Coupling of global and local vibrational modes in dynamic allostery of proteins.
Biophys J
; 91(6): 2055-62, 2006 Sep 15.
Article
en En
| MEDLINE
| ID: mdl-16798805
ABSTRACT
It is now recognized that internal global protein dynamics play an important role in the allosteric function of many proteins. Alterations of protein flexibility on effector binding affect the entropic cost of binding at a distant site. We present a coarse-grained model for a potential amplification of such entropic allostery due to coupling of fast, localized modes to the slow, global modes. We show how such coupling can give rise to large compensating entropic and enthalpic terms. The model corresponds to the pattern of calorimetry and NMR data from experiments on the Met repressor.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Modelos Moleculares
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Biophys J
Año:
2006
Tipo del documento:
Article
País de afiliación:
Reino Unido