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Volumn , Issue 2, 1999, Pages 389-400

Conformational preferences of peptides containing reverse-turn mimetic bicyclic lactams: Inverse γ-turns versus type-II' β-turns - Insights into β-hairpin stability

Author keywords

NMR spectroscopy; Reverse turn mimics; Hairpins; Turns; Turns

Indexed keywords

LACTAM DERIVATIVE; SYNTHETIC PEPTIDE;

EID: 0032820462     PISSN: 1434193X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-0690(199902)1999:2<389::AID-EJOC389>3.0.CO;2-7     Document Type: Article
Times cited : (118)

References (70)
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  • 61
    • 0345238876 scopus 로고    scopus 로고
    • note
    • In competitive solvents, such as water and DMSO, the chemical shifts of peptide amide protons exhibit differential temperature dependences. Solvent-exposed protons exhibit a large temperature dependence, while intramolecular hydrogen-bonded (solvent-shielded) protons exhibit only a small temperature dependence.
  • 63
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    • note
    • [23] using the all-atom AMBER* parameters and the GB/SA solvation water model in Macromodel 5.5. Improved conformational analysis using the MC/SD protocol in GB/SA water was performed on compound 9b. A 10-membered-ring NH5⋯O2 H-bond interaction was observed in most of the conformers sampled during the simulation, thus suggesting that the benzyl substituent plays a critical role in determining the turn mimetic properties of the indolizidinone ring system.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.