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For other persons of the same name, see Fred Richards. Fred Richards may refer to Frederic M Richards (b 1925 Sterling Professor Emeritus of Molecular Biophysics and Biochemistry at Yale University

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

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. 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 (ɨˈmɛrɨtəs is an Adjective that is used in the title of a retired Professor, Bishop or other professional Proteins are large Organic compounds made of Amino acids arranged in a linear chain and joined together by Peptide bonds between the Carboxyl A colloid is a type of mechanical Mixture where one substance is dispersed evenly throughout another The experiment was performed on Dec 7, 1957 involving the protein Ribonuclease A (RNase A). Events 43 BC - Marcus Tullius Cicero assassinated 1696 - Connecticut Route 108, one of the oldest highways Year 1957 ( MCMLVII) was a Common year starting on Tuesday (link displays the 1957 Gregorian calendar) Ribonuclease A (RNase A is an Endonuclease that cleaves single-stranded RNA. 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. Myoglobin is a single-chain globular Protein of 153 Amino acids containing a Heme ( Iron -containing Porphyrin) Prosthetic

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. X-ray scattering techniques are a family of non-destructive analytical techniques which reveal information about the crystallographic structure chemical composition Myoglobin is a single-chain globular Protein of 153 Amino acids containing a Heme ( Iron -containing Porphyrin) Prosthetic Lysozyme is a family of Enzymes ( which damage bacterial cell walls by catalyzing Hydrolysis of 14-beta-linkages between N-acetylmuramic acid and

Contents

Career summary

Important papers

Articles with over 500 citations:

  1. B. The Carlsberg Laboratory in Copenhagen, Denmark was created in 1875 by J The University of Cambridge (often Cambridge University) located in Cambridge, England, is the second-oldest university in the Pfizer Incorporated ( is a major Pharmaceutical company, which ranks number one in the world in sales Guggenheim Fellowships are American grants that have been awarded annually since 1925 by the John Simon Guggenheim Memorial Foundation to those "who The National Academy of Sciences (NAS is a corporation in the United States whose members serve Pro bono as "advisers to the nation on science Merck & Co Inc ( also known as Merck Sharp & Dohme or MSD outside the USA and Canada, is one of the largest Pharmaceutical companies The American Academy of Arts and Sciences (AAAS is an organization dedicated to scholarship and the advancement of learning 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. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document.
    • 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. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. 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. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. 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

External links

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