Abstract

In a hangar-style space draped in dim blue light stand seven tall, cylindrical machines. The machines, NMR spectrometers, resemble wingless man-made satellites. Most of them rest at floor level, with a sample loading port reached by a small staircase, but a few protrude above the floor. Marius Clore. Image courtesy of Marius Clore. NMR spectrometers operate at the atomic level, and the size of a spectrometer reflects the strength of its superconducting magnets. By exploiting the magnetic fields of atomic nuclei and using high-pulse radio waves, NMR spectrometers help researchers like Marius Clore, a molecular biophysicist and structural biologist at the National Institute of Diabetes and Digestive and Kidney Diseases at the NIH in Bethesda, Maryland, determine the structure and dynamics of molecules such as proteins and nucleic acids. For nearly four decades, Clore, elected to the National Academy of Sciences (NAS) in 2014, has studied the molecular structure and dynamics of biological macromolecules, and spearheaded the development and refinement of biomolecular NMR. Through work carried out in three countries on two continents, he has pushed the limits of NMR technology, laying the foundation for 3D and 4D NMR techniques and ushering in discoveries such as the high-resolution, 3D structure of the immune modulator interleukin-1β. However, Clore’s path to NMR was not straightforward. Clore grew up in the Chelsea area of central London during the 1960s. Along with his mother and father, a film producer who worked on the 1981 film The French Lieutenant’s Woman , which starred actress Meryl Streep, Clore lived in a two-story apartment near the home field of Chelsea Football Club. Around the age of five years, Clore, who started attending the French Lycee school in London, already knew what he wanted to do when he grew up. “I was a little bit of a hypochondriac,” …

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