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Volumn 307, Issue 1, 2001, Pages 393-405

Using chimeric immunity proteins to explore the energy landscape for α-helical protein folding

Author keywords

Chimera; Intermediate; Sequence; Topology; Transition state

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; CHIMERIC PROTEIN; PROTEIN IM2; PROTEIN IM9; UNCLASSIFIED DRUG; UREA;

EID: 0035896036     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4492     Document Type: Article
Times cited : (28)

References (64)
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  • 28
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    • Exploring the energy surface of protein-folding by structure-reactivity relationships and engineered proteins - Observation of hammond behavior for the gross structure of the transition-state and anti-Hammond behavior for structural elements for unfolding folding of barnase
    • (1995) Biochemistry , vol.34 , pp. 6805-6814
    • Matthews, J.M.1    Fersht, A.R.2
  • 40
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    • 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
  • 54
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenyllethanesulfonyl α-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.