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Volumn 78, Issue 2, 2013, Pages 224-237

Chirality-driven folding of short β-lactam pseudopeptides

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL ANALYSIS; ENANTIOPURE; EQUILIBRIUM MODELS; HOMOCHIRAL; MIMETICS; NMR TECHNIQUES; OPEN STRUCTURE; PSEUDO-PEPTIDE; RELATIVE STABILITIES;

EID: 84872565257     PISSN: 00223263     EISSN: 15206904     Source Type: Journal    
DOI: 10.1021/jo302368y     Document Type: Article
Times cited : (8)

References (73)
  • 45
    • 0030175304 scopus 로고    scopus 로고
    • (i +2), they are often not distinguished. Thus, when type preference of β-turns is investigated as a function of their amino acid sequence, most commonly only the ratio of type (I + III) to type II is determined. See: Perczel, A.; Jákli, I.; Foxman, B. M.; Fasman, G. D. Biopolymers 1996, 38, 723-732
    • (1996) Biopolymers , vol.38 , pp. 723-732
    • Perczel, A.1    Jákli, I.2    Foxman, B.M.3    Fasman, G.D.4
  • 67
    • 0009859463 scopus 로고    scopus 로고
    • Birkhausen: New York, For gas-phase experimental studies conducted on configurationally altered short peptides, see
    • Sapse, A. M. Molecular Orbital Calculations for Amino Acids and Peptides; Birkhausen: New York, 2000. For gas-phase experimental studies conducted on configurationally altered short peptides, see
    • (2000) Molecular Orbital Calculations for Amino Acids and Peptides
    • Sapse, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.