Dr. Prem Ramasamy, completed his Ph.D. in Biophysics with specialization in structural biology from All India Institute of Medical Sciences (AIIMS), New Delhi, India and working as a Postdoctoral Associate at the Department of Biochemistry, Brandeis University, Waltham, MA, USA. He is on the editorial board of European Journal of Medicinal Plants, Der Pharmacia Sinica, Asian Journal of Pharmaceutical Research and Health Care, and Advance research in Pharmaceuticals & Biologicals and also serving on reviewer panel of many peer-reviewed journals including Protein Science, Acta Cryst Sect. F, Frontiers journals, Molecular and Cellular Biochemistry. 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.

Terpene synthase: Prem Ramasamy is working on to characterize the structure and enantiomer selection mechanism of the limonene synthase, a monoterpene cyclase from the navel orange, and trying to identify the enzyme’s reaction intermediates in the catalytic pathway. 

Vision pathway: Prem Ramasamy is studying several of the proteins involved in visual phototransduction. His work focuses on the calcium-dependent interaction between recoverin and rhodopsin kinase, which delays termination of the visual signal by phosphorylation of rhodopsin. More recently, he is also working on two fungal opsins that are naturally fused to either a guanylyl cyclase or phosphodiesterase and modulate the phototransduction-signaling cascade.