About the Speaker:

Bio:

B.S., 1988, University of Rochester

C.P.G.S., 1989, University of Cambridge

Ph.D., 1997, Caltech

ACS Postdoctoral Fellow, 1996-98, MIT

Research Interests:

The Mueller group is pioneering the development and application of NMR crystallography – the synergistic combination of solid-state NMR, X-ray crystallography, and computational chemistry – to enzyme active sites, where it provides atomic-resolution characterization of stable intermediates as well as species near transitions states. Enabling this is the ability to measure active-site isotropic and anisotropic NMR chemical shifts under conditions of active catalysis, and the development of fully quantum mechanical computational models of the enzyme active site that allow the accurate prediction of NMR spectral parameters.

About the Colloquium:

Title:

NMR Crystallography: An Atomic-Resolution Probe of Structure and Mechanism in the Molecular Sciences

Abstract:

NMR crystallography – the synergistic application of solid-state NMR, X-ray diffraction, and first- principles computational chemistry – is developing as an atomic-resolution probe of structure and function across the molecular sciences. Here, I will discuss the integrative foundation of this approach and present two recent examples from our work that highlight this development. The first is to photomechanical materials, connecting the molecular-level structural rearrangement to the experimentally-observed macroscopic expansion of an anthracene ester nanorods [1]. The second is to structural biology, revealing chemically-detailed structure and dynamics in the enzyme active site of tryptophan synthase, and how this has changed our understanding of its mechanism and reaction specificity [2,3].
[1] Chemical Science (2021) 12, 453-463
[2] PNAS (2022) 119, e2109235119
[3] PNAS (2022) 119, e2114690119