Abstract
Molecular modeling of the thrombin inhibitor, cyclotheonamide A (CA), found two conformational families for theCA backbone, one of which resembles the bound CA structure as recently determined by X-ray crystallography. The relative rigidity of the Arg to Dpa backbone region provides structural preorganization of the CA backbone, and should enhance thrombin binding by reducing entropy cost. a-ketoarnide flexibility should facilitate formation of the transition-state analogue complex.
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