Heat capacity change for ribonuclease A folding.
The change in heat capacity deltaCp for the folding of ribonuclease A was determined using differential scanning calorimetry and thermal denaturation curves. The methods gave equivalent results, deltaCp = 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.
Pace
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Department of Medical Biochemistry and Genetics, Texas A&M University, College Station 77843-1114, USA. nickpace@tamu.edu
Grimsley
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Thomas
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Makhatadze
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GI
D002152:Calorimetry, Differential Scanning; D006358:Hot Temperature; D011489:Protein Denaturation; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D013816:Thermodynamics
D012259:Ribonuclease, Pancreatic