Ontology highlight
ABSTRACT:
SUBMITTER: Royer WE
PROVIDER: S-EPMC26166 | biostudies-literature | 1996 Dec
REPOSITORIES: biostudies-literature
Royer W E WE Pardanani A A Gibson Q H QH Peterson E S ES Friedman J M JM
Proceedings of the National Academy of Sciences of the United States of America 19961201 25
One of the most remarkable structural aspects of Scapharca dimeric hemoglobin is the disruption of a very well-ordered water cluster at the subunit interface upon ligand binding. We have explored the role of these crystallographically observed water molecules by site-directed mutagenesis and osmotic stress techniques. The isosteric mutation of Thr-72-->Val in the interface increases oxygen affinity more than 40-fold with a surprising enhancement of cooperativity. The only significant structural ...[more]