Free-energy landscape of protein oligomerization from atomistic simulations.

ABSTRACT: In the realm of protein-protein interactions, the assembly process of homooligomers plays a fundamental role because the majority of proteins fall into this category. A comprehensive understanding of this multistep process requires the characterization of the driving molecular interactions and the transient intermediate species. The latter are often short-lived and thus remain elusive to most experimental investigations. Molecular simulations provide a unique tool to shed light onto these complex processes complementing experimental data. Here we combine advanced sampling techniques, such as metadynamics and parallel tempering, to characterize the oligomerization landscape of fibritin foldon domain. This system is an evolutionarily optimized trimerization motif that represents an ideal mod

SUBMITTER: Barducci A 

PROVIDER: S-EPMC3856838 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature