Recommended Conferences

Dr. Prem K. Ramasamy

Dr. Prem K. Ramasamy
Brandeis University, Oprian laboratory, Biochemistry Department, Waltham, MA
 
Biography
Dr. Prem Ramasamy completed his Ph.D. in Biophysics with specialization in structural biology from All India Institute of Medical Sciences (AIIMS), New Delhi and working as a Postdoctoral Associate at the Department of Biochemistry, Brandeis University, USA. He is on the editorial board of European Journal of Medicinal Plants and Asian Journal of Pharmaceutical Research and Health Care and also serving on reviewer panel of many peer-reviewed journals including Frontiers, Molecular and Cellular Biochemistry, PLoS One and Journal of Environmental Biology. He has been working on understanding the mechanism of several different proteins, notably on recoverin, a small calcium ion binding protein in the vertebrate visual system, as well as several terpene synthases, enzymes involved in the committed step in terpene biosynthetic pathways. Recently, he has solved the structure of the guanylyl cyclase domain of a newly discovered rhodopsin-guanylyl cyclase fusion protein from the aquatic fungus Blastocladiela emersonii. This fusion protein is of particular interest because of its use in optogenetic studies. For his doctorate, he was working on structural studies and inhibitor design of various proteins including phospholipase A2, hyaluronidase, and lactoferrin.
 
Research Interest
I am currently working as a postdoctoral associate in the laboratory of Dr. Daniel Oprian at Brandeis University where my research focus is twofold. First, I am working on to characterize the structure and enantiomer selection mechanism of the limonene synthase, a monoterpene from the navel orange. I have established methods to in-crystallo freeze trap the enzymatic reaction intermediates in the catalytic pathway. Second, I study several of the proteins involved in visual phototransduction. My work focuses on the calcium-dependent interaction between recoverin and rhodopsin kinase, which delays termination of the visual signal by phosphorylation of rhodopsin. To this end, I have solved the 20-year-old problem of inability of recoverin to crystallize in the active form with two bound Ca2+ ions. More recently, I am also working on two fungal opsins that are naturally fused to either a guanylyl cyclase or phosphodiesterase and modulate the phototransduction-signaling cascade.
 

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