메뉴 건너뛰기




Volumn 304, Issue 5, 2000, Pages 967-982

The SH3-fold family: Experimental evidence and prediction of variations in the folding pathways

Author keywords

Folding kinetics; Folding prediction; SH3 domain; Sso7d; Transistion state

Indexed keywords

PROTEIN; PROTEIN SSO7D; UNCLASSIFIED DRUG;

EID: 0034671177     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4234     Document Type: Article
Times cited : (144)

References (58)
  • 10
    • 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
  • 14
    • 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.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 29
  • 30
    • 0031576337 scopus 로고    scopus 로고
    • Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
    • (1997) J. Mol. Biol. , vol.273 , pp. 330-337
    • Ladurner, A.G.1    Fersht, A.R.2
  • 40
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four-helix-bundle protein
    • (1997) Fold. Des. , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 52
    • 0014347799 scopus 로고
    • Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
    • (1968) Biopolymers , vol.6 , pp. 1425-1436
    • Venkatachalam, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.