Structure-based prediction of the stability of transmembrane helix-helix interactions: the sequence dependence of glycophorin A dimerization.

@article{Mackenzie1998StructurebasedPO,
  title={Structure-based prediction of the stability of transmembrane helix-helix interactions: the sequence dependence of glycophorin A dimerization.},
  author={Kevin Mackenzie and Donald M. Engelman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 7},
  pages={3583-90}
}
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… CONTINUE READING