This is a PYI award. Dr. LeMaster is studying the protein, dienelactone hydrolase whose X-ray analysis has recently been carried out. The combination of solution and crystalline structural analyses will prove useful for studying the enzymatic properties of this protein which plays an important role in the ecological detoxification of chloroaromatics. By means of nuclear magnetic resonance spectroscopy the ionization state and conformation of the active site residues of the enzyme can be monitored in the presence and absence of substrate analogs as a means of gaining a better understanding of the mechanistic properties of this important class of enzymes. High resolution nuclear magnetic resonance spectroscopy has begun to provide solution structures of small proteins. This technique offers an important complement to X-ray crystallography in structural analysis in that macromolecules can be studied under conditions more closely approximating the physiological milieu. This will prove particularly advantageous in studying association reactions such as protein-peptide and protein-nucleic acid complexes for which X-ray analysis has met with only partial success.
