title: Enthalpy-entropy balance and convergence temperatures in protein unfolding.
abstract: 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.
authors.affiliation: Department of Biochemistry and Biophysics, II University of Naples, Italy.
authors.forename: R
authors.initials: R
authors.lastname: Ragone
authors.forename: G
authors.initials: G
authors.lastname: Colonna
mesh_terms: D008962:Models, Theoretical; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics; D014867:Water
chemical_list: D011506:Proteins; D014867:Water