Outer Membrane Protein Folding and Topology from a Computational Transfer Free Energy Scale.

ABSTRACT: Knowledge of the transfer free energy of amino acids from aqueous solution to a lipid bilayer is essential for understanding membrane protein folding and for predicting membrane protein structure. Here we report a computational approach that can calculate the folding free energy of the transmembrane region of outer membrane β-barrel proteins (OMPs) by combining an empirical energy function with a reduced discrete state space model. We quantitatively analyzed the transfer free energies of 20 amino acid residues at the center of the lipid bilayer of OmpLA. Our results are in excellent agreement with the experimentally derived hydrophobicity scales. We further exhaustively calculated the transfer free energies of 20 amino acids at all positions in the TM region of OmpLA. We found that the asy

SUBMITTER: Lin M 

PROVIDER: S-EPMC4881743 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature