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Volumn 10, Issue 7, 2001, Pages 1381-1392

Elongation of the BH8 β-hairpin peptide: Electrostatic interactions in β-hairpin formation and stability

Author keywords

hairpin; NMR; Peptides; Protein folding; Secondary structure

Indexed keywords

ALANINE; GLUCOSE; LYSINE; PEPTIDE;

EID: 0034967395     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.52901     Document Type: Article
Times cited : (49)

References (38)
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    • Development of the multiple sequence approximation within the AGADIR model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
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  • 31
    • 0028790273 scopus 로고
    • Comparison between the Φ distribution of the amino acids in the protein database and NMR data indicates that amino acids have various Φ propensities in the random coil conformation
    • (1995) J. Mol. Biol. , vol.254 , pp. 322-333
    • Serrano, L.1
  • 34
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    • Guidelines for protein design: The energetics of β-sheet side-chain interactions
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.