Abstract
A stereochemical analysis of the substrate and inhibitor specificities of bovine pancreatic ribonuclease A is presented. A scheme is proposed in which the binding specificity for this protein-nucleic acid interaction is rationalized in terms of a simple system of H-bonds. The functional groups that govern substrate binding for transphosphorylation and hydrolysis, respectively, are considered and differentiated, and predictions are offered concerning the interaction of presumptive substrates with RNase.