G. Marius Clore - Biography#

Clore is a British/American biophysicist internationally recognized for his pioneering research on the development of NMR for the structure determination of proteins and their complexes in solution, and his recent ground-breaking discovery of the use of paramagnetic relaxation enhancement and other NMR relaxation-based methods to visualize and probe sparsely-populated regions of the free energy landscape of biological complexes that are inaccessible to conventional structural and biophysical techniques. The latter represents a major advance in biochemistry and biophysics, and has yielded fundamental insights into weak macromolecular interactions, and the mechanisms whereby the opposing constraints of speed and specificity are optimized in biology.

Clore was born in London, U.K. in 1955 and is currently a dual British/US citizen. He grew up and was educated in London receiving his undergraduate degree (BSc. 1st class honours) in Biochemistry from University College London (1976), his medical degree from University College Hospital Medical School (1979), and his PhD from the MRC National Institute for Medical Research (1982).

Clore's recent research has focused on fundamental questions associated with protein dynamics, interactions and recognition processes, especially those involved in signal transduction and transcription. A recent example is the structural description of the search by a transcription factor for its specific DNA binding site through a sea of non-specific DNA, a problem studied since the 1980’s but never adequately resolved. Clore provided the first direct experimental demonstration of a protein either sliding along the major groove of DNA or hopping from one DNA duplex to another. A less familiar but analogous example is that when two proteins bind, they initially form a non-specific interaction in what is called an encounter complex, followed by a search for the final state. This process is similar to the search problem in protein-DNA binding but not as well known, although it had been theoretically predicted, because encounter complexes had not previously been observed for any system experimentally. Clore's experiments have revolutionized our understanding of protein interactions by visualizing the detailed structural pathway that lead to the formation of a specifically-bound complex.
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