Chapter 7 Microsecond Time-Scale Hydroxyl Radical Profiling of Solvent-Accessible Protein Residues

Comprehensive Analytical Chemistry

Volumn 52, Issue , 2008, Pages 151-177

  Hambly, David M ^a   Gross, Michael L ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

EID: 67249157665     PISSN: 0166526X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0166-526X(08)00207-9     Document Type: Review

References (125)

1. Koch M.H., Vachette P., and Svergun D.I. Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution. Q. Rev. Biophys. 36 2 (2003) 147-227
2. Braun W., Kallen J., Mikol V., Walkinshaw M.D., and Wuthrich K. Three-dimensional structure and actions of immunosuppressants and their immunophilins. FASEB J. 9 1 (1995) 63-72
3. Harrer R. Associations between light-harvesting complexes and Photosystem II from Marchantia polymorpha L. determined by two- and three-dimensional electron microscopy. Photosynth. Res. 75 3 (2003) 249-258
4. Volkmann N., Liu H., Hazelwood L., Krementsova E.B., Lowey S., Trybus K.M., and Hanein D. The structural basis of myosin V processive movement as revealed by electron cryomicroscopy. Mol. Cell 19 5 (2005) 595-605
5. Wolfe C.L., Warrington J.A., Treadwell L., and Norcum M.T. A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteins. J. Biol. Chem. 280 46 (2005) 38870-38878
6. Galas D.J., and Schmitz A. DNAse footprinting: A simple method for the detection of protein-DNA binding specificity. Nucleic Acids Res. 5 9 (1978) 3157-3170
7. Bradshaw R.A., and Burlingame A.L. From proteins to proteomics. IUBMB Life 57 4-5 (2005) 267-272
8. Chamrad D.C., Koerting G., Gobom J., Thiele H., Klose J., Meyer H.E., and Blueggel M. Interpretation of mass spectrometry data for high-throughput proteomics. Anal. Bioanal. Chem. 376 7 (2003) 1014-1022
9. Wagner G., and Wuthrich K. Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. J. Mol. Biol. 160 2 (1982) 343-361
10. Tullius T.D. Physical studies of protein-DNA complexes by footprinting. Annu. Rev. Biophys. Biophys. Chem. 18 (1989) 213-237
11. Zhong M., Lin L., and Kallenbach N.R. A method for probing the topography and interactions of proteins: Footprinting of myoglobin. Proc. Natl. Acad. Sci. USA 92 6 (1995) 2111-2115
12. McMahan S.A., and Burgess R.R. Use of aryl azide cross-linkers to investigate protein-protein interactions: An optimization of important conditions as applied to Escherichia coli RNA polymerase and localization of a sigma 70-alpha cross-link to the C-terminal region of alpha. Biochemistry 33 40 (1994) 12092-12099
13. Chen Y., Ebright Y.W., and Ebright R.H. Identification of the target of a transcription activator protein by protein-protein photocrosslinking. Science 265 5168 (1994) 90-92
14. Heyduk E., and Heyduk T. Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach. Biochemistry 33 32 (1994) 9643-9650
15. Miyake R., Murakami K., Owens J.T., Greiner D.P., Ozoline O.N., Ishihama A., and Meares C.F. Dimeric association of Escherichia coli RNA polymerase alpha subunits, studied by cleavage of single-cysteine alpha subunits conjugated to iron-(S)-1-[p-(bromoacetamido)benzyl]ethylenediaminetetraacetate. Biochemistry 37 5 (1998) 1344-1349
16. Kluger R., and Alagic A. Chemical cross-linking and protein-protein interactions - A review with illustrative protocols. Bioorg. Chem. 32 6 (2004) 451-472
17. Konermann L., and Simmons D.A. Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry. Mass Spectrom. Rev. 22 1 (2003) 1-26
18. Krishna M.M., Hoang L., Lin Y., and Englander S.W. Hydrogen exchange methods to study protein folding. Methods 34 1 (2004) 51-64
19. Resing K.A., Hoofnagle A.N., and Ahn N.G. Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure. J. Am. Soc. Mass Spectrom. 10 8 (1999) 685-702
