Frederic M. Richards

Frederic Middlebrook Richards (born c. 1925) or commonly referred to as Fred Richards is Sterling Professor Emeritus of Molecular Biophysics and Biochemistry at Yale University

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Richards most notable accomplishment was when through a simple experiment, he changed the current view that proteins were colloids into the modern view that proteins are well-ordered structures. The experiment was performed on Dec 7, 1957 involving the protein Ribonuclease A (RNase A). Using a particular protease, RNase A breaks into two parts called: RNase S and the S-protein. Initially, no one could purify the two components without. Richards found that when separated RNase S and the S-peptide had no RNase activity, but when recombined in the test tube the RNase activity is restored.^[1] The conclusion from this experiment shows that proteins maintain order and has thus influenced the idea ligands binding to proteins which used by all pharmicutical companies to design drugs. This result was two years before the protein structure of myoglobin confirmed this.

Along with Hal Wyckoff, the effort to solve the RNase S structure was spearheaded by Fred Richards. RNase S became the third protein structure determined by X-ray diffraction of crystals after myoglobin and lysozyme.

Career summary

• 1948, B.S. Massachusetts Institute of Technology
• 1952, Ph.D. Harvard University
• 1952-1953, Research Fellow, Harvard University
• 1954, NRC Postdoctoral Fellow, Carlsberg Laboratory, Denmark
• 1955, NSF Fellow, Cambridge University, England
• 1955, joined Yale faculty
• 1965, Pfizer--Paul Lewis Award in Enzyme Chemistry
• 1967-1968, Guggenheim Fellow
• 1971, Member, National Academy of Sciences
• 1978, Kai Linderstrom- Lang Prize in Protein Chemistry
• 1988, American Society for Biochemistry and Molecular Biology--Merck Award
• 1988, Protein Society--Stein and Moore Award
• 19xx, Member, American Academy of Arts and Sciences

Important papers

Articles with over 500 citations:

1. B. Lee and F. M. Richards. The interpretation of protein structures: Estimation of static accessibility. J Mol Biol, 55(3):379–400, 1971. doi:10.1016/0022-2836(71)90324-X.
   • Times Cited: 3327
2. F. M. Richards. Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng, 6:151–76, 1977. doi:10.1146/annurev.bb.06.060177.001055
   • Times Cited: 1545
3. Wishart DS, Sykes BD, Richards FM. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol. 1991 Nov 20;222(2):311-33. PubMed
   • Times Cited: 1170
4. Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 1992 Feb 18;31(6):1647-51. PubMed
   • Times Cited: 1167
5. Ponder JW, Richards FM. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J Mol Biol. 1987 Feb 20;193(4):775-91. PubMed
   • Times Cited: 1088
6. Richards FM, Vithayathil PJ. The preparation of subtilisn-modified ribonuclease and the separation of the peptide and protein components. J Biol Chem. 1959 Jun;234(6):1459-65. PubMed
   • Times Cited: 569
7. F. M. Richards. The interpretation of protein structures: total volume, group volume distributions and packing density. J Mol Biol, 82(1):1–14, 1974. doi:10.1016/0022-2836(74)90570-1
   • Times Cited: 544
8. Peters K, Richards FM. Chemical cross-linking: reagents and problems in studies of membrane structure. Annu Rev Biochem. 1977;46:523-51. PubMed
   • Times Cited: 522

References

1. ^ Richards FM. (1958) On the Enzymic Activity of Subtilisin-modified Ribonuclease. PNAS v44(2):pp162--166. PMID 16590160