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Volumn 130, Issue 3, 2008, Pages 821-823

Toward β-amino acid proteins: Design, synthesis, and characterization of a fifteen kilodalton β-peptide tetramer

Author keywords

[No Author keywords available]

Indexed keywords

BETA AMINO ACID; BETA PEPTIDE; DIMER; PEPTIDE; UNCLASSIFIED DRUG;

EID: 38349158424     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja077245x     Document Type: Article
Times cited : (75)

References (23)
  • 8
    • 0842282173 scopus 로고    scopus 로고
    • Wavefunction, Inc, Irvine, CA
    • Spartan '04; Wavefunction, Inc.: Irvine, CA.
    • Spartan '04
  • 13
    • 0029118618 scopus 로고
    • Sedimentation equilibrium as thermodynamic tool
    • Academic Press: New York
    • Laue, T. M. Sedimentation equilibrium as thermodynamic tool. In Methods in Enzymology: Energetics of Biological Macromolecules; Academic Press: New York, 1995; Vol. 259, pp 427-452.
    • (1995) Methods in Enzymology: Energetics of Biological Macromolecules , vol.259 , pp. 427-452
    • Laue, T.M.1
  • 16
    • 24944475661 scopus 로고    scopus 로고
    • Although an ideal two-state transition exhibits 100% reversibility, the thermal denaturation of many natural proteins has been interpreted in terms of a two-state model despite reversibilities as low as 80, See, for example: Hible, G, Renault, L, Schaeffer, F, Christova, P, Radulescu, A. Z, Evrin, C, Gilles, A. M, Cherfils, J. J. Mol. Biol. 2005, 352, 1044-1059
    • Although an ideal two-state transition exhibits 100% reversibility, the thermal denaturation of many natural proteins has been interpreted in terms of a two-state model despite reversibilities as low as 80%. See, for example: Hible, G.; Renault, L.; Schaeffer, F.; Christova, P.; Radulescu, A. Z.; Evrin, C.; Gilles, A. M.; Cherfils, J. J. Mol. Biol. 2005, 352, 1044-1059.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.