Ontology highlight
ABSTRACT:
SUBMITTER: Robert CH
PROVIDER: S-EPMC41387 | biostudies-other | 1995 Aug
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 19950801 16
We examine how the polypeptide chain in protein crystal structures exploits the multivalent hydrogen-bonding potential of bound water molecules. This shows that multiple interactions with a single water molecule tend to occur locally along the chain. A distinctive internal-coordinate representation of the local water-binding segments reveals several consensus conformations. The fractional water occupancy of each was found by comparison of the total number of conformations in the database regardl ...[more]