Partitioning of amino acids into a model membrane: capturing the interface.

ABSTRACT: Energetics of protein side chain partitioning between aqueous solution and cellular membranes is of fundamental importance for correctly capturing the membrane binding and specific protein-lipid interactions of peripheral membrane proteins. We recently reported a highly mobile membrane mimetic (HMMM) model that accelerates lipid dynamics by modeling the membrane interior partially as a fluid organic solvent while retaining a literal description of the lipid head groups and the beginning of the tails. While the HMMM has been successfully applied to study spontaneous insertion of a number of peripheral proteins into membranes, a quantitative characterization of the energetics of membrane-protein interactions in HMMM membranes has not been performed. We report here the free energy profiles fo

SUBMITTER: Pogorelov TV 

PROVIDER: S-EPMC3983343 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature