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Volumn 11, Issue 3, 2002, Pages 522-528

Propagation of a single destabilizing mutation throughout the Escherichia coli ribonuclease HI native state

Author keywords

Amino acid substitution; Hydrogen exchange; Mutation; Protein folding; Protein stability

Indexed keywords

DEUTERIUM; HYDROGEN; RIBONUCLEASE H;

EID: 0036180562     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.37202     Document Type: Article
Times cited : (23)

References (24)
  • 21
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • published erratum appears in Nat. Struct. Biol. 1997 Jun;4(6):505
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 22
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.