Samuel Krimm
American biophysicist
From Wikipedia, the free encyclopedia
Samuel Krimm (born October 19, 1925) is an American physicist with a research focus in biophysics (spectroscopy, macromolecules, protein folding). He is professor emeritus and research scientist emeritus at University of Michigan.[3][4]
- Polytechnic Institute of Brooklyn (1947)
- Princeton University (1949, 1950)
- APS Fellow (1959)
- APS Polymer Physics Prize (1977)
- Humboldt Prize (1983)
Samuel Krimm | |
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| Born | October 19, 1925[1] |
| Alma mater |
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| Awards |
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| Scientific career | |
| Fields | Biophysics |
| Institutions | University of Michigan |
| Doctoral students | Willie Hobbs Moore[2] |
Education
Krimm earned a BS in chemistry, from Polytechnic Institute of Brooklyn (1947), and MS and PhD in physical chemistry from Princeton University (1949, 1950).[5]
Career highlights
Krimm was elected fellow of the American Physical Society in 1959.[6]
In 1977, Krimm received the American Physical Society's Polymer Physics Prize "For his outstanding experimental studies and theoretical developments in infrared and Ra-man spectroscopy and X-ray scattering from natural and synthetic polymers".[6]
In 1983, he was awarded the Humboldt Prize.[7]
From 1967-1972 he was doctoral advisor for Willie Hobbs Moore, who earned the first PhD in physics for an African-American woman at an American university.[2]
He was the first Director of the University of Michigan Program in Protein Structure and Design, created in 1985.[8]
He has published over 300 peer-reviewed articles, on the infrared and Raman spectroscopy of synthetic polymers and proteins, and in the field of theoretical and computational studies of the structures of such macromolecules.[9]
In his most recent work, he and colleague/collaborator Noemi Mirkin have proposed a new paradigm in the field of protein folding they term "milieu folding" demonstrating that the presence of particular molecules in the surrounding aqueous environment of a protein molecule ("milieu") can alter the propensities for the folded structure of the protein. They suggest that this is a more appropriate framework than "misfolding" to explore and understand protein-folding diseases.[10][11]