DynaMut: predicting the impact of mutations on protein conformation, flexibility and stability.

ABSTRACT: Proteins are highly dynamic molecules, whose function is intrinsically linked to their molecular motions. Despite the pivotal role of protein dynamics, their computational simulation cost has led to most structure-based approaches for assessing the impact of mutations on protein structure and function relying upon static structures. Here we present DynaMut, a web server implementing two distinct, well established normal mode approaches, which can be used to analyze and visualize protein dynamics by sampling conformations and assess the impact of mutations on protein dynamics and stability resulting from vibrational entropy changes. DynaMut integrates our graph-based signatures along with normal mode dynamics to generate a consensus prediction of the impact of a mutation on protein stabilit

SUBMITTER: Rodrigues CH 

PROVIDER: S-EPMC6031064 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature