Ontology highlight
ABSTRACT:
SUBMITTER: MacKenzie KR
PROVIDER: S-EPMC19879 | biostudies-literature | 1998 Mar
REPOSITORIES: biostudies-literature
MacKenzie K R KR Engelman D M DM
Proceedings of the National Academy of Sciences of the United States of America 19980301 7
The ability to predict the effects of point mutations on the interaction of alpha-helices within membranes would represent a significant step toward understanding the folding and stability of membrane proteins. We use structure-based empirical parameters representing steric clashes, favorable van der Waals interactions, and restrictions of side-chain rotamer freedom to explain the relative dimerization propensities of 105 hydrophobic single-point mutants of the glycophorin A (GpA) transmembrane ...[more]