Lab Activities

Watching Enzyme Structural Dynamics through Solvent Exchange Inhibitor Binding

Our lab uses near field THz microspectroscopy to observe vibrations of atoms in proteins, and provides information about structure and conformation which requires crystallized samples. We are interested in the structural changes of proteins that occur as a result of binding to ligands and inhibitors. I have been working on a method to bind lysozyme crystals to their ligand, 3NAG that can be reproduced experimentally without damaging the crystals, so they can still be measured. Our goal is to eventually use what we know about lysozyme-3NAG binding as a reference to understand the more complex TIM protein and its conformational changes when bound to different molecules. This work is being pursued by our excellent undergraduate BIOLOGY major, Amandine Tirino!  Let's go Amandine!