Hydrogen-bonding and packing features of membrane proteins: functional implications.

ABSTRACT: The recent structural elucidation of about one dozen channels (in which we include transporters) has provided further evidence that these membrane proteins typically undergo large movements during their function. However, it is still not well understood how these proteins achieve the necessary trade-off between stability and mobility. To identify specific structural properties of channels, we compared the helix-packing and hydrogen-bonding patterns of channels with those of membrane coils; the latter is a class of membrane proteins whose structures are expected to be more rigid. We describe in detail how in channels, helix pairs are usually arranged in packing motifs with large crossing angles (|tau| approximately 40 degrees ), where the (small) side chains point away from the packing core

SUBMITTER: Hildebrand PW 

PROVIDER: S-EPMC2257885 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature