Electronic Resource
Palo Alto, Calif.
:
Annual Reviews
Annual Review of Physical Chemistry
56 (2005), S. 521-548
ISSN:
0066-426X
Source:
Annual Reviews Electronic Back Volume Collection 1932-2001ff
Topics:
Chemistry and Pharmacology
,
Physics
Notes:
Heat capacity (Cp) is one of several major thermodynamic quantities commonly measured in proteins. With more than half a dozen definitions, it is the hardest of these quantities to understand in physical terms, but the richest in insight. There are many ramifications of observed Cp changes: The sign distinguishes apolar from polar solvation. It imparts a temperature (T) dependence to entropy and enthalpy that may change their signs and which of them dominate. Protein unfolding usually has a positive ??Cp, producing a maximum in stability and sometimes cold denaturation. There are two heat capacity contributions, from hydration and protein-protein interactions; which dominates in folding and binding is an open question. Theoretical work to date has dealt mostly with the hydration term and can account, at least semiquantitatively, for the major Cp-related features: the positive and negative Cp of hydration for apolar and polar groups, respectively; the convergence of apolar group hydration entropy at T Đ 112ʻ́C; the decrease in apolar hydration Cp with increasing T; and the T-maximum in protein stability and cold denaturation.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1146/annurev.physchem.56.092503.141202
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