David P. Goldenberg, PhD

Prof. Goldenberg has been a faculty member at the University of Utah since 1985. He received an A.B. degree, with majors in chemistry and mathematics, from Whitman College and his Ph.D. in biology from the Massachusetts Institute of Technology. His research interests lie at the intersections of biology, chemistry and physics, particularly in the areas of protein folding, structure, dynamics and function. The courses that he teaches, at both the undergraduate and graduate levels, are similarly interdisciplinary. In addition to research publications, he has recently published "Principles of NMR Spectroscopy: An Illustrated Guide" (University Science Books), a text book for advanced undergraduates and graduate students. He has served on the Executive Committee of the Protein Society, the Board of Directors of the Federation of American Societies of Experimental Biology (FASEB) and on grant review panels for the National Science Foundation and the National Institutes of Health.

Research Statement

The long-range goal of my research is to understand the role of protein dynamics in determining the stabilities of protein structures, the specificity of their formation and their functional properties. Our current efforts are focused on two aspects of protein dynamics. The first is the characterization of unfolded proteins, which are now recognized to play important roles in vivo. We are particularly interested in determining how the properties of unfolded proteins change in response to solution conditions and the presence of high concentrations of other macromolecules, as found intracellularly. The second focus of our work is the interaction between a protease, trypsin, and a natural inhibitor of this enzyme, bovine pancreatic trypsin inhibitor (BPTI). BPTI is a member of a large class of natural protease inhibitors that act by binding to the active sites of their targets, much as a substrate would, but are resistant to hydrolysis. We believe that the rigidity of the enzyme-inhibitor complex is key to preventing the catalytic reaction, and we are currently using NMR spectroscopy, thermodynamic and kinetic measurements and x-ray crystallography to learn more about the factors that determine flexibility in the context of an enzyme-substrate complex and about the nature of the motions that are necessary for catalytic function.

Selected Publications