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Volumn 316, Issue 3, 2002, Pages 789-798

Three topologically equivalent core residues affect the transition state ensemble in a protein folding reaction

Author keywords

Cytokine; Folding kinetics; Interleukin 1 ; Protein folding; trefoil

Indexed keywords

INTERLEUKIN 1BETA; PHENYLALANINE;

EID: 0036304410     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5270     Document Type: Article
Times cited : (22)

References (34)
  • 2
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • (2000) Proc. Natl. Acad. Sci. USA , vol.V97 , pp. 1525-1529
    • Fersht, A.R.1
  • 6
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 9
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding? An investigation for small globular proteins
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 11
    • 0034612995 scopus 로고    scopus 로고
    • Identification of distant homologues of fibroblast growth factors suggests a common ancestor for all β-trefoil proteins
    • (2000) J. Mol. Biol. , vol.302 , pp. 1041-1047
    • Ponting, C.P.1    Russell, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.