The magnitude of changes in guanidine-HCl unfolding m-values in the protein, iso-1-cytochrome c, depends upon the substructure containing the mutation

Protein Science

Volumn 7, Issue 8, 1998, Pages 1789-1795

  Hammack, Barbara ^a   Attfield, Kathleen ^a   Clayton, Daniel ^a   Dec, Eric ^a   Dong, Aichun ^b   Sarisky, Catherine ^a   Bowler, Bruce E ^a,c  

^a UNIVERSITY OF DENVER   (United States)

^b UNIVERSITY OF NORTHERN COLORADO   (United States)

^c Department of Chemistry and Biochemistry ^*  (United States)

Author keywords

Equilibrium unfolding; Guanidine hydrochloride denaturation; Iso 1 cytochrome c; m values, protein stability; Protein substructures

Indexed keywords

ASPARTIC ACID; CYTOCHROME C; GLUTAMIC ACID; GUANIDINE; LYSINE; METHIONINE; SERINE;

AMINO ACID SUBSTITUTION; ARTICLE; DENATURATION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

EID: 0032468160     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070814     Document Type: Article

References (11)

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