On Computing Equilibrium Binding Constants for Protein-Protein Association in Membranes.

ABSTRACT: Protein association in lipid membranes is fundamental to membrane protein function and of great biomedical relevance. All-atom and coarse-grained models have been extensively used to understand the protein-protein interactions in the membrane and to compute equilibrium association constants. However, slow translational and rotational diffusion of protein in membrane presents challenges to the effective sampling of conformations defining the ensembles of free and bound states contributing to the association equilibrium and the free energy of dimerization. We revisit the homodimerization equilibrium of the TM region of glycophorin A. Conformational sampling is performed using umbrella sampling along previously proposed one-dimensional collective variables and compared with sampling over a tw

SUBMITTER: Majumder A 

PROVIDER: S-EPMC11260346 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature