Toward genomic identification of beta-barrel membrane proteins: composition and architecture of known structures.

ABSTRACT: The amino acid composition and architecture of all beta-barrel membrane proteins of known three-dimensional structure have been examined to generate information that will be useful in identifying beta-barrels in genome databases. The database consists of 15 nonredundant structures, including several novel, recent structures. Known structures include monomeric, dimeric, and trimeric beta-barrels with between 8 and 22 membrane-spanning beta-strands each. For this analysis the membrane-interacting surfaces of the beta-barrels were identified with an experimentally derived, whole-residue hydrophobicity scale, and then the barrels were aligned normal to the bilayer and the position of the bilayer midplane was determined for each protein from the hydrophobicity profile. The abundance of each ami

SUBMITTER: Wimley WC 

PROVIDER: S-EPMC2373429 | biostudies-literature | 2002 Feb

REPOSITORIES: biostudies-literature