Membrane depth-dependent energetic contribution of the tryptophan side chain to the stability of integral membrane proteins.

ABSTRACT: Lipid solvation provides the primary driving force for the insertion and folding of integral membrane proteins. Although the structure of the lipid bilayer is often simplified as a central hydrophobic core sandwiched between two hydrophilic interfacial regions, the complexity of the liquid-crystalline bilayer structure and the gradient of water molecules across the bilayer fine-tune the energetic contributions of individual amino acid residues to the stability of membrane proteins at different depths of the bilayer. The tryptophan side chain is particularly interesting because despite its widely recognized role in anchoring membrane proteins in lipid bilayers, there is little consensus about its hydrophobicity among various experimentally determined hydrophobicity scales. Here we investiga

SUBMITTER: Hong H 

PROVIDER: S-EPMC3731455 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature