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NIH Honors Davies with a Day of Science

By Sharon Ricks

On the Front Page...
"When one discusses the three-dimensional shape of a protein at NIH, three things immediately come to mind: the first is excellence, the second is NIDDK, and the third is David Davies," remarked NIDDK director Dr. Phillip Gorden, launching an all-day symposium titled, "Structural Thinking in Molecular Biology." "They don't necessarily have to be in that order, but they are inextricably linked."

Continued...
The symposium honored Dr. David R. Davies, chief of the molecular structure section in NIDDK's Laboratory of Molecular Biology, for 42 years of contributions to the study of structural biology at NIH. "What defines a scientist who actually moves a field rather than makes a contribution?" asked Gorden. "I really don't know. I suspect that during David's formative period at Oxford, he did not have any great insight or focus. He simply looked around at his classmates like Margaret Thatcher and decided that to be a consistent winner, it was better to be a crystallographer than a politician."

NIDDK Director Dr. Phillip Gorden (l) greets Day of Science honoree Dr. David Davies.

Speakers from the University of Oregon, MIT, NIDDK, Stanford Medical Center, NCI, Yale and Cambridge, and more than 200 colleagues gathered in Wilson Hall to share insights on protein structure and its inextricable link with Davies' career.

Nobel Laureate Max Perutz traced the history of protein structure back to 1934, when scientists learned that protein crystals produce x-ray diffraction. "I showed x-ray pictures to my friends," said Perutz. "But when they asked me what they meant, I changed the subject. We didn't know anything about proteins except that they are made of amino acid chains, so anything that we could squeeze out with x-ray crystallography was great!" Perutz said he visits Davies every 2 or 3 years, and always learns something new.

Nobel Laureate Max Perutz traces the history of protein structure back to 1934.

Dr. Brian Matthews, a Howard Hughes professor at the University of Oregon and one of Davies' former postdocs, shared some new information on proteins. In a recent study, he found that the core sites of an average protein are much more important than the surface sites. NCI's Dr. Michael Potter described the history of the McPC603 protein that Davies crystallized and solved, and NIDDK's Dr. Gary Felsenfeld discussed chromatin structure.

At the conclusion, a colleague presented Davies with a banner that read, "F.D.R. triplex 1957-1997." According to Felsenfeld, he, Davies and Dr. Alexander Rich discovered the first three-stranded helical nucleic acid molecule in the late 1950's. The F.D.R. triplex stands for Felsenfeld, Davies and Rich.

Banner Day: Dr. Gary Felsenfeld (r), Davies (c) and Dr. Alexander Rich, who together discovered the first three-stranded helical nucleic acid molecule in the late 1950's, gather following the symposium.

Davies graduated from Oxford University in 1949 and received a Ph.D. in 1952. In 1955, he joined NIMH and moved to NIDDK 6 years later. His research uses x-ray crystallography to determine the three-dimensional structure of proteins and nucleic acids.

At the symposium, NIDDK's Dr. William Eaton proclaimed Davies as the father of structural biology at NIH. Eaton said Davies was a major force in establishing seven different groups in protein crystallography and noted Davies' role in the development of the field of structural nuclear magnetic resonance.

"The most remarkable thing about David is the consistent excitement that he brings to science and that science brings to him," Gorden remarked. "If David were Scottish rather than Welsh, we would surely clone him."


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