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Frederic Middlebrook Richards, commonly referred to as Fred Richards, was an American biochemist and biophysicist known for solving the pioneering crystal structure of the ribonuclease S enzyme in 1967 and for defining the concept of solvent-accessible surface. He contributed many key experimental and theoretical results and developed new methods, garnering over 20,000 journal citations in several quite distinct research areas. In addition to the protein crystallography and biochemistry of ribonuclease S, these included solvent accessibility and internal packing of proteins, the first side-chain rotamer library, high-pressure crystallography, new types of chemical tags such as biotin/avidin, the nuclear magnetic resonance chemical shift index, and structural and biophysical characterization of the effects of mutations.
Richards spent his entire academic research career at Yale University, where he became Sterling Professor of Molecular Biophysics and Biochemistry in the department that he created and chaired, "one of the major centers in the world for the study of biophysics and structural biology". He was elected to the National Academy of Sciences USA and the American Academy of Arts and Sciences, and received many other scientific awards. He served as head of the Jane Coffin Childs Memorial Fund for Medical Research and was elected as president both of the American Society for Biochemistry and Molecular Biology and of the Biophysical Society.
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