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Volumn 10, Issue 5, 2002, Pages 649-657

The structure of the transition state for folding of domain-swapped dimeric p13suc1

Author keywords

Dimer; Domain swapping; p13suc1; Protein engineering; Protein folding; Topology

Indexed keywords

DIMER; MONOMER; PROTEIN DERIVATIVE; PROTEIN SUC1; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; SUC1 PROTEIN, S POMBE;

EID: 0036105533     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00762-1     Document Type: Article
Times cited : (19)

References (24)
  • 1
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed 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
  • 3
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 4
    • 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
  • 16
    • 0027382315 scopus 로고
    • Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
    • (1993) Biochemistry , vol.32 , pp. 11270-11278
    • Jackson, S.E.1    ElMasry, N.2    Fersht, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.