20. Zhang Z., and Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2 4 (1993) 522-531
21. Englander S.W., and Poulsen A. Hydrogen-tritium exchange of the random chain polypeptide. Biopolymers 7 3 (1969) 379-393
22. Mandell J.G., Baerga-Ortiz A., Falick A.M., and Komives E.A. Measurement of solvent accessibility at protein-protein interfaces. Methods Mol. Biol. 305 (2005) 65-80
23. Baerga-Ortiz A., Bergqvist S., Mandell J.G., and Komives E.A. Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles. Protein Sci. 13 1 (2004) 166-176
24. Kuck D. Half a century of scrambling in organic ions: Complete, incomplete, progressive and composite atom interchange. Int. J. Mass Spectrom. 213 2/3 (2002) 101-144
25. Deng Y., Pan H., and Smith D.L. Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry. J. Am. Chem. Soc. 121 9 (1999) 1966-1967
26. Reed D.R., and Kass S.R. Hydrogen-deuterium exchange at non-labile sites: A new reaction facet with broad implications for structural and dynamic determinations. J. Am. Soc. Mass Spectrom. 12 11 (2001) 1163-1168
27. Johnson R.S., Krylov D., and Walsh K.A. Proton mobility within electrosprayed peptide ions. J. Mass Spectrom. 30 2 (1995) 386-387
28. Demmers J.A.A., Rijkers D.T.S., Haverkamp J., Killian J.A., and Heck A.J.R. Factors affecting gas-phase deuterium scrambling in peptide ions and their implications for protein structure determination. J. Am. Chem. Soc. 124 37 (2002) 11191-11198
29. Kim M.Y., Maier C.S., Reed D.J., and Deinzer M.L. Site-specific amide hydrogen/deuterium exchange in E. coli thioredoxins measured by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 123 40 (2001) 9860-9866
30. Akashi S., and Takio K. Conformational changes of proteins observed by hydrogen/deuterium exchange and electrospray ionization mass spectrometry. J. Mass Spectrom. Soc. Jpn. 46 1 (1998) 75-82
31. Guy P., Remigy H., Jaquinod M., Bersch B., Blanchard L., Dolla A., and Forest E. Study of the new stability properties induced by amino acid replacement of tyrosine 64 in cytochrome c553 from Desulfovibrio vulgaris Hildenborough using electrospray ionization mass spectrometry. Biochem. Biophys. Res. Commun. 218 1 (1996) 97-103
32. Jaquinod M., Guy P., Halgand F., Caffrey M., Fitch J., Cusanovich M., and Forest E. Stability study of Rhodobacter capsulatus ferrocytochrome c2 wild-type and site-directed mutants using hydrogen/deuterium exchange monitored by electrospray ionization mass spectrometry. FEBS Lett. 380 1,2 (1996) 44-48
33. Maier C.S., Kim O.-H., and Deinzer M.L. Conformational properties of the A-state of cytochrome c studied by hydrogen/deuterium exchange and electrospray mass spectrometry. Anal. Biochem. 252 1 (1997) 127-135
34. Valentine S.J., and Clemmer D.E. H/D exchange levels of shape-resolved cytochrome c conformers in the gas phase. J. Am. Chem. Soc. 119 15 (1997) 3558-3566
35. Wagner D.S., and Anderegg R.J. Conformation of Cytochrome c studied by deuterium exchange-electrospray ionization mass spectrometry. Anal. Chem. 66 5 (1994) 706-711
36. Engen J.R., and Smith D.L. Investigating the higher order structure of proteins: Hydrogen exchange, proteolytic fragmentation, and mass spectrometry. Methods Mol. Biol. (Totowa, NJ) 146 Mass Spectrometry of Proteins and Peptides (2000) 95-112
37. Zhu M.M., Rempel D.L., Du Z., and Gross M.L. Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX. J. Am. Chem. Soc. 125 (2003) 5252-5253
38. Zhu M.M., Rempel D.L., and Gross M.L. Modeling data from titration, amide H/D exchange, and mass spectrometry to obtain protein-ligand binding constants. J. Am. Soc. Mass Spectrom. 15 3 (2004) 388-397
