Leighton Coates

TL;DR: The room temperature X-ray structure of unliganded SARS-CoV-2 3CL Mpro is reported, revealing the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature, which suggests that the room temperature structure may provide more relevant information at physiological temperatures for aiding in molecular docking studies.

TL;DR: All eight enzymes required for de novo heme biosynthesis have been predicted from the nuclear genome of the human malaria parasite Plasmodium falciparum using a GFP reporter in live transfected parasites to study the subcellular localization of three of them.

TL;DR: A supercomputer-driven pipeline for in silico drug discovery using enhanced sampling molecular dynamics (MD) and ensemble docking is presented, including the use of quantum mechanical, machine learning, and artificial intelligence methods to cluster MD trajectories and rescore docking poses.

TL;DR: Both neutron and X-ray diffraction data have been used to investigate the transition state of the aspartic proteinase endothiapepsin, revealing the clearest picture yet of the catalytic mechanism by which the enzyme operates.

TL;DR: The objective was to locate crucial protons at the active site of an inhibitor complex since this will have major implications for a detailed understanding of the mechanism of action of aspartic proteinases.