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Ronald T. Raines

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Ronald T. Raines
BornAugust 13, 1958 (1958-08-13) (age 66)
Montclair, New Jersey
NationalityAmerican
Alma materMassachusetts Institute of Technology
Known forResearch on collagen, ribonucleases, protein chemistry, and biofuels
Scientific career
FieldsChemical Biology
InstitutionsUniversity of Wisconsin–Madison
Massachusetts Institute of Technology
ThesisEnergetics of enzymatic catalysis: Triosephosphate isomerase
Doctoral advisorJeremy R. Knowles
Other academic advisorsWilliam J. Rutter (postdoctoral)
Christopher T. Walsh (undergraduate)

Ronald T. Raines is an American chemical biologist. He is the Roger and Georges Firmenich Professor of Natural Products Chemistry at the Massachusetts Institute of Technology. He is known for using ideas and methods of physical organic chemistry to solve important problems in biology.

Education

Raines was born and raised in the New Jersey suburbs of New York City. His father was a Ph.D. chemist, having worked with Charles O. Beckman at Columbia University. Raines graduated from West Essex High School in North Caldwell, New Jersey. He received Sc.B. degrees in chemistry and biology at the Massachusetts Institute of Technology, doing undergraduate research with Christopher T. Walsh on pyridoxal phosphate-dependent enzymes. He earned A.M. and Ph.D. degrees in chemistry at Harvard University for work with Jeremy R. Knowles on catalysis by triosephosphate isomerase. Raines was a Helen Hay Whitney postdoctoral fellow with William J. Rutter in the Department of Biochemistry and Biophysics at the University of California, San Francisco, where he cloned and expressed the gene encoding bovine pancreatic ribonuclease.

Career

Raines was a member of the faculty at the University of Wisconsin–Madison from 1989 until 2017. There, he was the Henry A. Lardy Professor of Biochemistry, Linus Pauling Professor of Chemical Biology, and a Professor of Chemistry.[1] In 2009, he was a Visiting Associate in Chemistry at Caltech; in 2014, he was the Givaudan–Karrer Distinguished Visiting Professor at the Universität Zürich.[2] In 2017, he returned to Cambridge, Massachusetts to join the faculty of his alma mater, MIT. Altogether, he has mentored more than 100 graduate students and postdoctorates.[3]

Raines and his coworkers have made the followinga contributions.

  • Revelation of the basis for the conformational stability of collagen, which is the most abundant protein in animals.[4] This work led to the discovery that unappreciated chemical forces—the n→π* interaction[5] and C5 hydrogen bond[6]—contribute to the stability of nearly every protein.[7] His hyperstable collagens are in preclinical trials for the detection and treatment of wounds.
  • Discovery of how to endow an otherwise innocuous human RNA-cleaving enzyme with toxicity that is specific for cancer cells.[8] Such a ribonuclease is in a human clinical trial as an anti-cancer agent.
  • Mechanistic insight on cellular redox homeostasis[9] and on imperatives for the uptake of cationic proteins and peptides by mammalian cells.[10]
  • Invention of chemical processes to synthesize proteins[11] and to convert crude biomass into useful fuels and chemicals,[12] and fluorogenic probes to image the uptake of molecules into living cells.[13]

Raines serves on the editorial advisory boards of the journals ACS Chemical Biology; Bioconjugate Chemistry; Current Opinion in Chemical Biology; Peptide Science; Protein Engineering, Design & Selection; and Protein Science. He was the Chair of the NIH study section that evaluates grant applications in synthetic and biological chemistry.

Awards and honors

References

  1. ^ "National Academy of Inventors and American Peptide Society Honor Professor Ronald Raines".
  2. ^ "Givaudan Karrer Lectureships".
  3. ^ Ronald T. Raines - Chemistry Tree
  4. ^ Shoulders, M. D.; Raines, R. T. (2009). "Collagen structure and stability". Annu. Rev. Biochem. 78: 929–958. doi:10.1146/annurev.biochem.77.032207.120833. PMC 2846778. PMID 19344236.
  5. ^ Newberry, R. W.; Raines, R. T. (2017). "The n→π* interaction". Acc. Chem. Res. 50 (8): 1838–1846. doi:10.1021/acs.accounts.7b00121. PMC 5559721. PMID 28735540.
  6. ^ Newberry, R. W.; Raines, R. T. (2016). "A prevalent intraresidue hydrogen bond stabilizes proteins". Nat. Chem. Biol. 12 (12): 1084–1088. doi:10.1038/nchembio.2206. PMC 5110370. PMID 27748749.
  7. ^ Newberry, R. W.; Raines, R. T. (2019). "Secondary forces in protein folding". ACS Chem. Biol. 14 (8): 1677–1686. doi:10.1021/acschembio.9b00339. PMC 6995338. PMID 31243961.
  8. ^ Leland, P. A.; Raines, R. T. (2001). "Cancer chemotherapy – Ribonucleases to the rescue". Chem. Biol. 8 (5): 405–413. doi:10.1016/S1074-5521(01)00030-8. PMC 2913432. PMID 11358688.
  9. ^ Kersteen, E. A.; Raines, R. T. (2003). "Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics". Antioxid. Redox Signal. 5 (4): 413–424. doi:10.1089/152308603768295159. PMC 2814249. PMID 13678529.
  10. ^ Fuchs, S. M.; Raines, R. T. (2006). "Internalization of cationic peptides: The road less (or more?) traveled". Cell. Mol. Life Sci. 63 (16): 1819–1822. doi:10.1007/s00018-006-6170-z. PMC 2812862. PMID 16909213.
  11. ^ Nilsson, B. L.; Soellner, M. B.; Raines, R. T. (2005). "Chemical synthesis of proteins". Annu. Rev. Biophys. Biomol. Struct. 34: 91–118. doi:10.1146/annurev.biophys.34.040204.144700. PMC 2845543. PMID 15869385.
  12. ^ Caes, B. R.; Teixeira, R. E.; Knapp, K. G.; Raines, R. T. (2015). "Biomass to furanics: Renewable routes to chemicals and fuels". ACS Sustain. Chem. Eng. 3 (11): 2591–2605. doi:10.1021/acssuschemeng.5b00473.
  13. ^ Lavis, L. D.; Raines, R. T. (2008). "Bright ideas for chemical biology". ACS Chem. Biol. 3 (3): 142–155. doi:10.1021/cb700248m. PMC 2802578. PMID 18355003.

Sources

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