The Transmembrane Helix Tilt May Be Determined by the Balance between Precession Entropy and Lipid Perturbation.

ABSTRACT: Hydrophobic helical peptides interact with lipid bilayers in various modes, determined by the match between the length of the helix's hydrophobic core and the thickness of the hydrocarbon region of the bilayer. For example, long helices may tilt with respect to the membrane normal to bury their hydrophobic cores in the membrane, and the lipid bilayer may stretch to match the helix length. Recent molecular dynamics simulations and potential of mean force calculations have shown that some TM helices whose lengths are equal to, or even shorter than, the bilayer thickness may also tilt. The tilt is driven by a gain in the helix precession entropy, which compensates for the free energy penalty resulting from membrane deformation. Using this free energy balance, we derived theoretically an equat

SUBMITTER: Gofman Y 

PROVIDER: S-EPMC4053537 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature