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Volumn 287, Issue 3, 2001, Pages 636-641

Role of the connectivity of secondary structure segments in the folding of α1-antitrypsin

Author keywords

Circular permutant; Kinetic trap; Metastable state; Protein folding; Serpin; 1 antitrypsin

Indexed keywords

ALPHA 1 ANTITRYPSIN; SERINE PROTEINASE INHIBITOR;

EID: 0035964912     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.5638     Document Type: Article
Times cited : (7)

References (33)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 5
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 29
  • 30
    • 0023700976 scopus 로고
    • Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites
    • (1988) J. Biol. Chem. , vol.263 , pp. 16626-16630
    • Bruch, M.1    Weiss, V.2    Engel, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.