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Heat capacity change for ribonuclease A folding

Published online by Cambridge University Press:  01 July 1999

C. NICK PACE ,
GERALD R. GRIMSLEY ,
SUSAN T. THOMAS  and
GEORGE I. MAKHATADZE
C. NICK PACE
Affiliation:
Department of Medical Biochemistry and Genetics, Texas A&M University, College Station, Texas 77843-1114 Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128 Center for Macromolecular Design, Texas A&M University, College Station, Texas 77843-2128
GERALD R. GRIMSLEY
Affiliation:
Department of Medical Biochemistry and Genetics, Texas A&M University, College Station, Texas 77843-1114
SUSAN T. THOMAS
Affiliation:
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409
GEORGE I. MAKHATADZE
Affiliation:
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409
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Abstract

The change in heat capacity ΔCp for the folding of ribonuclease A was determined using differential scanning calorimetry and thermal denaturation curves. The methods gave equivalent results, ΔCp = 1.15 ± 0.08 kcal mol−1 K−1. Estimates of the conformational stability of ribonuclease A based on these results from thermal unfolding are in good agreement with estimates from urea unfolding analyzed using the linear extrapolation method.

Keywords

differential scanning calorimetryheat capacity changeprotein foldingprotein stabilityribonuclease Aurea denaturation

Information

Type
Research Article
Information
Protein Science , Volume 8 , Issue 7 , July 1999 , pp. 1500 - 1504
Copyright
© 1999 The Protein Society

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