Heat capacity in proteins.
Annu Rev Phys Chem
; 56: 521-48, 2005.
Article
em En
| MEDLINE
| ID: mdl-15796710
ABSTRACT
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 deltaCp, 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 approximately 112 degrees C; the decrease in apolar hydration Cp with increasing T; and the T-maximum in protein stability and cold denaturation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Desnaturação Proteica
/
Água
/
Proteínas
/
Temperatura Baixa
/
Temperatura Alta
Idioma:
En
Revista:
Annu Rev Phys Chem
Ano de publicação:
2005
Tipo de documento:
Article