39. Powell K.D., Ghaemmaghami S., Wang M.Z., Ma L., Oas T.G., and Fitzgerald M.C. A general mass spectrometry-based assay for the quantitation of protein-ligand binding interactions in solution. J. Am. Chem. Soc. 124 35 (2002) 10256-10257
40. Powell K.D., and Fitzgerald M.C. Accuracy and precision of a new H/D exchange- and mass spectrometry-based technique for measuring the thermodynamic properties of protein-peptide complexes. Biochemistry 42 17 (2003) 4962-4970
41. Kaltashov I.A., and Eyles S.J. Crossing the phase boundary to study protein dynamics and function: Combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase. J. Mass Spectrom. 37 6 (2002) 557-565
42. Dihazi G.H., and Sinz A. Mapping low-resolution three-dimensional protein structures using chemical cross-linking and Fourier transform ion-cyclotron resonance mass spectrometry. Rapid Commun. Mass Spectrom. 17 17 (2003) 2005-2014
43. Schulz D.M., Ihling C., Clore G.M., and Sinz A. Mapping the topology and determination of a low-resolution three-dimensional structure of the calmodulin-melittin complex by chemical cross-linking and high-resolution FTICRMS: Direct demonstration of multiple binding modes. Biochemistry 43 16 (2004) 4703-4715
44. Sinz A. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom. 38 12 (2003) 1225-1237
45. Green N.S., Reisler E., and Houk K.N. Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers. Protein Sci. 10 7 (2001) 1293-1304
46. Glocker M.O., Borchers C., Fiedler W., Suckau D., and Przybylski M. Molecular characterization of surface topology in protein tertiary structures by Amino-Acylation and mass spectrometric peptide mapping. Bioconjug. Chem. 5 6 (1994) 583-590
47. Ohguro H., Palczewski K., Walsh K.A., and Johnson R.S. Topographic study of arrestin using differential chemical modifications and hydrogen/deuterium exchange. Protein Sci. 3 12 (1994) 2428-2434
48. Amico V., Foti S., Saletti R., Cambria A., and Petrone G. Identification of iodination sites in cytochrome c by high-performance liquid chromatography and fast atom bombardment mass spectrometry. Biomed. Environ. Mass Spectrom. 16 1-12 (1988) 431-437
49. Stadtman E.R., and Levine R.L. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 25 3-4 (2003) 207-218
50. Onisko B., Fernandez E.G., Freire M.L., Schwarz A., Baier M., Camina F., Garcia J.R., Rodriguez-Segade Villamarin S., and Requena J.R. Probing PrPSc structure using chemical cross-linking and mass spectrometry: Evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate. Biochemistry 44 30 (2005) 10100-10109
51. Bennett K.L., Kussmann M., Bjork P., Godzwon M., Mikkelsen M., Sorensen P., and Roepstorff P. Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping - A novel approach to assess intermolecular protein contacts. Protein Sci. 9 8 (2000) 1503-1518
52. Peterson James J., Young Malin M., and Takemoto Larry J. Probing alpha-crystallin structure using chemical cross-linkers and mass spectrometry. Mol. Vis. [Electronic] 10 (2004) 857-866
53. Heyduk T., Baichoo N., and Heyduk E. Hydroxyl radical footprinting of proteins using metal ion complexes. Met. Ions. Biol. Syst. 38 (2001) 255-287
54. Maleknia S.D., Brenowitz M., and Chance M.R. Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry. Anal. Chem. 71 18 (1999) 3965-3973
55. Fenton J.H., and Jackson H. The oxidation of polyhydric alcohols in presence of iron. J. Chem. Soc., Trans. 75 (1899) 1
56. Fenton H.J.H., and Jones H.O. The oxidation of organic acids in presence of ferrous iron. Part I. J. Chem. Soc., Trans. 77 (1900) 69-76
57. Sharp J.S., Becker J.M., and Hettich R.L. Protein surface mapping by chemical oxidation: Structural analysis by mass spectrometry. Anal. Biochem. 313 2 (2003) 216-225
58. Urey H.C., Dawsey L.H., and Rice F.O. Absorption spectrum and decomposition of hydrogen peroxide by light. J. Am. Chem. Soc. 51 (1929) 1371-1383
