Ashish Sethi

I am a structural biologist who is passionate about studying protein structures and dynamics primarily using solution NMR. My current interests are in the molecular mechanism of activation of G-protein coupled receptors, especially the Relaxin Family Peptide Receptor (RXFP1 and RXFP2), and the structure and function of lyssavirus (rabies) proteins, particularly the intrinsically disordered P-protein and its role in suppressing the innate immune response. I have expertise in the recombinant production of proteins in bacterial cells and apply solution NMR techniques to understand how proteins work focusing on defining ligand binding sites and understanding the conformational changes that occur on ligand binding. I have also optimised/developed new methods for quick data acquisition in NMR, which is extremely useful in working with proteins that have poor solubility and critical stability in solution. I was awarded the Bill Sawyer Medal by Department of Biochemistry and Molecular Biology, the University of Melbourne for the outstanding research achievements in my PhD candidature in 2016. I was an invited speaker at Australia & New Zealand Magnetic Resonance Society Conference (ANZMAG) in 2015 and 2017. During my PhD, I also received the Best Student Poster Prize at two international conferences in 2013 and 2014 and the best oral presentation award at the Department of Biochemistry and Molecular Biology graduate retreat in 2015. Recently I have applied Small X-ray Scattering (SAXS) technique to solve the structures of proteins from relaxin peptide family and also determined the structure of rabies virus phosphoprotein and its five different isoforms.