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Heat capacity increments: Conformational transitions in polypeptides
Author(s) -
Couchman P. R.,
Gajnos G. E.,
Ryan C. L.,
Karasz F. E.
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360221108
Subject(s) - chemistry , heat capacity , macromolecule , isobaric process , solvent , thermodynamics , globular protein , electromagnetic coil , denaturation (fissile materials) , folding (dsp implementation) , random coil , helix (gastropod) , chemical physics , crystallography , organic chemistry , biochemistry , circular dichroism , nuclear chemistry , snail , biology , electrical engineering , engineering , ecology , physics
A 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.