59. Holt R.B., McLane C.K., and Oldenberg O. Ultraviolet absorption spectrum of hydrogen peroxide. J. Chem. Phys. 16 (1948) 225-229
60. Schrank S.G., Jose H.J., Moreira R.F., and Schroder H.F. Applicability of Fenton and H2O2/UV reactions in the treatment of tannery wastewaters. Chemosphere 60 5 (2005) 644-655
61. Sharp J.S., Becker J.M., and Hettich R.L. Analysis of protein solvent accessible surfaces by photochemical oxidation and mass spectrometry. Anal. Chem. 76 3 (2004) 672-683
62. Morand K., Talbo G., and Mann M. Oxidation of peptides during electrospray ionization. Rapid Commun. Mass Spectrom. 7 8 (1993) 738-743
63. Maleknia S.D., Chance M.R., and Downard K.M. Electrospray-assisted modification of proteins: A radical probe of protein structure. Rapid Commun. Mass Spectrom. 13 23 (1999) 2352-2358
64. Wong J.W.H., Maleknia S.D., and Downard K.M. Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 16 2 (2005) 225-233
65. Maleknia S.D., Wong J.W.H., and Downard K.M. Photochemical and electrophysical production of radicals on millisecond timescales to probe the structure, dynamics and interactions of proteins. Photochem. Photobiol. Sci. 3 8 (2004) 741-748
66. Wong J.W.H., Maleknia S.D., and Downard K.M. Study of the ribonuclease-S-protein-peptide complex using a radical probe and electrospray ionization mass spectrometry. Anal. Chem. 75 7 (2003) 1557-1563
67. Maleknia S.D., and Downard K. Radical approaches to probe protein structure, folding, and interactions by mass spectrometry. Mass Spectrom. Rev. 20 6 (2001) 388-401
68. Hawkins C.L., and Davies M.J. Generation and propagation of radical reactions on proteins. Biochim. Biophys. Acta 1504 2-3 (2001) 196-219
69. Davies M.J., and Dean R.T. Radical-mediated protein oxidation: From chemistry to medicine (1997), Oxford University Press, Oxford pp 44-45
70. Sclavi B., Sullivan M., Chance M.R., Brenowitz M., and Woodson S.A. RNA folding at millisecond intervals by synchrotron hydroxyl radical footprinting. Science (Washington, DC) 279 5358 (1998) 1940-1943
71. Gulotta M., Gilmanshin R., Buscher T.C., Callender R.H., and Dyer R.B. Core formation in apomyoglobin: Probing the upper reaches of the folding energy landscape. Biochemistry 40 17 (2001) 5137-5143
72. Vu D.M., Myers J.K., Oas T.G., and Dyer R.B. Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein. Biochemistry 43 12 (2004) 3582-3589
73. Shcherbakova I., Mitra S., Beer R.H., and Brenowitz M. Fast Fenton footprinting: A laboratory-based method for the time-resolved analysis of DNA, RNA and proteins. Nucleic Acids Res. 34 6 (2006) e48
74. Takamoto K., and Chance M.R. Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 251-276
75. Brenowitz M., Erie D.A., and Chance M.R. Catching RNA polymerase in the act of binding: Intermediates in transcription illuminated by synchrotron footprinting. Proc. Natl. Acad. Sci. USA 102 13 (2005) 4659-4660
76. Sclavi B., Woodson S., Sullivan M., Chance M., and Brenowitz M. Following the folding of RNA with time-resolved synchrotron X-ray footprinting. Meth. Enzymol. 295 Energetics of Biological Macromolecules, Part B (1998) 379-402
77. Chance M.R. Unfolding of apomyoglobin examined by synchrotron footprinting. Biochem. Biophys. Res. Commun. 287 3 (2001) 614-621
78. Rashidzadeh H., Khrapunov S., Chance M.R., and Brenowitz M. Solution structure and interdomain interactions of the Saccharomyces cerevisiae "TATA binding protein" (TBP) probed by radiolytic protein footprinting. Biochemistry 42 13 (2003) 3655-3665
79. Guan J.-Q., Takamoto K., Almo S.C., Reisler E., and Chance M.R. Structure and dynamics of the actin filament. Biochemistry 44 9 (2005) 3166-3175
80. Maleknia S.D., Ralston C.Y., Brenowitz M.D., Downard K.M., and Chance M.R. Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques. Anal. Biochem. 289 2 (2001) 103-115
81. Garrison W.M. Reaction mechanisms in the radiolysis of peptides, polypeptides, and proteins. Chem. Rev. (Washington, DC) 87 2 (1987) 381-398
82. Reddy S.G., Wong K.K., Parast C.V., Peisach J., Magliozzo R.S., and Kozarich J.W. Dioxygen inactivation of pyruvate formate-lyase: EPR evidence for the formation of protein-based sulfinyl and peroxyl radicals. Biochemistry 37 2 (1998) 558-563
83. Wheeler O.H., and Montalvo R. Radiolysis of phenylalanine and tyrosine and aqueous solution. Radiat. Res. 40 1 (1969) 1-10
84. Steenken S., and O'Neill P. Oxidative demethoxylation of methoxylated phenols and hydroxybenzoic acids by the hydroxyl radical. An in situ electron spin resonance, conductometric pulse radiolysis and product analysis study. J. Phys. Chem. 81 6 (1977) 505-508
85. Armstrong R.C., and Swallow A.J. Pulse- and gamma-radiolysis of aqueous solutions of tryptophan. Radiat. Res. 40 3 (1969) 563-579
86. Jovanovic S.V., and Simic M.G. Repair of tryptophan radicals by antioxidants. J. Free Radic. Biol. Med. 1 2 (1985) 125-129
87. Josimovic L., Jankovic I., and Jovanovic S.V. Radiation induced decomposition of tryptophan in the presence of oxygen. Radiat. Phys. Chem. 41 6 (1993) 835-841
88. Davies M.J., Fu S., Wang H., and Dean R.T. Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radic. Biol. Med. 27 11/12 (1999) 1151-1163
89. Winchester R.V., and Lynn K.R. X- and g-radiolysis of some tryptophan dipeptides. Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 17 6 (1970) 541-548
90. Candeias L.P., Wardman P., and Mason R.P. The reaction of oxygen with radicals from oxidation of tryptophan and indole-3-acetic acid. Biophys. Chem. 67 1-3 (1997) 229-237
91. Jayson G.G., Scholes G., and Weiss J. Formation of formylkynurenine by the action of X-rays on tryptophan in aqueous solution. Biochem. J. 57 (1954) 386-390
92. Simat T.J., and Steinhart H. Oxidation of free Tryptophan and Tryptophan residues in peptides and proteins. J. Agric. Food Chem. 46 2 (1998) 490-498
93. Uchida K., and Kawakishi S. 2-Oxohistidine as a novel biological marker for oxidatively modified proteins. FEBS Lett. 332 3 (1993) 208-210
94. Uchida K., and Kawakishi S. Selective oxidation of imidazole ring in histidine residues by the ascorbic acid-copper ion system. Biochem. Biophys. Res. Commun. 138 2 (1986) 659-665
95. Kopoldova J., and Hrncir S. Gamma-radiolysis of aqueous solution of histidine. Zeitschrift fuer Naturforschung, C: J. Biosci. 32C 7-8 (1977) 482-487
96. Bansal K.M., and Sellers R.M. Polarographic and optical pulse radiolysis study of the radicals formed by hydroxyl radical attack on imidazole and related compounds in aqueous solutions. J. Phys. Chem. 79 17 (1975) 1775-1780
97. Rao P.S., Simic M., and Hayon E. Pulse radiolysis study of imidazole and histidine in water. J. Phys. Chem. 79 13 (1975) 1260-1263
98. Burgess V.A., Easton C.J., and Hay M.P. Selective reaction of glycine residues in hydrogen atom transfer from amino acid derivatives. J. Am. Chem. Soc. 111 3 (1989) 1047-1052
99. Von Sonntag C., and Schuchmann H.-P. Peroxyl radicals in aqueous solutions. Peroxyl Radic. (1997) 173-234
100. Bennett J.E. Kinetic electron paramagnetic resonance study of the reactions of tert-butylperoxyl radicals in aqueous solution. J. Chem. Soc., Faraday Trans. 86 19 (1990) 3247-3252
101. Neta P., Huie R.E., and Ross A.B. Rate constants for reactions of peroxyl radicals in fluid solutions. J. Phys. Chem. Ref. Data 19 2 (1990) 413-513
102. Bothe E., Schuchmann M.N., Schulte-Frohlinde D., and Von Sonntag C. Hydroperoxyl elimination from a-hydroxyalkylperoxyl radicals in aqueous solution. Photochem. Photobiol. 28 4-5 (Singlet Oxygen Relat. Species Chem. Biol.) (1978) 639-644
103. Ilan Y., Rabani J., and Henglein A. Pulse radiolytic investigations of peroxy radicals produced from 2-propanol and methanol. J. Phys. Chem. 80 14 (1976) 1558-1562
104. Abramovitch S., and Rabani J. Pulse radiolytic investigations of peroxy radicals in aqueous solutions of acetate and glycine. J. Phys. Chem. 80 14 (1976) 1562-1565
105. 2 radicals. J. Phys. Chem. 78 21 (1974) 2089-2093
106. Howard J.A. Absolute rate constants for reactions of oxyl radicals. Adv. Free Radical Chem. (London) 4 (1972) 49-173
107. Bennett J.E., Brown D.M., and Mile B. Electron spin resonance of the reactions of alkylperoxy radicals. 2. Equilibrium between alkylperoxy radicals and tetroxide molecules. Trans. Faraday Soc. 66 2 (1970) 397-405
108. Adamic K., Howard J.A., and Ingold K.U. Absolute rate constants for hydrocarbon autoxidation. XVI. Reactions of peroxy radicals at low temperatures. Can. J. Chem. 47 20 (1969) 3803-3808
109. Buxton G.V., Greenstock C.L., Helman W.P., and Ross A.B. Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (.OH/.O-) in aqueous solution. J. Phys. Chem. Ref. Data 17 2 (1988) 513-886
110. von Sonntag C. The Chemical Basis of Radiation Biology (1987), Taylor and Francis, London
111. Xu G., and Chance M.R. Radiolytic modification and reactivity of amino acid residues serving as structural probes for protein footprinting. Anal. Chem. 77 14 (2005) 4549-4555
112. Levine R.L., Berlett B.S., Moskovitz J., Mosoni L., and Stadtman E.R. Methionine residues may protect proteins from critical oxidative damage. Mech. Ageing Dev. 107 3 (1999) 323-332
113. Levine R.L., Moskovitz J., and Stadtman E.R. Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation. IUBMB Life 50 4-5 (2000) 301-307
114. Levine R.L., Mosoni L., Berlett B.S., and Stadtman E.R. Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. USA 93 26 (1996) 15036-15040
115. Vogt W. Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic. Biol. Med. 18 1 (1995) 93-105
116. DeFelippis M.R., Faraggi M., and Klapper M.H. Evidence for through-bond long-range electron transfer in peptides. J. Am. Chem. Soc. 112 14 (1990) 5640-5642
117. Klapper M.H., and Faraggi M. Applications of pulse radiolysis to protein chemistry. Q. Rev. Biophys. 12 4 (1979) 465-519
118. Faraggi M., DeFelippis M.R., and Klapper M.H. Long-range electron transfer between tyrosine and tryptophan in peptides. J. Am. Chem. Soc. 111 14 (1989) 5141-5145
119. Prutz W.A., Siebert F., Butler J., Land E.J., Menez A., and Montenay-Garestier T. Charge transfer in peptides: Intramolecular radical transformations involving methionine, tryptophan and tyrosine. Biochim. Biophys. Acta (BBA) - Protein Struct. Mol. Enzymol. 705 2 (1982) 139-149
120. Eaton W.A., Munoz V., Hagen S.J., Jas G.S., Lapidus L.J., Henry E.R., and Hofrichter J. Fast kinetics and mechanisms in protein folding. Annu. Rev. Biophys. Biomol. Struct. 29 (2000) 327-359
121. Ivankov D.N., and Finkelstein A.V. Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc. Natl. Acad. Sci. USA 101 24 (2004) 8942-8944
122. Gilmanshin R., Williams S., Callender R.H., Woodruff W.H., and Dyer R.B. Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA 94 8 (1997) 3709-3713
123. Kiselar J.G., Maleknia S.D., Sullivan M., Downard K.M., and Chance M.R. Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry. Int. J. Radiat. Biol. 78 2 (2002) 101-114
124. Ma B., Elkayam T., Wolfson H., and Nussinov R. Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc. Natl. Acad. Sci. USA 100 10 (2003) 5772-5777
125. Hambly D.M., and Gross M.L. Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale. J. Am. Soc. Mass Spectrom. 16 12 (2005) 2057-2063