Evaluating tilt angles of membrane-associated helices: comparison of computational and NMR techniques.

ABSTRACT: A computational method to calculate the orientation of membrane-associated alpha-helices with respect to a lipid bilayer has been developed. It is based on a previously derived implicit membrane representation, which was parameterized using the structures of 46 alpha-helical membrane proteins. The method is validated by comparison with an independent data set of six transmembrane and nine antimicrobial peptides of known structure and orientation. The minimum energy orientations of the transmembrane helices were found to be in good agreement with tilt and rotation angles known from solid-state NMR experiments. Analysis of the free-energy landscape found two types of minima for transmembrane peptides: i), Surface-bound configurations with the helix long axis parallel to the membrane, and ii)

SUBMITTER: Ulmschneider MB 

PROVIDER: S-EPMC1367316 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature