Ontology highlight
ABSTRACT:
SUBMITTER: Durham E
PROVIDER: S-EPMC2712621 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Journal of molecular modeling 20090221 9
The burial of hydrophobic amino acids in the protein core is a driving force in protein folding. The extent to which an amino acid interacts with the solvent and the protein core is naturally proportional to the surface area exposed to these environments. However, an accurate calculation of the solvent-accessible surface area (SASA), a geometric measure of this exposure, is numerically demanding as it is not pair-wise decomposable. Furthermore, it depends on a full-atom representation of the mol ...[more]