Leonard Mueller, University of California, Riverside
My group is developing NMR crystallography – the synergistic combination of solid-state NMR, X-ray diffraction, and first-principles computational chemistry – as an atomic-resolution probe of structure and function across the molecular sciences. I will present two examples from our recent work that highlights its development and application. The first connects molecular level structural rearrangement with macroscopic response in the photomechanical expansion of molecular crystal nanorods. The second reveals chemically-rich structure (by which we mean the location of all atoms, including hydrogen) in the enzyme active site of the pyridoxal-5′-phosphate-dependent enzyme tryptophan synthase, and how this has fundamentally changed our understanding of the mechanism are reaction specificity.
Flyer File: mueller_leonard_ccb_flyer.pdf