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Updated: Aug 9, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Heat capacity change for ribonuclease A folding
C N Pace1, G R Grimsley, S T Thomas
1Department of Medical Biochemistry and Genetics, Texas A&M University, College Station 77843-1114, USA. nickpace@tamu.edu
Abstract:
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.
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