Lipid bilayer deformation and the free energy of interaction of a Kv channel gating-modifier toxin.

ABSTRACT: A number of membrane proteins act via binding at the water/lipid bilayer interface. An important example of such proteins is provided by the gating-modifier toxins that act on voltage-gated potassium (Kv) channels. They are thought to partition to the headgroup region of lipid bilayers, and so provide a good system for probing the nature of interactions of a protein with the water/bilayer interface. We used coarse-grained molecular dynamics simulations to compute the one-dimensional potential of mean force (i.e., free energy) profile that governs the interaction between a Kv channel gating-modifier toxin (VSTx1) and model phospholipid bilayers. The reaction coordinate sampled corresponds to the position of the toxin along the bilayer normal. The course-grained representation of the protein

SUBMITTER: Wee CL 

PROVIDER: S-EPMC2553134 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature