## Abstract A general theory has been developed for conformational intramolecular transitions in a single macromolecule with a high degree of polymerization (an infinite length model) capable of forming two types of ordered structures: the α‐helix and the folded β‐structure, as well as acquiring th
Heat capacity increments: Conformational transitions in polypeptides
✍ Scribed by P. R. Couchman; G. E. Gajnos; C. L. Ryan Jr.; F. E. Karasz
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 624 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Synopsis
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.
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