Whole-body rocking motion of a fusion peptide in lipid bilayers from size-dispersed 15N NMR relaxation.

ABSTRACT: Biological membranes present a highly fluid environment, and integration of proteins within such membranes is itself highly dynamic: proteins diffuse laterally within the plane of the membrane and rotationally about the normal vector of this plane. We demonstrate that whole-body motions of proteins within a lipid bilayer can be determined from NMR (15)N relaxation rates collected for different-sized bicelles. The importance of membrane integration and interaction is particularly acute for proteins and peptides that function on the membrane itself, as is the case for pore-forming and fusion-inducing proteins. For the influenza hemagglutinin fusion peptide, which lies on the surface of membranes and catalyzes the fusion of membranes and vesicles, we found large-amplitude, rigid-body wobbling

SUBMITTER: Lorieau JL 

PROVIDER: S-EPMC3168931 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature