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Volumn 3, Issue 8, 2004, Pages 741-748

Photochemical and electrophysical production of radicals on millisecond timescales to probe the structure, dynamics and interactions of proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; APOMYOGLOBIN; CALMODULIN; HYDROXYL RADICAL; MELITTIN; OXYGEN RADICAL; PEPTIDE; RADICAL; RIBONUCLEASE; SOLVENT; UREA;

EID: 4644253428     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b315904c     Document Type: Article
Times cited : (61)

References (40)
  • 1
    • 0027482738 scopus 로고
    • Reactive species and their accumulation on radical-damaged proteins
    • R. T. Dean T. Roger S. Gieseg M. J. Davies Reactive species and their accumulation on radical-damaged proteins Trends Biochem. Sci. 1993 18 437-41.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 437-441
    • Dean, R.T.1    Roger, T.2    Gieseg, S.3    Davies, M.J.4
  • 2
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • R. T. Dean S. Fu R. Stocker M. J. Davies Biochemistry and pathology of radical-mediated protein oxidation Biochem. J. 1997 15 1-18.
    • (1997) Biochem. J. , vol.15 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 3
    • 0035795180 scopus 로고    scopus 로고
    • Generation and propagation of radical reactions on proteins
    • C. L. Hawkins M. J. Davies Generation and propagation of radical reactions on proteins Biochim. Biophys. Acta 2001 504 196-219.
    • (2001) Biochim. Biophys. Acta , vol.504 , pp. 196-219
    • Hawkins, C.L.1    Davies, M.J.2
  • 4
    • 0033041916 scopus 로고    scopus 로고
    • Reactive oxygen species-induced molecular damage and its application in pathology
    • S. Toyokuni Reactive oxygen species-induced molecular damage and its application in pathology Pathol. Int. 1999 49 91-102.
    • (1999) Pathol. Int. , vol.49 , pp. 91-102
    • Toyokuni, S.1
  • 6
    • 0035473032 scopus 로고    scopus 로고
    • Photo-oxidation of proteins and its role in cataractogenesis
    • M. J. Davies R. J. Truscott Photo-oxidation of proteins and its role in cataractogenesis J. Photochem. Photobiol., B 2001 63 114-25.
    • (2001) J. Photochem. Photobiol., B , vol.63 , pp. 114-125
    • Davies, M.J.1    Truscott, R.J.2
  • 7
    • 0034565044 scopus 로고    scopus 로고
    • The biochemistry of aging
    • J. A. Knight The biochemistry of aging Adv. Clin. Chem. 2000 35 1-62.
    • (2000) Adv. Clin. Chem. , vol.35 , pp. 1-62
    • Knight, J.A.1
  • 8
    • 0037082103 scopus 로고    scopus 로고
    • Reactive oxygen species and protein oxidation in aging: A look back, a look ahead
    • K. Hensley R. A. Floyd Reactive oxygen species and protein oxidation in aging: a look back, a look ahead. Arch. Biochem. Biophys. 2002 397 377-83.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 377-383
    • Hensley, K.1    Floyd, R.A.2
  • 9
    • 0036628724 scopus 로고    scopus 로고
    • Role of oxidative stress and protein oxidation in the aging process
    • R. S. Sohal Role of oxidative stress and protein oxidation in the aging process Free Radical Biol. Med. 2002 33 37-44.
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 37-44
    • Sohal, R.S.1
  • 10
    • 0036306115 scopus 로고    scopus 로고
    • Why Are Proteins So Robust To Site Mutations?
    • D. M. Taverna R. A. Goldstein Why Are Proteins So Robust To Site Mutations? J. Mol. Biol. 2002 315 479-484.
    • (2002) J. Mol. Biol. , vol.315 , pp. 479-484
    • Taverna, D.M.1    Goldstein, R.A.2
  • 11
    • 4644347018 scopus 로고    scopus 로고
    • Evolutionary perspectives on protein structure, stability, and functionality
    • R. A. Goldstein Evolutionary perspectives on protein structure, stability, and functionality Lect. Notes Phys. 2002 585 82-107.
    • (2002) Lect. Notes Phys. , vol.585 , pp. 82-107
    • Goldstein, R.A.1
  • 12
    • 0032733489 scopus 로고    scopus 로고
    • Electrospray-Assisted Modification of Proteins. A Radical Probe of Protein Structure
    • S. D. Maleknia M. R. Chance K. M. Downard Electrospray-Assisted Modification of Proteins. A Radical Probe of Protein Structure Rapid Commun. Mass Spectrom. 1999 13 2352-2358.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2352-2358
    • Maleknia, S.D.1    Chance, M.R.2    Downard, K.M.3
  • 13
    • 0035865266 scopus 로고    scopus 로고
    • Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques
    • S. D. Maleknia C. Y. Ralston M. D. Brenowitz K. M. Downard M. R. Chance Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques Anal. Biochem. 2001 289 103-115.
    • (2001) Anal. Biochem. , vol.289 , pp. 103-115
    • Maleknia, S.D.1    Ralston, C.Y.2    Brenowitz, M.D.3    Downard, K.M.4    Chance, M.R.5
  • 14
    • 0035719748 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry
    • S. D. Maleknia K. M. Downard Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry Eur. J. Biochem. 2001 268 5578-5588.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5578-5588
    • Maleknia, S.D.1    Downard, K.M.2
  • 15
    • 0035497782 scopus 로고    scopus 로고
    • Radical Approaches to Probe Protein Structure, Folding, and Interactions by Mass Spectrometry
    • S. D. Maleknia K. M. Downard Radical Approaches to Probe Protein Structure, Folding, and Interactions by Mass Spectrometry Mass Spectrom. Rev. 2001 20 388-401.
    • (2001) Mass Spectrom. Rev. , vol.20 , pp. 388-401
    • Maleknia, S.D.1    Downard, K.M.2
  • 16
    • 2242445690 scopus 로고    scopus 로고
    • Electrospray generated oxygenated radicals to probe protein structure
    • E. Gelpi, John Wiley & Sons, Chichester, UK
    • S. D. Maleknia, M. R. Chance and K. M. Downard, Electrospray generated oxygenated radicals to probe protein structure, in Advances in mass spectrometry, ed. E. Gelpi, John Wiley & Sons, Chichester, UK, 2001, pp. 543–544.
    • (2001) Advances in Mass Spectrometry , pp. 543-544
    • Maleknia, S.D.1    Chance, M.R.2    Downard, K.M.3
  • 17
    • 0036150988 scopus 로고    scopus 로고
    • Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry
    • J. G. Kiselar S. D. Maleknia M. Sullivan K. M. Downard M. R. Chance Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry Int. J. Radiat. Biol. 2002 78 101-114.
    • (2002) Int. J. Radiat. Biol. , vol.78 , pp. 101-114
    • Kiselar, J.G.1    Maleknia, S.D.2    Sullivan, M.3    Downard, K.M.4    Chance, M.R.5
  • 18
    • 0036006581 scopus 로고    scopus 로고
    • Hydroxyl radical probe of the surface of lysozyme by synchrotron X-ray radiolysis and mass spectrometry
    • S. D. Maleknia J. G. Kiselar K. M. Downard Hydroxyl radical probe of the surface of lysozyme by synchrotron X-ray radiolysis and mass spectrometry Rapid Commun. Mass Spectrom. 2002 16 53-61.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 53-61
    • Maleknia, S.D.1    Kiselar, J.G.2    Downard, K.M.3
  • 19
    • 0242500901 scopus 로고    scopus 로고
    • Study of the Ribonuclease S-Protein–Peptide Complex Using a Radical Probe and Electrospray Ionization Mass Spectrometry
    • J. W. H. Wong S. D. Maleknia K. M. Downard Study of the Ribonuclease S-Protein–Peptide Complex Using a Radical Probe and Electrospray Ionization Mass Spectrometry Anal. Chem. 2003 75 1557-1563.
    • (2003) Anal. Chem. , vol.75 , pp. 1557-1563
    • Wong, J.W.H.1    Maleknia, S.D.2    Downard, K.M.3
  • 20
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in the presence of iron
    • H. J. H. Fenton Oxidation of tartaric acid in the presence of iron J. Chem. Soc. 1894 65 899-910.
    • (1894) J. Chem. Soc. , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 21
    • 8544249099 scopus 로고
    • The oxidation of polyhydric alcohols in the presence of iron
    • H. J. H. Fenton H. Jackson The oxidation of polyhydric alcohols in the presence of iron J. Chem. Soc. 1899 75 1-11.
    • (1899) J. Chem. Soc. , vol.75 , pp. 1-11
    • Fenton, H.J.H.1    Jackson, H.2
  • 22
    • 0026680555 scopus 로고
    • A stable solid that generates hydroxyl radical upon dissociation in aqueous solutions: Reactions with proteins and nucleic acids
    • P. A. King V. E. Anderson J. O. Edwards R. C. Gustafson R. C. Plumb J. W. Suggs A stable solid that generates hydroxyl radical upon dissociation in aqueous solutions: Reactions with proteins and nucleic acids J. Am. Chem. Soc. 1992 114 5430-5432.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 5430-5432
    • King, P.A.1    Anderson, V.E.2    Edwards, J.O.3    Gustafson, R.C.4    Plumb, R.C.5    Suggs, J.W.6
  • 23
    • 0002193871 scopus 로고
    • Primary products in radiation chemistry
    • I. Farhatazis and M. A. Rodgers, VCH Publishers, New York
    • N. V. Klassen, Primary products in radiation chemistry, in Radiation Chemistry: Principles and Applications, ed. I. Farhatazis and M. A. Rodgers, VCH Publishers, New York, 1987, pp. 29–64.
    • (1987) Radiation Chemistry: Principles and Applications , pp. 29-64
    • Klassen, N.V.1
  • 24
    • 0000302143 scopus 로고
    • Reaction mechanisms in the radiolysis of peptides
    • W. M. Garrison Reaction mechanisms in the radiolysis of peptides Chem. Rev. 1987 87 381-398.
    • (1987) Chem. Rev. , vol.87 , pp. 381-398
    • Garrison, W.M.1
  • 25
    • 0001230161 scopus 로고    scopus 로고
    • Formation of N-formylkynurenine suggests the involvement of apolipoprotein B-100 centered tryptophan radicals in the initiation of LDL lipid peroxidation
    • A. Gieβauf B. van Wickern T. Simat H. Steinhart H. Esterbauer Formation of N-formylkynurenine suggests the involvement of apolipoprotein B-100 centered tryptophan radicals in the initiation of LDL lipid peroxidation FEBS Lett. 1996 389 136-140.
    • (1996) FEBS Lett. , vol.389 , pp. 136-140
    • Gieβauf, A.1    van Wickern, B.2    Simat, T.3    Steinhart, H.4    Esterbauer, H.5
  • 26
    • 0033568535 scopus 로고    scopus 로고
    • Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry
    • S. D. Maleknia M. D. Brenowitz M. R. Chance Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry Anal. Chem. 1999 71 3965-3973.
    • (1999) Anal. Chem. , vol.71 , pp. 3965-3973
    • Maleknia, S.D.1    Brenowitz, M.D.2    Chance, M.R.3
  • 27
    • 0032319210 scopus 로고    scopus 로고
    • Following the folding of RNA with time-resolved synchrotron X-ray footprinting
    • B. Sclavi S. Woodson M. Sullivan M. R. Chance M. Brenowitz Following the folding of RNA with time-resolved synchrotron X-ray footprinting Methods Enzymol. 1998 295 379-402.
    • (1998) Methods Enzymol. , vol.295 , pp. 379-402
    • Sclavi, B.1    Woodson, S.2    Sullivan, M.3    Chance, M.R.4    Brenowitz, M.5
  • 28
    • 0026116076 scopus 로고
    • Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry
    • J. A. Loo R. R. Loo H. R. Udseth C. G. Edmonds R. D. Smith Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry Rapid Commun. Mass Spectrom. 1991 5 3 101-5.
    • (1991) Rapid Commun. Mass Spectrom. , vol.5 , Issue.3 , pp. 101-105
    • Loo, J.A.1    Loo, R.R.2    Udseth, H.R.3    Edmonds, C.G.4    Smith, R.D.5
  • 29
    • 0001510590 scopus 로고
    • Ion formation from charged droplets: Roles of geometry, energy, and time
    • J. B. Fenn Ion formation from charged droplets: roles of geometry, energy, and time J. Am. Soc. Mass Spectrom. 1993 4 7 524-35.
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , Issue.7 , pp. 524-535
    • Fenn, J.B.1
  • 30
    • 0036335091 scopus 로고    scopus 로고
    • Protein-ion charge-state distributions in electrospray ionization mass spectrometry: Distinguishing conformational contributions from masking effects
    • D. R. Gumerov R. Dmitry A. Dobo I. A. Kaltashov Protein-ion charge-state distributions in electrospray ionization mass spectrometry: distinguishing conformational contributions from masking effects Eur. J. Mass Spectrom. 2002 8 2 123-129.
    • (2002) Eur. J. Mass Spectrom. , vol.8 , Issue.2 , pp. 123-129
    • Gumerov, D.R.1    Dmitry, R.2    Dobo, A.3    Kaltashov, I.A.4
  • 31
    • 0037258408 scopus 로고    scopus 로고
    • Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry
    • R. Grandori Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry J. Mass Spectrom. 2003 38 1 11-15.
    • (2003) J. Mass Spectrom. , vol.38 , Issue.1 , pp. 11-15
    • Grandori, R.1
  • 32
    • 0037442729 scopus 로고    scopus 로고
    • Protein surface mapping by chemical oxidation: Structural analysis by mass spectrometry
    • J. S. Sharp J. M. Becker R. L. Hettich Protein surface mapping by chemical oxidation: structural analysis by mass spectrometry Anal. Biochem. 2003 313 216-225.
    • (2003) Anal. Biochem. , vol.313 , pp. 216-225
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 33
    • 0842283944 scopus 로고    scopus 로고
    • Analysis of protein solvent accessibile surfaces by photochemical oxidation and mass spectrometry
    • J. S. Sharp J. M. Becker R. L. Hettich Analysis of protein solvent accessibile surfaces by photochemical oxidation and mass spectrometry Anal. Chem. 2004 76 672-683.
    • (2004) Anal. Chem. , vol.76 , pp. 672-683
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 34
    • 0027931824 scopus 로고
    • Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach
    • E. Heyduk T. Heyduk Mapping protein domains involved in macromolecular interactions: a novel protein footprinting approach Biochemistry 1994 33 9643-9650.
    • (1994) Biochemistry , vol.33 , pp. 9643-9650
    • Heyduk, E.1    Heyduk, T.2
  • 35
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • F. M. Hughson P. E. Wright R. L. Baldwin Structural characterization of a partly folded apomyoglobin intermediate Science 1990 249 1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 36
    • 0032477947 scopus 로고    scopus 로고
    • UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse apomyoglobin
    • Z. Chi S. A. Asher UV resonance Raman determination of protein acid denaturation: selective unfolding of helical segments of horse apomyoglobin Biochemistry 1998 37 2865-2872.
    • (1998) Biochemistry , vol.37 , pp. 2865-2872
    • Chi, Z.1    Asher, S.A.2
  • 39
    • 0025879057 scopus 로고
    • A Mass Spectrometry Method for Mapping the Interface Topography of Interacting Proteins, Illustrated by the Melittin–Calmodulin System
    • R. F. Steiner S. Albaugh C. Fenselau C. Murphy M. Vestling A Mass Spectrometry Method for Mapping the Interface Topography of Interacting Proteins, Illustrated by the Melittin–Calmodulin System Anal. Biochem. 1991 196 120-125.
    • (1991) Anal. Biochem. , vol.196 , pp. 120-125
    • Steiner, R.F.1    Albaugh, S.2    Fenselau, C.3    Murphy, C.4    Vestling, M.5


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