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Volumn 313, Issue 2, 2003, Pages 216-225

Protein surface mapping by chemical oxidation: Structural analysis by mass spectrometry

Author keywords

Collisional dissociation; Electrospray; Fenton chemistry; Mass spectrometry; Oxidation; Protein derivatization

Indexed keywords

AMINO ACIDS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PROTEINS; SOLVENTS;

EID: 0037442729     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00612-7     Document Type: Article
Times cited : (127)

References (34)
  • 1
    • 0036007555 scopus 로고    scopus 로고
    • Identification of the interface of a large protein-protein complex using H/D exchange and Fourier transform ion cyclotron resonance mass spectrometry
    • Yamada N., Suzuki E., Hirayama K. Identification of the interface of a large protein-protein complex using H/D exchange and Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun. Mass Spectrom. 16:2002;293-299.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 293-299
    • Yamada, N.1    Suzuki, E.2    Hirayama, K.3
  • 2
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith D.L., Deng Y., Zhang Z. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32:1997;135-146.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 3
    • 0029930590 scopus 로고    scopus 로고
    • Conformational heterogeneity of stability of apomyoglobin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry
    • Wang F., Tang X. Conformational heterogeneity of stability of apomyoglobin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry. Biochemistry. 35:1996;4069-4078.
    • (1996) Biochemistry , vol.35 , pp. 4069-4078
    • Wang, F.1    Tang, X.2
  • 4
    • 0035894045 scopus 로고    scopus 로고
    • Monitoring structural changes of proteins in an ion trap over approximately 10-200 ms: Unfolding transitions in cytochrome c ions
    • Badman E.R., Hoaglund-Hyzer C.S., Clemmer D.E. Monitoring structural changes of proteins in an ion trap over approximately 10-200. ms: unfolding transitions in cytochrome c ions Anal. Chem. 73:2001;6000-6007.
    • (2001) Anal. Chem. , vol.73 , pp. 6000-6007
    • Badman, E.R.1    Hoaglund-Hyzer, C.S.2    Clemmer, D.E.3
  • 5
    • 0035840954 scopus 로고    scopus 로고
    • Kinetic intermediates in the folding of gaseous protein ions characterized by electron capture dissociation mass spectrometry
    • Horn D.M., Breuker K., Frank A.J., McLafferty F.W. Kinetic intermediates in the folding of gaseous protein ions characterized by electron capture dissociation mass spectrometry. J. Am. Chem. Soc. 123:2001;9792-9799.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9792-9799
    • Horn, D.M.1    Breuker, K.2    Frank, A.J.3    McLafferty, F.W.4
  • 6
    • 0035919776 scopus 로고    scopus 로고
    • The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate
    • Gustafsson M., Griffiths W.J., Furusjo E., Johansson J. The palmitoyl groups of lung surfactant protein C reduce unfolding into a fibrillogenic intermediate. J. Mol. Biol. 310:2001;937-950.
    • (2001) J. Mol. Biol. , vol.310 , pp. 937-950
    • Gustafsson, M.1    Griffiths, W.J.2    Furusjo, E.3    Johansson, J.4
  • 8
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau D., Mak M., Przybylski M. Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc. Natl. Acad. Sci. USA. 89:1992;5630-5634.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 9
    • 0036081149 scopus 로고    scopus 로고
    • Chemical-modification rescue assessed by mass spectrometry demonstrates that gamma-thia-lysine yields the same activity as lysine in aldolase
    • Hopkins C.E., O'Connor P.B., Allen K.N., Costello C.E., Tolan D.R. Chemical-modification rescue assessed by mass spectrometry demonstrates that gamma-thia-lysine yields the same activity as lysine in aldolase. Protein Sci. 11:2002;1591-1599.
    • (2002) Protein Sci. , vol.11 , pp. 1591-1599
    • Hopkins, C.E.1    O'Connor, P.B.2    Allen, K.N.3    Costello, C.E.4    Tolan, D.R.5
  • 10
    • 0033005165 scopus 로고    scopus 로고
    • Probing the reactivity of nucleophile residues in human 2,3-diphosphoglycerate/deoxy-hemoglobin complex by aspecific chemical modifications
    • Scaloni A., Ferranti P., De Simone G., Mamone G., Sannolo N., Malorni A. Probing the reactivity of nucleophile residues in human 2,3-diphosphoglycerate/deoxy-hemoglobin complex by aspecific chemical modifications. FEBS Lett. 452:1999;190-194.
    • (1999) FEBS Lett. , vol.452 , pp. 190-194
    • Scaloni, A.1    Ferranti, P.2    De Simone, G.3    Mamone, G.4    Sannolo, N.5    Malorni, A.6
  • 11
    • 0035865266 scopus 로고    scopus 로고
    • Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques
    • Maleknia S.D., Ralston C.Y., Brenowitz M.D., Downard K.M., Chance M.R. Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques. Anal. Biochem. 289:2001;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
  • 12
    • 0033568535 scopus 로고    scopus 로고
    • Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry
    • Maleknia S.D., Brenowitz M., Chance M.R. Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry. Anal. Chem. 71:1999;3965-3973.
    • (1999) Anal. Chem. , vol.71 , pp. 3965-3973
    • Maleknia, S.D.1    Brenowitz, M.2    Chance, M.R.3
  • 13
    • 0036150988 scopus 로고    scopus 로고
    • Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry
    • Kiselar J.G., Maleknia S.D., Sullivan M., Downard K.M., Chance M.R. Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry. Int. J. Radiat. Biol. 78:2002;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
  • 14
    • 0036006581 scopus 로고    scopus 로고
    • Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry
    • Maleknia S.D., Kiselar J.G., Downard K.M. Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Commun. Mass Spectrom. 16:2002;53-61.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 53-61
    • Maleknia, S.D.1    Kiselar, J.G.2    Downard, K.M.3
  • 15
    • 0035719748 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry
    • Maleknia S.D., Downard K.M. Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry. Eur. J. Biochem. 268:2001;5578-5588.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5578-5588
    • Maleknia, S.D.1    Downard, K.M.2
  • 16
    • 0032733489 scopus 로고    scopus 로고
    • Electrospray-assisted modification of proteins: A radical probe of protein structure
    • Maleknia S.D., Chance M.R., Downard K.M. Electrospray-assisted modification of proteins: a radical probe of protein structure. Rapid Commun. Mass Spectrom. 13:1999;2352-2358.
    • (1999) Rapid Commun. Mass Spectrom. , vol.13 , pp. 2352-2358
    • Maleknia, S.D.1    Chance, M.R.2    Downard, K.M.3
  • 17
    • 0027931824 scopus 로고
    • Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach
    • Heyduk E., Heyduk T. Mapping protein domains involved in macromolecular interactions: a novel protein footprinting approach. Biochemistry. 33:1994;9643-9650.
    • (1994) Biochemistry , vol.33 , pp. 9643-9650
    • Heyduk, E.1    Heyduk, T.2
  • 18
    • 0035226911 scopus 로고    scopus 로고
    • Hydroxyl radical footprinting of proteins using metal ion complexes
    • Heyduk T., Baichoo N., Heyduk E. Hydroxyl radical footprinting of proteins using metal ion complexes. Met. Ions Biol. Syst. 38:2001;255-287.
    • (2001) Met. Ions Biol. Syst. , vol.38 , pp. 255-287
    • Heyduk, T.1    Baichoo, N.2    Heyduk, E.3
  • 19
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D., Wright P.E. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263:1996;531-538.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 20
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer D., Yao J., Dyson H.J., Wright P.E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. 5:1998;148-155.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 21
    • 0030056766 scopus 로고    scopus 로고
    • The native state of apomyoglobin described by proton NMR spectroscopy: The A-B-G-H interface of wild-type sperm whale apomyoglobin
    • Lecomte J.T., Kao Y.H., Cocco M.J. The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin. Proteins. 25:1996;267-285.
    • (1996) Proteins , vol.25 , pp. 267-285
    • Lecomte, J.T.1    Kao, Y.H.2    Cocco, M.J.3
  • 22
    • 0032775818 scopus 로고    scopus 로고
    • Conformational properties of native sperm whale apomyoglobin in solution
    • Lecomte J.T., Sukits S.F., Bhattacharya S., Falzone C.J. Conformational properties of native sperm whale apomyoglobin in solution. Protein Sci. 8:1999;1484-1491.
    • (1999) Protein Sci. , vol.8 , pp. 1484-1491
    • Lecomte, J.T.1    Sukits, S.F.2    Bhattacharya, S.3    Falzone, C.J.4
  • 23
    • 0036467707 scopus 로고    scopus 로고
    • Characterization of monomeric and dimeric forms of recombinant Sml1p-histag protein by electrospray mass spectrometry
    • Uchiki T., Hettich R., Gupta V., Dealwis C. Characterization of monomeric and dimeric forms of recombinant Sml1p-histag protein by electrospray mass spectrometry. Anal. Biochem. 301:2002;35-48.
    • (2002) Anal. Biochem. , vol.301 , pp. 35-48
    • Uchiki, T.1    Hettich, R.2    Gupta, V.3    Dealwis, C.4
  • 24
    • 0034641742 scopus 로고    scopus 로고
    • Automated de novo sequencing of proteins by tandem high-resolution mass spectrometry
    • Horn D.M.Z., McLafferty F.W. Automated de novo sequencing of proteins by tandem high-resolution mass spectrometry. Proc. Natl. Acad. Sci. USA. 97:2000;10313-10317.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10313-10317
    • Horn, D.M.Z.1    McLafferty, F.W.2
  • 25
    • 0025780005 scopus 로고
    • Sustained off-resonance irradiation for CAD involving FTMS. CAD technique that emulates infrared multiphoton dissociation
    • Gauthier J.W., Trautman T.R., Jacobson D.B. Sustained off-resonance irradiation for CAD involving FTMS. CAD technique that emulates infrared multiphoton dissociation. Anal. Chim. Acta. 246:1991;211-225.
    • (1991) Anal. Chim. Acta , vol.246 , pp. 211-225
    • Gauthier, J.W.1    Trautman, T.R.2    Jacobson, D.B.3
  • 26
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz R., Braun W. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Computational Chem. 19:1998;319-333.
    • (1998) J. Computational Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 27
    • 0025296867 scopus 로고
    • High-resolution study of the three-dimensional structure of horse heart metmyoglobin
    • Evans S.V., Brayer G.D. High-resolution study of the three-dimensional structure of horse heart metmyoglobin. J. Mol. Biol. 213:1990;885-897.
    • (1990) J. Mol. Biol. , vol.213 , pp. 885-897
    • Evans, S.V.1    Brayer, G.D.2
  • 29
    • 0030870810 scopus 로고    scopus 로고
    • Mapping conformational changes in a protein: Application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein
    • Baichoo N., Heyduk T. Mapping conformational changes in a protein: application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein. Biochemistry. 36:1997;10830-10836.
    • (1997) Biochemistry , vol.36 , pp. 10830-10836
    • Baichoo, N.1    Heyduk, T.2
  • 30
    • 0002586920 scopus 로고    scopus 로고
    • Internet-based analytical chemistry resources: A model project
    • Fenyo D., Zhang W., Chait B.T., Beavis R.C. Internet-based analytical chemistry resources: a model project. Anal. Chem. 68:1996;721A-726A.
    • (1996) Anal. Chem. , vol.68
    • Fenyo, D.1    Zhang, W.2    Chait, B.T.3    Beavis, R.C.4
  • 31
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • Roepstorff P., Fohlman J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 11:1984;601.
    • (1984) Biomed. Mass Spectrom. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 33
  • 34
    • 0034663738 scopus 로고    scopus 로고
    • Protein threading using PROSPECT: Design and evaluation
    • Xu Y., Xu D. Protein threading using PROSPECT: design and evaluation. Proteins. 40:2000;343-354.
    • (2000) Proteins , vol.40 , pp. 343-354
    • Xu, Y.1    Xu, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.