Affinity Labeling of Purine Nucleotide Sites in Proteins

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The goal of this award is to develop the tools which will allow a systematic exploration of the amino acid residues in the purine nucleotide binding sites of proteins. Such sites will be affinity labeled using reagents which contain alkylating groups capable of reacting covalently with the protein. The purine nucleotide moiety will thus provide the specifity for chemical modification of the proteins within the binding sites. The effects of these reagents will be examined on three proteins, pyruvate kinase, a membrane-bound ADP receptor protein from human platelets and cAMP phosphodiesterase. The results of the research should enhance our understanding of the structure and architecture of the active sites of proteins, and how these biomacromolecules catalyze or regulate the myriad reactions that occur in living systems.