The role of hydrophobic interactions in positioning of peripheral proteins in membranes.

ABSTRACT:

Background

Three-dimensional (3D) structures of numerous peripheral membrane proteins have been determined. Biological activity, stability, and conformations of these proteins depend on their spatial positions with respect to the lipid bilayer. However, these positions are usually undetermined.

Results

We report the first large-scale computational study of monotopic/peripheral proteins with known 3D structures. The optimal translational and rotational positions of 476 proteins are determined by minimizing energy of protein transfer from water to the lipid bilayer, which is approximated by a hydrocarbon slab with a decadiene-like polarity and interfacial regions characterized by water-permeation profiles. Predicted membrane-binding sites, protein tilt angles and membrane pene

SUBMITTER: Lomize AL 

PROVIDER: S-EPMC1934363 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature