Robert G. Griffin is a physical chemist recognized for the development of methods to perform high resolution nuclear magnetic resonance (NMR) studies of solids and the application of these methods to chemical and biophysical problems, primarily in membrane proteins and amyloid fibrils. In addition, he developed the instrumentation and methodology to perform high frequency dynamic nuclear polarization in solids, a technique that enhances solid state NMR sensitivity by factors of 102-103 and thus renders a host of problems newly tractable. Griffin was born and raised in Little Rock, Arkansas, and graduated from the University of Arkansas, Fayetteville with honors in chemistry. His PhD in physical chemistry was obtained from Washington University, St. Louis, Missouri and was followed by postdoctoral fellowships in physical chemistry at the Massachusetts Institute of Technology (MIT). His independent work has been carried out at the Francis Bitter Magnet Laboratory at MIT, where he has been the director since 1992. In 1988 he joined the faculty of the MIT Chemistry Department where he is Arthur Amos Noyes Professor and teaches physical chemistry. He is a member of the American Academy of Arts and Sciences and theNational Academy of Sciences.

Research Interests

Robert Griffin's laboratory is interested in the development and application of methods to determine the structure and function of membrane and amyloid proteins via high resolution magic angle spinning (MAS) nuclear magnetic resonance (NMR) spectroscopy with dynamic nuclear polarization (DNP). Initially, his lab developed a suite of dipole recoupling techniques to measure internuclear distances that reported structural changes in the photocycle intermediates of the transmembrane, light-driven ion pump bacteriorhodopsin (bR). However, it became clear that the low sensitivity of MAS NMR severely limited the detection of interesting signals. This motivated the development of the high frequency gyrotron microwave sources required for DNP at the high magnetic fields used in MAS NMR of macromolecules. With DNP it is possible to increase the sensitivity of NMR by a factor of 102-103 which enables studies that were otherwise impossible. For example, it is now feasible to examine species in the bR photocycle when they are present at the 5% level. In other applications, DNP-enhanced MAS NMR has been used to determine the structure of the membrane protein M218-60 from influenza-A, the structure of fibrils of Ab1-42, the toxic species in Alzheimer's disease, and of b2-microglobulin associated with dialysis related amyloidosis.

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Primary Section

Section 29: Biophysics and Computational Biology

Secondary Section

Section 14: Chemistry