Heat capacity in proteins

被引:348
作者
Prabhu, NV [1 ]
Sharp, KA [1 ]
机构
[1] Univ Penn, ER Johnson Res Fdn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA
关键词
hydrophobic effect; entropy-enthalpy compensation; protein stability; protein hydration;
D O I
10.1146/annurev.physchem.56.092503.141202
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
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 Delta 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 approximate to 112 degrees C; the decrease in apolar hydration Cp with increasing T; and the T-maximum in protein stability and cold denaturation.
引用
收藏
页码:521 / 548
页数:28
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