Office: MRB 341
Research Title: Biomolecular Spectroscopy
The major interest of our research group is the elucidation of the structure and function of proteins and nucleic acids by spectroscopic methods. Spectroscopic methods – visible/UV absorption, circu-lar dichroism, fluorescence, NMR, infrared and Raman – have been widely and fruitfully applied to the study of protein and nucleic acid structure and function. Except for high resolution NMR, none of these methods can give the details of a high-resolution X-ray structure, but they have significant advantages in other respects. They can be applied to unordered systems, such as solutions and membranes. In many cases, information about dynamics can be obtained. In favorable cases, spectroscopic methods are more sensitive to one or more specific structural parameters than is X-ray diffraction. Finally, spectroscopic methods generally require less material and a smaller investment in human effort.
Cloning techniques have made many previously scarce proteins and nucleic acids available for study. Moreover, the sequence of these molecules is generally available, but information about their three-dimensional structure is frequently lacking. Site-directed mutagenesis can be applied to readily generate a wide variety of modified proteins, and it is important to characterize these proteins structurally. Our experimental studies are frequently coupled with theoretical calculations using energy minimization, molecular dynamics, and molecular orbital theory. Examples of systems which we have studied include myoglobin, hemoglobin, cytochrome oxidase, MHC proteins, bovine pancreatic trypsin inhibitor, tropomyosin, trypsin inhibitor, acyl carrier protein, RNA polymerase, pectate lyase C, and cytochrome b5.