메뉴 건너뛰기




Volumn 298, Issue 5, 2000, Pages 971-984

A breakdown of symmetry in the folding transition state of protein L

Author keywords

Folding kinetics; Protein folding; Protein L; Transition state; Hairpin formation

Indexed keywords

BACTERIAL PROTEIN; IMMUNOGLOBULIN BINDING FACTOR; IMMUNOGLOBULIN G; PROTEIN L; UNCLASSIFIED DRUG;

EID: 0034685619     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3701     Document Type: Article
Times cited : (221)

References (38)
  • 13
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 28
    • 0040589805 scopus 로고    scopus 로고
    • Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: Secondary structure propensities are not conserved in proteins with the same fold
    • (1997) Protein Sci , vol.6 , pp. 162-174
    • Ramirez-Alvarado, M.1    Serrano, L.2    Blanco, F.J.3
  • 33


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.