions with desorption electrospray ionization. Science 306 (2004) 471-473. doi: 10.1126/science. 1104404
405. H. TAN, T. NG et al.: Effects of light spectrum in flatbed scanner densitometry of stained polyacrylamide gels. Biotechniques 42 (2007) 474-478. doi: 10.2144/000112402
406. K. TANAKA, H. WAKI et al.: Protein and polymer analyses up to m/z 100, 000 by laser ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 2 (1988) (8) 151-153. http://masspec.scripps.edu/mshistory/timeline/ time pdf/1988 Tanaka2.pdf
407. H. TAO, W. LIU et al.: Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS. Biotechniques 48 (2010) 61-64. doi: 10.2144/000113304
408. K. TAWA & K. MORIGAKI: Substrate-supported phospholipid membranes studied by surface plasmon resonance and surface plasmon fluorescence spectroscopy. Biophys. J. 89 (2005) 2750-2758. doi: 10.1529/biophysj.105.065482
409. C. TAYLOR & H. LIPSON: Optical transforms. Their preparation and application to X-ray diffraction problems. (G. Bell and Sons, London), 1964
410. P. TESSIER, A. LENHOFF et al.: Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography. Biophys. J. 82 (2002) 1620-1631. doi: 10.1016/S0006-3495 (02) 75513-6
411. B. THOMSON: Radio frequency quadrupole ion guides in modern mass spectrometry. Can. J. Chem. 76 (1998) 499-505. doi: 10.1139/cjc-76-5-499
412. A. TISELIUS: A new apparatus for analysis of colloidal mixtures. Trans. Faraday Soc. 33 (1937) 524-531. doi: 10.1039/TF9373300524
413. H. TOWBIN, T. STAEHELIN et al.: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354. http://www.pnas.org/content/76/ 9/4350.full.pdf+html
414. D. TRONRUD & B. MATTHEWS: Sorting the chaff from the weat at the PDB. Protein Sci. 18 (2009) 2-5. doi: 10.1002/pro.13
415. R. TSIEN: The green fluorescent protein. Annu. Rev. Biochem. 67 (1998) 509-544. doi: 10.1146/annurev. biochem.67.1.509
416. C. TSOU: Relation between modification of functional groups of proteins and their biological activity. I. A graphical method for the determination of the number and type of essential groups. Sci. Sin. 11 (1962) 1535-1558. http://en. cnki.com.cn/Article en/CJFDTOTAL-SHWL196203006.htm
417. E. VALERO & F. GARCÍA-CARMONA: Optimizing enzymatic cycling assays: Spectrophotometric determination of low levels of pyruvate and L-lactate. Anal. Biochem. 239 (1996) 47-52. doi: 10.1006/abio.1996.0289
418. J. VENTER et al.: The sequence of the human genome. Science 291 (2001) 1304-1351. doi: 10.1126/science.1058040. http://www.stanford.edu/class/cs273a/ papers.spr07/09/celera.pdf
419. H. VESTERBERG & H. SCENSSON: Isoelectric fractionation, analysis, and characterization of ampholytes in natural pH-gradients. Acta Chim. Scand. 20 (1966) 820-834
420. T. WAGENKNECHT, R. GRASSUCCI et al.: Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli. J. Mol. Biol. 1988 (199) 137-47. doi: 10.1016/0022-2836 (88) 90384-1
421. B. WALLACE & R. JANES: Synchrotron radiation circular dichroism spectroscopy of proteins secondary structure, fold recognition and structural genomics. Curr. Opin. Chem. Biol. 5 (2001) 567-571. doi: 10.1016/S1367-5931 (00) 00243-X
422. O. WARBURG & W. CHRISTIAN: Isolierung und kristallisation des gärungsferments enolase. Biochem. Z. 310 (1942) 384-421
423. V. WASINGER, S. CORDWELL et al.: Progress with gene-product mapping of the Mollicutes: Mycoplasma genitalium. Electrophoresis 16 (1995) 1090-1094. doi: 10.1002/elps.11501601185
424. K. WEBER & M. OSBORN: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244 (1969) 4406-4412. http://www.jbc.org/content/244/16/4406.full. pdf+html?sid=146d9763-7bb6-4c46-a775-d43c3ac79d26
425. X. WEI & L. LI: Comparative glycoproteomics: approaches and applications. Brief. Funct. Genomic Proteomic 8 (2009) 104-113. doi: 10.1093/bfgp/eln053
426. J. WEILAND, J. ANDERSON et al.: Inexpensive chemifluorescent detection of antibodyalkaline phosphatase conjugates on western blots using 4-methylumbelliferyl phosphate. Anal. Biochem. 361 (2007) 140-142. doi: 10.1016/j.ab.2006.04.012
427. D. WESSEL & U. FLÜGGE: A method for the quantitative recovery of protein in the presence of detergents and lipids. Anal. Biochem. 138 (1984) 141-143. doi: 10.1016/0003-2697 (84) 90782-6
