Structure-Function Studies of L-3-Hydorxyacyl Coenzyme A Dehydrogenase, Fumarase and Cytoplasmic Malate Dehydrogenase

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Molecular data and detail are vital factors in understanding biochemical phenomena related to enzymes. Dr. Banaszak is carrying out an X-ray crystallographic study of L-3- hydroxyacyl CoA Dehydrogenase, cytoplasmic malate dehydrogenase (sMDH) and fumarase. Although these structural studies are at different stages, the long range objectives in each case are similar. Structural investigations of the type proposed are fundamental to understanding the mechanism of catalytic activity of enzymes which carry out essential steps in a number of fundamental biochemical pathways. Dr. Gail Rhodes, of the University of South Maine, will spend part of the summer in the laboratory in order to continue model building and refinement studies of the proteins L-3- hydroxyacyl Coenzyme A dehydrogenase and cytoplasmic malate dehydrogenase. This opportunity will enable him to develop a research program related to protein structure at his University where his research interests focus on the molecular structure of proteins, protein model building, structure refinement and the comparison of protein structures.