The change in heat capacity Delta C-p for the folding of ribonuclease A was
determined using differential scanning calorimetry and thermal denaturatio
n curves. The methods gave equivalent results, Delta C-p = 1.15 +/- 0.08 kc
al mol(-1) K-1 Estimates of the conformational stability of ribonuclease A
based on these results from thermal unfolding are in good agreement with es
timates from urea unfolding analyzed using the linear extrapolation method.