428. R. WESTERMEIER: Electrophoresis in practice. 4 edn.. (Wiley-VCH, Weinheim), 2005. ISBN 3-527-31181-5
429. C. WHITEHOUSE, R. DREYER et al.: Electrospray ionization for mass-spectrometry of large biomolecules. Science 246 (1989) (4926) 64-71. http://www.uni-ulm.de/aok/bernhardt/Teaching/ClusterWS06-07/uebungen/ Cluster06-07-Seminar02.pdf
430. D. WILSON & L. KONERMANN: A capillary mixer with adjustable reaction chamber volume for millisecond time-resolved studies by electrospray mass spectrometry. Anal. Chem. 75 (2003) 6408-6414. doi: 10.1021/ac0346757
431. D. WINZOR: Determination of the net charge (valence) of a protein: A fundamental but elusive parameter. Anal. Biochem. 325 (2004) 1-20. doi: 10.1016/j.ab.2003.09.035
432. G. WISDOM: Conjugation of antibodies to horseradish peroxidase. Methods Mol. Biol. 295 (2005) 127-30. doi: 10.1385/1592598730
433. A. WOLLRAB: Gaschromatographie. (Diesterweg Moritz, Braunschweig), 1983. ISBN 978-342-505455-1
434. V. WOODS, JR. & Y. HAMURO: High resolution, high throughput amide deuterium exchange mass spectrometry (DXMS) determination of protein binding sites structure and dynamics. J. Cell. Biochem. 37 (2001) 89-98. doi:10.1002/jcb.10069
435. F. WORLD: Affinity labelling - an overview. Methods Enzymol. 46 (1977) 3-14. doi: 10.1016/S0076-6879 (77) 46005-1
436. K. WUTHRICH: NMR of proteins and nucleic acids. 2nd edn.. (J. Wiley, New York), 1986. ISBN 978-0471828938
437. Q. XUE & E. YEUNG: Differences in the chemical reactivity of individual molecules of an enzyme. Nature 373 (1995) 681-683. doi: 10.1038/373681a0
438. J. YAGO, F. G. SEVILLA et al.: A Windows program for the derivation of steadystate equations in enzyme systems. Appl. Math. Comput. 181 (2006) 837-852. doi: 10.1016/j.amc.2006.02.016
439. R. YALOW & S. BERSON: Assay of plasma insulin in human subjects by immunological methods. Nature 184 (1959) 1648-1649. doi: 10.1038/1841648b0
440. J. YANKEELOV, JR., C. MITCHELL et al.: A simple trimerization of 2, 3-butanedione yielding a selective reagent for the modification of arginine in proteins. J. Am. Chem. Soc. 90 (1968) 1664-1666. doi: 10.1021/ja01008a056
441. K. YASUI, M. UEGAKI et al.: Enhanced solubilization of membrane proteins by alkylamines and polyamines. Protein Sci. 19 (2010) 486-493. doi: 10.1002/pro.326
442. H. YOM & R. BREMEL: Xerographic paper as a transfer medium for western blots: Quantification of bovine alpha s1-casein by western blot. Anal. Biochem. 200 (1992) 249-253. doi: 10.1016/0003-2697 (92) 90461-F
443. V. YUE & P. SCHIMMEL: Direct and specific photochemical cross-linking of adenosine-5'-triphosphate to an aminoacyl-tRNA-synthase. Biochemistry 16 (1977) 4678-4684. doi: 10.1021/bi00640a023
444. A. ZAMYATNIN: Amino acid, peptide, and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13 (1984) 145-165. doi: 10.1146/annurev. bb.13.060184.001045
445. A. ZARRINE-AFSAR & A. DAVIDSON: The analysis of protein folding kinetic data produced in protein engineering experiments. Methods 34 (2004) 41-50. doi: 10.1016/j.ymeth.2004.03.013
446. J.-H. ZHANG, T. CHUNG et al.: A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 4 (1999) 67-73. http://genecruiser.broadinstitute.org/bbbc/linked files/Zhang JBiomolScr 1999.pdf
447. W. ZHUANG, D. ABRAMAVICIUS et al.: Two-dimensional vibrational optical probes for peptide fast folding investigation. Proc. Natl. Acad. Sci. USA 103 (2006) 18 934-18 938. doi: 10.1073/pnas.0606912103
448. A. ZIEGLER & G. KöHLER: Analytical isoelectric focusing in polymerizable thin layers containing sephadex. FEBS Lett. 64 (1976) 48-51. doi: 10.1016/0014-5793 (76) 80245-1
449. A. ZIEGLER & G. KöHLER: Resolving power of isotachophoresis and isoelectric focussing for immunoglobulins. FEBS Lett. 71 (1976) 142-146. doi: 10.1016/0014-5793 (76) 80917-9
450. X. ZUO & D. SPEICHER: A method for global analysis of complex proteomes using sample prefractionation by solution isoelectrofocusing prior to two-dimensional electrophoresis. Anal. Biochem. 284 (2000) 266-278. doi: 10.1006/abio.2000.4714