Sarkarai Nadar joined HWCOM in 2012. His research aims to understand the mechanism of arsenic resistance and detoxification using biophysical methods and X-ray crystallography. He crystallized and solved the three-dimensional structure of ArsI, C-As lyase, a carbon arsenic bond cleaving enzyme from the thermophilic bacterium Thermomonospora curvata and Ars, Arsinothricin N-acetyltransferase from Pseudomonas putida KT2440. The focus of Nadar’s Ph.D. research was to design the DNA oligonucleotide sequences that form a four-way junction, characterize them using various biophysical methods, and find three-dimensional structures using X-ray crystallography.
Protein structures and the structure-function relationship of enzymes involved in arsenic biotransformation Anti-cancer drugs for Trible Negative Breast Cancer (TNBC) using computational methods and consecutive biophysical and biochemical assays