Ph.D., University of California - Berkeley, 1986
Department of Chemistry and Chemical Biology, School of Arts and Sciences, New Brunswick; Rutgers
Areas of Interest
Nuclear Magnetic Resonance, Protein Folding, Molecular Recognition, Structural Biology.
Grants, Honors, and Awards
Editorial Board for Letters in Peptide Science; Alfred P. Sloan Fellow; Rutgers University Board of Trustees Scholarly Excellence Fellowship; Margaret O. Dayhoff Biophysical Society Award; Camille & Henry Dreyfus Teacher-Scholar Award; Johnson and Johnson Discovery Research Fund; Searle Scholar, Fulford Junior Research Fellow, Oxford University 1986-88; Henry Rutgers Research Fellow.
Academic Interests and Plans
Our research involves the development and application of nuclear magnetic resonance (NMR) spectroscopy to the study of proteins. Methods of high-resolution NMR in conjunction with computer algorithms are used to examine the dynamics and three-dimensional structures of proteins in solution.
One area of interest is to use NMR to understand the manner in which a protein folds from an unstructured state to its final compact globular structure. The study of the folding intermediates may provide a description of the pathways by which this important process occurs. A second area of interest involves protein-protein interactions and molecular recognition in proteins of medical and biological interest. The emphasis of the research is to develop novel NMR methods and apply existing techniques to model peptide and protein systems in order to explore these important problems in biophysical chemistry.