Event

Title: Capturing time-dependent biomolecular structure changes with novel magnetic resonance methods

Abstract: Understanding in detail the mechanisms by which biological molecules undergo structural changes is of central concern to modern biophysical science. Elucidating the molecular processes that drive protein folding, complex formation, and enzyme activity will benefit from new experimental methods that combine atomic spatial resolution with millisecond-to-microsecond time resolution. I will describe a new set of techniques for initiating structural conversion processes by sudden “inverse temperature jumps” carried out by rapidly cooling solutions from 95 °C, where biomolecules are disordered, to physiological temperatures, where ordered structures are thermodynamically favored. Thermally triggered molecular rearrangements are then captured with millisecond or better time resolution by rapidly freezing the solution after a variable evolution time and using solid-state nuclear magnetic resonance (ssNMR) to extract structural information from frozen particles. Time-resolved ssNMR with rapid inverse temperature jumps provides new insights into protein folding and biomolecular complex formation, with applications to antimicrobial peptides, liquid-liquid phase separation, and ultra-fast folding proteins.

Bio: Blake Wilson is a postdoctoral researcher at the National Institute of Diabetes and Digestive Kidney Diseases (NIDDK) at the National Institutes of Health in Bethesda, Maryland. He obtained his BSc in Physics from the Massachusetts Institute of Technology in 2013, where he worked with Bob Griffin on instruments for dynamic nuclear polarization (DNP) enhanced solid-state nuclear magnetic resonance (ssNMR) experiments. He obtained his PhD in Physics from the University of California, Santa Barbara, where he was jointly advised by Mark Sherwin (Department of Physics) and Songi Han (Department of Chemistry and Biochemistry). During his PhD, Blake developed electron paramagnetic resonance (EPR) spectroscopy at high magnetic fields using a free electron laser as an ultra-high power microwave source to study transition metal complexes, nonlinear dynamics in strongly coupled electron spin systems, antiferromagnetic spintronics, and membrane protein dynamics. Blake’s postdoctoral research focuses on developing and applying time-resolved ssNMR techniques to study protein folding, biomolecular complex formation, and liquid-liquid phase separation with the goal of understanding molecular mechanisms important for human health.