Our laboratory works at the interface of chemistry and biochemistry. We apply chemical and biochemical principles and techniques to the problems of protein structure/function as well as to elucidate the chemical mechanisms of several key enzymes, some of which have medical importance. Organic chemistry (organic synthesis of novel biophysical probes and enzyme inhibitors and protein chemical modification techniques), physical chemistry and molecular modeling are being applied to complex protein structures. We make use of biochemical techniques such as recombinant DNA methodologies (PCR, site-directed mutagenesis, protein engineering, etc), microbiology (for protein expression) and protein purification. Protein characterization includes a number of biophysical techniques such as circular dichroism, 19F nuclear magnetic resonance, enzyme kinetics and inhibition studies, and differential scanning and isothermal titration calorimetry among other techniques. In collaboration with other scientists, we also utilize electron paramagnetic resonance, extended x-ray absorption fine structure (EXAFS) and protein crystallography in our studies. In essence, our group employs a variety of techniques to explore biochemistry from a molecular perspective.
Knowledge of an enzyme's catalytic mechanism can be of fundamental importance as well as a critical factor in the design and synthesis of inhibitors having therapeutic potential. A current area of focus is the biological chemistry of the carbon-sulfur bond as it relates to the amino acid methionine and its biochemical function in proteins as well as the study of the enzyme glyoxalase I, a detoxification metalloenzyme that utilizes a sulfur-containing cofactor, glutathione. A recent interest is in the area of bionanotechnology and the application of biological chemistry to the area of nanotechnology.