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Volumn 321, Issue 1, 2002, Pages 1-6

A buried polar residue in the hydrophobic interface of the coiled-coil peptide, GCN4-p1, plays a thermodynamic, not a kinetic role in folding

Author keywords

Buried polar residues; Circular dichroism spectroscopy; Leucine zipper peptides; Protein folding kinetics

Indexed keywords

ALANINE; DIMER; LEUCINE ZIPPER PROTEIN; M PROTEIN; PEPTIDE DERIVATIVE; VALINE;

EID: 0036353719     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00592-2     Document Type: Article
Times cited : (28)

References (21)
  • 7
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 10
    • 0032497322 scopus 로고    scopus 로고
    • A buried polar interaction can direct the relative orientation of helices in a coiled coil
    • (1998) Biochemistry , vol.37 , pp. 12603-12610
    • Oakley, M.G.1    Kim, P.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.