The seminar will take place, the 16th of June, at 16h, at the ENSCBP amphitheater, Building B, allée Geoffroy Saint-Hilaire, Pessac.
Ayyalusamy (Rams) Ramamoorthy, professor
Biophysics and Department of Chemistry, University of Michigan, Ann Arbor MI 48109
In spite of recent developments in structural biology, membrane proteins continue to pose tremendous challenges to most biophysical techniques. High-resolution structure determination of single-pass transmembrane proteins is even more challenging as they exhibit dynamically disordered structural folds that are not suitable for studies by most biophysical techniques. My group has been developing NMR methods and membrane mimetics such as nanodiscs and bicelles consisting of bulk water that enable native structural folding of single-pass transmembrane cytochrome proteins (cytochrome b5, cytochrome P450 and cytochrome P450-reductase) to measure dynamic structures, protein-protein interactions, and protein-membrane interactions under physiological conditions. High-resolution experimental results obtained from lipid bilayers containing full-length functional complexes of cytochrome-P450 and its redox partners will be presented. In the second-half of my talk, I will present atomistic resolution structures of amyloidogenic proteins (implicated in Alzheimer’s Disease and Type-2 diabetes) revealing the misfolding pathways and early intermediates that play key roles in amyloid toxicity.
Zhang et al. Angew. Chem. Int. Ed. Engl.,55, 4497-4499 (2016); Zhang et al. J. Biol. Chem., 290, 12705-12718 (2015); Ahuja et al., J. Biol. Chem., 288, 22080-22095 (2013); Brender et al., Acc. Chem. Res.116, 3650 (2012); Kotler et al., Chem. Soc. Rev. 43, 6692-6700 (2014).
Ayyalusamy Ramamoorthy, Ph.D., is a Professor of Chemistry and Biophysics at the University of Michigan, Ann Arbor. He graduated from the Indian Institute of Technology, India, with a Ph.D in Chemistry in 1990. He worked as Scientist in a National Lab in India from 1989 to 1992, and worked for JEOL Ltd in Tokyo as a Scientist from 1992 to 1993. He then moved to the United States to work as a Research Associate in the NIH Biological NMR center at the University of Pennsylvania, Philadelphia (1993-1996). Dr. Ramamoorthy is a winner of the CAREER development award from NSF, Young Scientist Award from JEOL, Research Partnership Award from Eli Lilly, and a Grant-in-Aid Award from American Heart Association. He has more than 115 peer-reviewed publications, several chapters in books, and edited two books and several special issues. Over the past 12 years, Dr. Ramamoorthy¹s studies have focused on the atomistic-level high-resolution imaging of membrane-associated peptides and proteins that play important roles in diabetes, Alzheimer¹s disease, cancer, and heart diseases. Research projects in his lab utilize a variety of biophysical techniques including sophisticated NMR spectroscopy experiments.
Research interests: Our research interests involve the structure, dynamics, and function of macromolecules such as membrane-associated peptides/proteins, nanomedicine and polymorphic pharmaceutical compounds. Specific biological systems that are presently being investigated are cytochrome-b5, cytochrome-P450, membrane-disruptive peptides (such as antimicrobial peptides, amyloid peptides, and HIV fusion peptide), dendrimers, and other nanomaterials. We use a variety of biophysical techniques (but mainly solid-state NMR spectroscopy) to investigate these nano-biological systems at atomistic-level resolution.
Our expertise in applying a variety of biophysical techniques (but mainly solid-state NMR spectroscopy) to investigate these nano-biological systems at atomistic-level resolution has been a great advantage in the investigation of nanomedicines like dendrimers and their derivatives.