Using genetically engineered derivatives and a wide range of chemical and physical methods, the contributions of specific domains and selected amino acid residues to the functional properties of these proteins are being explored. The specific proteins currently under investigation are the lactose repressor protein, a prototypic negative regulatory protein from E. coli, and Ultrabithorax, a homeodomain protein essntial for segmental identity during development in Drosophila. Two of these proteins, ubiquinol cytochrome c oxidoreductase and cytochrome oxidase, are the primary targets of study. The methods employed are primarily spectroscopic and kinetic to determine transient states of these enzymes and to construct the electron and proton translocation reactions. Dr. Phillips's laboratory examines three-dimensional structure and dynamics of biomolecules and relates these properties to function.
Emphasis is on the molecular mechanisms involved in the regulation of muscle contraction.
The specific proteins involved in the regulatory process under study are tropomyosin, actin, and troponin. In addition to application of x-ray crystallographic techniques to the study of this important system, theoretical analysis and development of other diffraction methods provide additional insights into the modes of action of these proteins. The goal of Dr. Nikonowicz's laboratory is to obtain a better understanding of the structure-function relationships underlying biologically relevant nucleic acid systems using heteronuclear nuclear magnetic resonance spectroscopy and a variety of computational methods.