My research portfolio integrates structural biology, protein engineering, and computational chemistry to address complex biochemical challenges. Currently, as a Research Associate at the University of Bristol, I lead projects focused on engineering horseradish peroxidase (HRP) to enhance its expression and stability in E. coli. For this we re-engineered the HRP sequence using computational tools and testing the predicted sequences in the lab to establish the expression and stability. This involves utilizing rigorous molecular biology techniques and precise biophysical characterization of the modified HRP sequences. I am also working on the understanding of heme peroxidase catalytic cycles by crystallizing reaction intermediates of Cytochrome C, Horseradish peroxidase and Ascorbate peroxidases, utilizing X-ray Free-Electron Lasers (XFEL) and Diffraction data.

Previously, I specialized in synthetic biology, where I designed and synthesized large Designed Helical Repeat (DHR) proteins. Utilizing Golden Gate Assembly and split-inteins, I developed methods for creating covalent protein assemblies. These macromolecular structures were characterized using Small Angle X-ray Scattering (SAXS), alongside other biophysical techniques.

My research foundation was established during my doctoral studies in quantum crystallography and computer-aided drug design (CADD). My thesis work focused on the quantification of hydrogen bonds and interaction energies in proteins. By employing experimental charge density analysis and aspherical refinement methods on X-ray and neutron diffraction data, I developed insights into electrostatic interactions to predict accurate lead structures for ligand screening.