Double bilayers and transmembrane gradients: a molecular dynamics study of a highly charged peptide.

ABSTRACT: The position and extent of movement of a charged peptide within a membrane bilayer provides much controversy. In our study, we have examined the nature of the highly charged helix-turn-helix motif (S3b and S4) to address how a highly charged peptide is stabilized within a bilayer in the presence of various transmembrane electrical potentials. Our double-bilayer simulation results show how the variation of the salt concentrations between the inner and outer bath establishes a transmembrane potential. Our results also show that important features of the peptide affected by changes in electrical potential are the center of mass depth, the swivel/kink degrees of conformation, and the hydrogen-bonding patterns. As the voltage gradient across the bilayer increased, the center of mass of the pept

SUBMITTER: Denning EJ 

PROVIDER: S-EPMC2547445 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature