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Volumn 121, Issue 49, 1999, Pages 11577-11578

NMR-based quanfification of β-sheet populations in aqueous solution through use of reference peptides for the folded and unfolded states [6]

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE DERIVATIVE;

EID: 0033572951     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja992733t     Document Type: Letter
Times cited : (129)

References (44)
  • 27
    • 0343586107 scopus 로고    scopus 로고
    • Analytical ultracentrifugation showed that none of these peptides self-associates under the conditions used for NMR analysis
    • Analytical ultracentrifugation showed that none of these peptides self-associates under the conditions used for NMR analysis.
  • 30
    • 0342281088 scopus 로고    scopus 로고
    • For other approaches to quantification of β-hairpin populations, see refs 3b, 4a,b and 5b,c
    • For other approaches to quantification of β-hairpin populations, see refs 3b, 4a,b and 5b,c.
  • 31
    • 0342716087 scopus 로고    scopus 로고
    • Details may be found in the Supporting Information
    • Details may be found in the Supporting Information.
  • 33
    • 0020855355 scopus 로고
    • (a) For leading references on use of H/D exchange to analyze peptide and protein conformation, see: Englander, S. W.; Kallenbach, N. R. Q. Rev. Biophys. 1984, 16, 521. Perrin, C. L.; Dwyer, T. J.; Rebek, J.; Duff, R. J. J. Am. Chem. Soc. 1990, 112, 3122. Arrington, C. B.; Teesch, L. M.; Robertson, A. D. J. Mol. Biol. 1999, 285, 1265.
    • (1984) Q. Rev. Biophys. , vol.16 , pp. 521
    • Englander, S.W.1    Kallenbach, N.R.2
  • 34
    • 0025003481 scopus 로고
    • (a) For leading references on use of H/D exchange to analyze peptide and protein conformation, see: Englander, S. W.; Kallenbach, N. R. Q. Rev. Biophys. 1984, 16, 521. Perrin, C. L.; Dwyer, T. J.; Rebek, J.; Duff, R. J. J. Am. Chem. Soc. 1990, 112, 3122. Arrington, C. B.; Teesch, L. M.; Robertson, A. D. J. Mol. Biol. 1999, 285, 1265.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3122
    • Perrin, C.L.1    Dwyer, T.J.2    Rebek, J.3    Duff, R.J.4
  • 35
    • 0033593247 scopus 로고    scopus 로고
    • (a) For leading references on use of H/D exchange to analyze peptide and protein conformation, see: Englander, S. W.; Kallenbach, N. R. Q. Rev. Biophys. 1984, 16, 521. Perrin, C. L.; Dwyer, T. J.; Rebek, J.; Duff, R. J. J. Am. Chem. Soc. 1990, 112, 3122. Arrington, C. B.; Teesch, L. M.; Robertson, A. D. J. Mol. Biol. 1999, 285, 1265.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1265
    • Arrington, C.B.1    Teesch, L.M.2    Robertson, A.D.3
  • 36
    • 0030037714 scopus 로고    scopus 로고
    • (b) For application of H/D exchange to β-sheet model systems, see: Nesloney, C. L.; Kelly, J. W. J. Am. Chem. Soc. 1996, 118, 5836.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5836
    • Nesloney, C.L.1    Kelly, J.W.2
  • 39
    • 0024279235 scopus 로고
    • Val-5 also occurs in a hydrogen-bonded position but cannot be used because this residue is followed by proline in reference peptides 1 and 8 but not in equilibrating peptides 4-6. Proline profoundly influences the backbone conformation of the preceding residue: Wilmot, C. M.; Thornton, J. M. J. Mol. Biol. 1988, 203, 221.
    • (1988) J. Mol. Biol. , vol.203 , pp. 221
    • Wilmot, C.M.1    Thornton, J.M.2
  • 44
    • 0342281085 scopus 로고    scopus 로고
    • note
    • This research was supported by the National Science Foundation (CHE-9820952). J.F.E. was supported by a fellowship from the Ministerio de Educacion y Cultura (Spain) and the Fulbright Commission. The NMR spectrometers were purchased in part with grant NIH 1 S10 RR04981. The CD spectrometer and analytical ultracentrifuge are part of the UW Biophysics Instrumentation Facility (NSF BIR-9512577).


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