Electrostatic Contributions to Protein Stability and Folding Energy
Ver/ Abrir
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/7013
comunitat-uji-handle3:10234/8638
comunitat-uji-handle4:
INVESTIGACIONMetadatos
Título
Electrostatic Contributions to Protein Stability and Folding EnergyFecha de publicación
2007-05-15xmlui.dri2xhtml.METS-1.0.item-edition
PostprintEditor
Federation of European Biochemical SocietiesCita bibliográfica
ROCA MOLINER, María Teresa; MESSER, Benjamin; WARSHEL, Arieh. Electrostatic Contributions to Protein Stability and Folding Energy. FEBS letters (2007), v. 581, n. 10, pp. 2065-2071Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://www.sciencedirect.com/science/article/pii/S0014579307004103Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
The ability to predict the thermal stability of proteins based on their corresponding sequence is a problem of great fundamental and practical importance. Here we report an approach for calculating the electrostatic ... [+]
The ability to predict the thermal stability of proteins based on their corresponding sequence is a problem of great fundamental and practical importance. Here we report an approach for calculating the electrostatic contribution to protein stability based on the use of the semimacroscopic protein dipole Langevin dipole (PDLD/S) in its linear response approximation version for self-energy with a dielectric constant, (εpεp) and an effective dielectric for charge–charge interactions (εeffεeff). The method is applied to the test cases of ubiquitin, lipase, dihydrofolate reductase and cold shock proteins with series of εpεp and εeffεeff. It is found that the optimal values of these dielectric constants lead to very promising results, both for the relative stability and the absolute folding energy. Consideration of the specific values of the optimal dielectric constants leads to an exciting conceptual description of the reorganization effect during the folding process. Although this description should be examined by further microscopic studies, the practical use of the current approach seems to offer a powerful tool for protein design and for studies of the energetics of protein folding. [-]
Publicado en
FEBS letters (2007), v. 581, n. 10Derechos de acceso
http://rightsstatements.org/vocab/CNE/1.0/
info:eu-repo/semantics/openAccess
info:eu-repo/semantics/openAccess
Aparece en las colecciones
- QFA_Articles [813]