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Robert W Parry Collegiate Professor of Chemistry and Biophysics
Office Location(s): 4533 Chemistry
Ramamoorthy Research Group Home Page
Membrane proteins act as enzymes, regulate transport processes, and play a central role in intercellular communication. In order to understand the diverse functions of membrane proteins and to engineer these functions for biomedical or biotechnological purposes, it is necessary to determine their high-resolution structure and to describe their dynamics. Structure determination of membrane proteins continues to be one of the most important and challenging aspects of science at the present time. Recent developments in solid-state NMR spectroscopy have shown that it is an ideal technique for immobile and non-crystalline proteins that are difficult to study by X-ray crystallography or by solution NMR. The development of solid-state NMR methods and their applications to determine the structure, folding and dynamics of membrane proteins are the main goals of the research program. Solid-state NMR experiments on membrane proteins incorporated in oriented and unoriented phospholipid bilayers are performed to determine the structure of membrane proteins. Peptide antibiotics, human apolipoprotein, cytochrome b5, viral protein, functional fragments of GABA receptors, and amyloidogenic peptides are some of the systems currently under investigation by this group. High-resolution details on the membrane interaction of nanomedicine (or drug delivery), polymorphism of pharmaceutical compounds, and metabalomics are also being investigated using solid-state NMR experiments. We are also interested in studying protein-ligand (protein, peptide, or drug) interactions using a variety of biophysical techniques (CD, DSC, ITC, fluorescence, NMR and AFM).
Chemistry BuildingRoom 4028930 N. University Ave.
Ann Arbor, MI