Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

Protein Science

Volumn 4, Issue 10, 1995, Pages 2138-2148

  Myers, Jeffrey K ^a,b   Nick Pace, C ^a,b   Martin Scholtz, J ^a,b  

^a Department of Medical Biochemistry and Genetics ^*  (United States)

^b TEXAS A AND M UNIVERSITY   (United States)

Author keywords

denaturation; guanidine hydrochloride; heat capacity changes; m values; protein folding; protein stability; solvent accessible surface area; urea

Indexed keywords

GUANIDINE; PROTEIN; UREA;

ARTICLE; CORRELATION FUNCTION; DISULFIDE BOND; ENERGY TRANSFER; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; THERMOSTABILITY;

ANIMAL; CALORIMETRY; COMPARATIVE STUDY; ENZYMES; GUANIDINE; GUANIDINES; HEAT; HUMAN; KINETICS; MATHEMATICS; MURAMIDASE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; REGRESSION ANALYSIS; RIBONUCLEASE T1; RIBONUCLEASES; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; THERMODYNAMICS;

EID: 0028820703     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.5560041020     Document Type: Article

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