Frederic M. Richards
Encyclopedia
Frederic Middlebrook Richards (c. 1925 – January 11, 2009), or commonly referred to as Fred Richards, was Sterling Professor
Emeritus
of Molecular Biophysics and Biochemistry at Yale University
.
s 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 (Subtilisin), RNase A was converted into a split protein (RNase S), which is composed of two parts called S-peptide and S-protein. Initially, no one could purify the two components. Richards found that, when separated, S-protein and S-peptide had no RNase activity, but, when recombined in the test tube, the RNase activity is restored. The conclusion from this experiment shows that proteins maintain order and has thus influenced the idea ligands binding to proteins which used by all pharmaceutical 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
.
Sterling Professor
A Sterling Professorship is the highest academic rank at Yale University, awarded to a tenured faculty member considered one of the best in his or her field...
Emeritus
Emeritus
Emeritus is a post-positive adjective that is used to designate a retired professor, bishop, or other professional or as a title. The female equivalent emerita is also sometimes used.-History:...
of Molecular Biophysics and Biochemistry at Yale University
Yale University
Yale University is a private, Ivy League university located in New Haven, Connecticut, United States. Founded in 1701 in the Colony of Connecticut, the university is the third-oldest institution of higher education in the United States...
.
Biography
Richards' most notable accomplishment was when through a simple experiment, he changed the current view that proteinProtein
Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. A polypeptide is a single linear polymer chain of amino acids bonded together by peptide bonds between the carboxyl and amino groups of...
s 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
Ribonuclease A
Ribonuclease A is a pancreatic ribonuclease that cleaves single-stranded RNA. Bovine pancreatic RNase A is one of the classic model systems of protein science.-History:...
(RNase A). Using a particular protease (Subtilisin), RNase A was converted into a split protein (RNase S), which is composed of two parts called S-peptide and S-protein. Initially, no one could purify the two components. Richards found that, when separated, S-protein and S-peptide had no RNase activity, but, when recombined in the test tube, the RNase activity is restored. The conclusion from this experiment shows that proteins maintain order and has thus influenced the idea ligands binding to proteins which used by all pharmaceutical companies to design drugs. This result was two years before the protein structure of myoglobin
Myoglobin
Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the...
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
Myoglobin
Myoglobin is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the...
and lysozyme
Lysozyme
Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases, enzymes that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between...
.
Career summary
- 1948, B.S. Massachusetts Institute of TechnologyMassachusetts Institute of TechnologyThe Massachusetts Institute of Technology is a private research university located in Cambridge, Massachusetts. MIT has five schools and one college, containing a total of 32 academic departments, with a strong emphasis on scientific and technological education and research.Founded in 1861 in...
- 1952, Ph.D. Harvard UniversityHarvard UniversityHarvard University is a private Ivy League university located in Cambridge, Massachusetts, United States, established in 1636 by the Massachusetts legislature. Harvard is the oldest institution of higher learning in the United States and the first corporation chartered in the country...
- 1952-1953, Research Fellow, Harvard University
- 1954, NRC Postdoctoral Fellow, Carlsberg LaboratoryCarlsberg LaboratoryThe Carlsberg Laboratory in Copenhagen, Denmark was created in 1875 by J. C. Jacobsen, the founder of the Carlsberg brewery, for the sake of advancing biochemical knowledge, especially relating to brewing. It featured a Department of Chemistry and a Department of Physiology...
, Denmark - 1955, NSF Fellow, Cambridge University, England
- 1955, joined YaleYale UniversityYale University is a private, Ivy League university located in New Haven, Connecticut, United States. Founded in 1701 in the Colony of Connecticut, the university is the third-oldest institution of higher education in the United States...
faculty - 1965, PfizerPfizerPfizer, Inc. is an American multinational pharmaceutical corporation. The company is based in New York City, New York with its research headquarters in Groton, Connecticut, United States...
--Paul Lewis Award in Enzyme Chemistry - 1967-1968, Guggenheim Fellow
- 1971, Member, National Academy of SciencesUnited States National Academy of SciencesThe National Academy of Sciences is a corporation in the United States whose members serve pro bono as "advisers to the nation on science, engineering, and medicine." As a national academy, new members of the organization are elected annually by current members, based on their distinguished and...
- 1978, Kai Linderstrom- Lang Prize in Protein Chemistry
- 1988, American Society for Biochemistry and Molecular Biology--MerckMerck & Co.Merck & Co., Inc. , also known as Merck Sharp & Dohme or MSD outside the United States and Canada, is one of the largest pharmaceutical companies in the world. The Merck headquarters is located in Whitehouse Station, New Jersey, an unincorporated area in Readington Township...
Award - 1988, Protein Society—Stein and Moore Award
- 1995, Connecticut Medal of Science
- 19xx, Member, American Academy of Arts and SciencesAmerican Academy of Arts and SciencesThe American Academy of Arts and Sciences is an independent policy research center that conducts multidisciplinary studies of complex and emerging problems. The Academy’s elected members are leaders in the academic disciplines, the arts, business, and public affairs.James Bowdoin, John Adams, and...
Important papers
Articles with over 500 citations:- B. Lee and F. M. Richards. The interpretation of protein structures: Estimation of static accessibility. J Mol Biol, 55(3):379–400, 1971. .
- Times Cited: 3327
- F. M. Richards. Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng, 6:151–76, 1977.
- Times Cited: 1545
- 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.
- Times Cited: 1170
- 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.
- Times Cited: 1167
- 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.
- Times Cited: 1088
- 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.
- Times Cited: 569
- F. M. Richards. The interpretation of protein structures: total volume, group volume distributions and packing density. J Mol Biol, 82(1):1–14, 1974.
- Times Cited: 544
- Peters K, Richards FM. Chemical cross-linking: reagents and problems in studies of membrane structure. Annu Rev Biochem. 1977;46:523-51.
- Times Cited: 522
External links
- Richards profile at Yale UniversityYale UniversityYale University is a private, Ivy League university located in New Haven, Connecticut, United States. Founded in 1701 in the Colony of Connecticut, the university is the third-oldest institution of higher education in the United States...