This site documents my work on the computational and structural analysis of putative venom ADP-ribosyltransferases (ARTs), with a focus on understanding their catalytic features, structural conservation, and potential functional roles.
My research integrates protein sequence analysis, structural modeling, and active-site characterization to evaluate whether these venom-derived proteins retain ART-like enzymatic properties. Using tools such as AlphaFold structure prediction, structural alignment, motif analysis, and cavity identification, I examine how conserved catalytic elements—such as NAD⁺-binding motifs and putative active-site residues—are preserved or altered across venom proteins compared to canonical ARTs.
This blog includes research progress updates, figures from structural analyses, conference posters, and presentations, providing an overview of both my computational workflow and the biological insights gained throughout the project. The goal of this work is to better understand how venom proteins may evolve enzymatic activity and how structural divergence can inform function.