Abstract
AbstractA thermodynamic treatment of the helix–coil transition of synthetic polypeptides in binary organic solvent mixtures is extended to describe isobaric heat‐capacity increments associated with the phenomenon. This development resolves such increments into three components: two associated respectively with intrinsic differences between the ordered and disordered states of the macromolecule and between the coil–solvent complex and its components, and a third term derived from the temperature dependence in the fraction of coil residues bound to active solvent. Insights derived from this analysis are also applied to the discussion of some heat capacity increments associated with the denaturation of globular proteins.
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