Abstract: 
The active sites of enzymes involved in protein biosynthesis, such as, aminoacyl tRNA synthetase (aaRS) are ideal examples of catalytic organizations that contain relics of prebiotic evolutionary features. Higher-level structural features are appended during evolution for further diverse functionality. In recent years, the structural organization, and dynamics of active site of aaRSs are investigated at atomistic detail. We present results our computational studies on active sites that reveal structural and dynamical features of aaRSs. AaRS has remarkable specificity and capacity for chiral discrimination. The confinement of the substrates and the orientation dependent interaction between active site and substrate are few key factors which determines the chiral discrimination. These factors are expected to be conserved through evolution for better performance of the canonical functions of the enzymes. We shall also refer to our studies on the biomimetic nano-spaces, monolayers, and bilayers where similar principles driving chiral discrimination are observed. Brief mention shall be made about the similar principles noted in other active sites involved in protein and peptide synthesis. At the end we shall discuss how these principles control drug binding to the active site of aaRS.

Speaker: Dr. Nilashis Nandi, Department of Chemistry, University of Kalyani, India.

Speaker bio: 
Nilashis Nandi received his B.Sc. (Hons.) (1983) and M.Sc. (1985) degrees from North Bengal University and Ph.D. (1992) from Visva Bharati University, India. He was a postdoctoral fellow at the Indian Institute of Science, India (1993-1997), J.S.P.S. postdoctoral fellow at the Nagoya University, Japan (1997-1999) and Alexander von Humboldt postdoctoral fellow at the Max Planck Institute of Colloids and Interfaces, Germany (1999-2000). He was a faculty member in the Birla Institute of Technology and Science, Pilani, India for the period 2001-2007 and joined as Professor in the University of Kalyani in 2008. He is the Fellow of West Bengal Academy of Science and Technology. His research interest is focused on theoretical and computational studies in biophysical chemistry and currently is pursuing to understand structure and dynamics of aminoacyl tRNA synthetases.

Host: Shawn McGlynn, ELSI.

Date: Fri, 5 March, 2021, 15:30-16:30 JST (Fri, 5 March, 06:30-07:30 UTC)

Venue: Online