Computing energy landscape maps and structural excursions of proteins.

ABSTRACT:

Background

Structural excursions of a protein at equilibrium are key to biomolecular recognition and function modulation. Protein modeling research is driven by the need to aid wet laboratories in characterizing equilibrium protein dynamics. In principle, structural excursions of a protein can be directly observed via simulation of its dynamics, but the disparate temporal scales involved in such excursions make this approach computationally impractical. On the other hand, an informative representation of the structure space available to a protein at equilibrium can be obtained efficiently via stochastic optimization, but this approach does not directly yield information on equilibrium dynamics.

Methods

We present here a novel methodology that first builds a multi-dimensional

SUBMITTER: Sapin E 

PROVIDER: S-EPMC5001232 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature