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Volumn 305, Issue , 2005, Pages 65-79

Measurement of Solvent Accessibility at Protein-Protein Interfaces

Author keywords

Amide H 2H exchange; hydration; MALDI TOF mass spectrometry

Indexed keywords

AMIDE; DEUTERIUM; HYDROGEN; LIGAND; PEPSIN A; PEPTIDE FRAGMENT; PROTEIN; SOLVENT;

EID: 21344450047     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1385/1-59259-912-5:065     Document Type: Chapter
Times cited : (28)

References (13)
  • 1
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein–protein interfaces by decreased amide proton solvent accessibility
    • 710
    • Mandell, J. G., Falick, A. M., and Komives, E. A. (1998) Identification of protein–protein interfaces by decreased amide proton solvent accessibility. Proc. Nat. Acad. Sci. USA 95, 14,705–14,710
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , Issue.14 , pp. 705-714
    • Mandell, J. G.1    Falick, A. M.2    Komives, E. A.3
  • 3
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • Baerga-Ortiz, A., Hughes, C. A., Mandell, J. G., and Komives, E. A. (2002) Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci. 11, 1300–1308.
    • (2002) Protein Sci , vol.11 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C. A.2    Mandell, J. G.3    Komives, E. A.4
  • 5
    • 0035815111 scopus 로고    scopus 로고
    • Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB
    • Hughes, C. A., Mandell, J. G., Anand, G. S., Stock, A. M., and Komives, E. A. (2001) Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB. J. Mol. Biol. 307, 967–976.
    • (2001) J. Mol. Biol , vol.307 , pp. 967-976
    • Hughes, C. A.1    Mandell, J. G.2    Anand, G. S.3    Stock, A. M.4    Komives, E. A.5
  • 6
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: the modern legacy of Linderstrøm-Lang
    • Englander, S., Mayne, L., Bai, Y., and Sosnick, T. (1997) Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Science 6, 1101–1109.
    • (1997) Protein Science , vol.6 , pp. 1101-1109
    • Englander, S.1    Mayne, L.2    Bai, Y.3    Sosnick, T.4
  • 7
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange. Proteins 17, 75–86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J. S.2    Mayne, L.3    Englander, S. W.4
  • 8
    • 0030199899 scopus 로고    scopus 로고
    • Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins
    • Dharmasiri, K. and Smith, D. L. (1996) Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins. Analytical Chemistry 68, 2340–2344.
    • (1996) Analytical Chemistry , vol.68 , pp. 2340-2344
    • Dharmasiri, K.1    Smith, D. L.2
  • 9
    • 0347994109 scopus 로고    scopus 로고
    • Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles
    • Baerga-Ortiz, A., Bergqvist, S. P., Mandell, J. G., and Komives, E. A. (2004) Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles. Protein Sci. 13, 166–176.
    • (2004) Protein Sci , vol.13 , pp. 166-176
    • Baerga-Ortiz, A.1    Bergqvist, S. P.2    Mandell, J. G.3    Komives, E. A.4
  • 10
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation
    • Zhang, Z. and Smith, D. L. (1993) Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci. 2, 522–531.
    • (1993) Protein Sci , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D. L.2
  • 11
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • Mandell, J. G., Falick, A. M., and Komives, E. A. (1998) Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Analytical Chemistry 70, 3987–3995.
    • (1998) Analytical Chemistry , vol.70 , pp. 3987-3995
    • Mandell, J. G.1    Falick, A. M.2    Komives, E. A.3
  • 12
    • 0000950943 scopus 로고
    • Measurement of fast proton exchange rates in isotopically labeled compounds
    • H., K. 621
    • Gemmecker, G., Jahnke, W., and H., K. (1993) Measurement of fast proton exchange rates in isotopically labeled compounds. J. Am. Chem. Soc. 115, 11,620–11,621.
    • (1993) J. Am. Chem. Soc , vol.115 , Issue.11 , pp. 620-11
    • Gemmecker, G.1    Jahnke, W.2
  • 13
    • 0346122798 scopus 로고    scopus 로고
    • GRAPZ: visualization, surface properties, and electrostatics of macromolecular structures and sequences
    • Petrey, D. and Honig, B. (2003) GRAPZ: visualization, surface properties, and electrostatics of macromolecular structures and sequences. Methods Enzymol. 374, 492–509.
    • (2003) Methods Enzymol , vol.374 , pp. 492-509
    • Petrey, D.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.