Enthalpy-entropy balance and convergence temperatures in protein unfolding.
We find that isoenthalpic and isoentropic temperatures characterizing the unfolding of small globular proteins are linked by a simple relationship, which takes into account the occurrence of common values of specific unfolding enthalpy and entropy changes. The difference between these temperatures implies that the hydration effect favors protein folding over a quite large range of temperatures.
Ragone
R
R
Department of Biochemistry and Biophysics, II University of Naples, Italy.
Colonna
G
G
D008962:Models, Theoretical; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics; D014867:Water
D011506:Proteins; D014867:Water