MIT professor of chemistry and head of the Francis Bitter Magnet Laboratory (FBML) Robert Griffin will receive the E. Bright Wilson Award in Spectroscopy at the spring awards symposium of the American Chemical Society (ACS) Division of Physical Chemistry. Griffin is being honored for his pioneering contributions to the field of nuclear magnetic resonance (NMR) spectroscopy.
In May of 1970, Griffin arrived at MIT as a postdoc in John Waugh’s laboratory, and two years later, in September 1972, he joined the Francis Bitter Magnet Laboratory. His research interests are focused on the structure of membranes, membrane proteins and amyloid proteins, which are not well understood. In addition, he is interested in developing new forms of spectroscopy and instrumentation that can determine structures when standard techniques and instrumentation fail. Accordingly, Griffin and his colleagues developed a new class of high-resolution magic angle spinning NMR methods, dipolar recoupling, to measure distances and torsion angles between atoms in molecules of a solid. The experiments led to some of the initial very high resolution NMR structures of solid proteins.
In later experiments Griffin developed approaches to perform high-frequency dynamic nuclear polarization (DNP) using gyrotron microwave sources and designer polarizing agents, developed together with Department of Physics senior scientist and Plasma Science and Fusion Center Associate Director Rick Temkin and Department of Chemistry Professor Tim Swager. DNP transfers the large polarization in an electron spin reservoir to nuclei and increases the sensitivity of NMR experiments by factors of greater than ε > 100. This means the time it takes to perform an experiment decreases by a factor of 10,000. Using DNP with ε = 100, an NMR experiment that would normally require signal averaging for 27 years can be completed in a day. Commercial instrumentation for DNP experiments is now available from Bruker BioSpin.
Griffin’s experiments have allowed him and others to examine structures of, among other things, membrane transport proteins and amyloid fibrils, which are associated with Parkinson’s disease, type 2 diabetes and Alzheimer’s disease. Fully understanding the structure of such proteins can lead researchers to create the kinds of drugs that will effectively manage or eliminate such diseases.
Named after the American chemist who pioneered methods of using infrared and microwave spectroscopy to determine molecular structure, the E. Bright Wilson Award recognizes outstanding accomplishments in fundamental or applied spectroscopy in chemistry. Griffin will receive the award at the March American Chemical Society National Meeting and Exposition, where he will give the Wilson Lecture. Of the 20 recipients since 1997, Griffin is only the second NMR researcher to receive the award.