Our research focuses on the mechanism behind protein recognition and proteins aggregation. Methods of high-resolution nuclear magnetic resonance (NMR) spectroscopy in conjunction with other biophysical methods, computer algorithms and molecular biology 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.