PHYSICAL CHEMISTRY OF BIOLOGICAL MACROMOLECULES

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The purpose of this project is to study the physical properties of a wide variety of biological macromolecules with the goal of correlating these properties to the structure and function of the macromolecules. The emphasis is on the thermodynamics of the interactions of these macromolecules and on their molecular size and shape. Analytical ultracentrifugation and mathematical modeling are the principal research techniques used. Studies on actin have been directed toward investigating the mechanisms involved in actin polymerization and the interaction of actin with actobindin. Studies on epidermal transglutaminase have involved characterization of proenzyme form and study of the mechanism of activation. Studies on yeast arginase have been directed toward studying the reversible homogeneous association of this enzyme and the role of metal ions in controlling this. Studies on synapsin have involved characterization of the reversible homogeneous association of the various forms of this protein. Studies of various deoxynucleotides have been directed toward investigating the reversible monomer-dimer equilibrium, as a function of structure. Studies on the CMP-N-acetylneuraminic acid synthetase gene have involved determination of the nucleotide sequence in the gene and study of some of the physical properties of the encoded enzyme.