Conformational landscapes of membrane proteins delineated by enhanced sampling molecular dynamics simulations

Harpole TJ, Delemotte L

Biochimica et Biophysica Acta (BBA) - Biomembranes 1860 (4) 909-926 [2018-04-00; online 2018-04-00]

The expansion of computational power, better parameterization of force fields, and the development of novel algorithms to enhance the sampling of the free energy landscapes of proteins have allowed molecular dynamics (MD) simulations to become an indispensable tool to understand the function of biomolecules. The temporal and spatial resolution of MD simulations allows for the study of a vast number of processes of interest. Here, we review the computational efforts to uncover the conformational free energy landscapes of a subset of membrane proteins: ion channels, transporters and G-protein coupled receptors. We focus on the various enhanced sampling techniques used to study these questions, how the conclusions come together to build a coherent picture, and the relationship between simulation outcomes and experimental observables.

Affiliated researcher

QC bibliography QC xrefs

PubMed 29113819

DOI 10.1016/j.bbamem.2017.10.033

Crossref 10.1016/j.bbamem.2017.10.033