Quantitative protein dynamics from dominant folding pathways.
Phys Rev Lett
; 99(11): 118102, 2007 Sep 14.
Article
en En
| MEDLINE
| ID: mdl-17930474
ABSTRACT
We develop a theoretical approach to the protein-folding problem based on out-of-equilibrium stochastic dynamics. Within this framework, the computational difficulties related to the existence of large time scale gaps are removed, and simulating the entire reaction in atomistic details using existing computers becomes feasible. We discuss how to determine the most probable folding pathway, identify configurations representative of the transition state, and compute the most probable transition time. We perform an illustrative application of these ideas, studying the conformational evolution of alanine dipeptide, within an all-atom model based on the empiric GROMOS96 force field.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Pliegue de Proteína
Idioma:
En
Revista:
Phys Rev Lett
Año:
2007
Tipo del documento:
Article