Helical packing patterns in membrane and soluble proteins.

ABSTRACT: This article presents the results of a detailed analysis of helix-helix interactions in membrane and soluble proteins. A data set of interacting pairs of helices in membrane proteins of known structure was constructed and a structure alignment algorithm was used to identify pairs of helices in soluble proteins that superimpose well with pairs of helices in the membrane-protein data set. Most helix pairs in membrane proteins are found to have a significant number of structural homologs in soluble proteins, although in some cases, primarily involving irregular helices, no close homologs exist. An analysis of geometric relationships between interacting helices in the two sets of proteins identifies some differences in the distributions of helix length, interfacial area, packing angle, and dis

SUBMITTER: Gimpelev M 

PROVIDER: S-EPMC1304916 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature