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James Naismith (chemist)

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For the sports coach, see James Naismith.

James Naismith
FRS FRSE FMedSci FRSC FRSB
James Naismith at the Royal Society admissions day in July 2014
Born
James Henderson Naismith

(1968-07-26) 26 July 1968 (age 56)[2]
Bellshill, Scotland[2]
NationalityScottish, British
Other namesJim Naismith
CitizenshipUnited Kingdom
Alma mater
SpouseRachel Middleton[2]
Children2
Awards
Scientific career
Fields
Institutions
ThesisStructural studies of concanavalin A and zinc aldolase (1992)
Doctoral advisor
Websitewww.rfi.ac.uk/about/people/interim-academic-lead-jim-naismith/ Edit this at Wikidata

James Henderson Naismith FRS FRSE FMedSci FRSC FRSB[2][3][4] (born 26 July 1968)[2] is Professor of Structural Biology[5] at the University of Oxford, Director of the Research Complex at Harwell[6] and Director of the Rosalind Franklin Institute.[7] He previously served as Bishop Wardlaw Professor of Chemical Biology at the University of St Andrews.[8][1][9][10]

Education

Naismith was educated at Hamilton Grammar School.[2] He went on to study at the University of Edinburgh where he received a first class Bachelor of Science degree in chemistry in 1989. He won a Carnegie Scholarship to work under the supervision of Bill Hunter, John Helliwell and David Garner[11][12] at the University of Manchester where he received his PhD in 1992[13] for research into the chemical structure of Concanavalin A and Zinc aldolase. In 2016 he was awarded a Doctor of Science (DSc) by the University of St Andrews.[14]

Career and research

Following his PhD, Naismith did postdoctoral research at the University of Texas Southwestern Medical Center as a NATO Fellow in the laboratory of Stephen Sprang.[2][15] He was appointed a lecturer at the University of St Andrews in 1995, Reader in 1999 and a Professor in 2001. Naismith's research investigates:

The application of protein structure determination by X-ray crystallography coupled to molecular biology and biochemistry to probe biological mechanisms and to target specific disease pathways. We have ongoing research in

  1. signal transduction
  2. physical basis of protein carbohydrate interactions
  3. pathogenic bacteria glycan assembly, we have cloned and crystallised a number of the enzymes involved in key steps of glycan synthesis in pathogenic bacteria.
  4. viral replication, we are purifying and crystallising a heterodimer crucial to replication of viruses in vivo,
  5. the biosynthesis of unusual natural products.[16]

His research has been funded by the Biotechnology and Biological Sciences Research Council (BBSRC), the Engineering and Physical Sciences Research Council (EPSRC), the Medical Research Council (MRC),[17] the Wellcome Trust and the European Union.[18]

Awards and honours

Naismith was elected a Fellow of the Royal Society (FRS) in 2014. His nomination reads:

Naismith is cited for his stunning structural and chemical dissection of the many proteins involved in natural product recognition, synthesis and export. His work has revealed new paradigms in the recognition of nucleic acids and carbohydrates, unveiled novel chemical mechanisms for enzymatic nucleophilic substitution and addition and provided the first views, both structural and dynamic, of polysaccharide export systems in bacteria. His work is characterised by a synthesis of three-dimensional structural understanding with profound chemical insight.[3]

Naismith is also Fellow of the Royal Society of Chemistry (FRSC), the Royal Society of Biology (FRSB), the Royal Society of Edinburgh (FRSE), the Academy of Medical Sciences, United Kingdom (FMedSci), an elected member of the European Molecular Biology Organization (EMBO) and in 2016 was elected a Fellow of the American Association for the Advancement of Science (AAAS).[19] His nomination for the Academy of Medical Sciences reads:

Jim Naismith is Professor of Chemical Biology at St Andrew's University. He recognised the emerging problem of antibiotic resistance and has devoted his scientific career to the development of new therapeutic compounds and the identification of novel targets specific to microbial pathogens. Highlights include solving the structure and mechanism of a bacterial fluorinating enzyme, determining the mechanism of tryptophan 7-halogenase and establishing the structure of an open Escherichia coli mechanosensitive channel. His contributions have been recognised by the Carbohydrate Chemistry Medal of the Royal Society of Chemistry, the Leverhulme Prize in Molecular Biology and the Colworth Medal of Biochemical Society.[4]

Personal life

Naismith is married to Rachel Middleton with whom he has one son and one daughter.[2]

References

  1. ^ a b James Naismith publications indexed by Google Scholar Edit this at Wikidata
  2. ^ a b c d e f g h Anon (2014). "Naismith, Prof. James Henderson". Who's Who (online edition via Oxford University Press ed.). A & C Black. doi:10.1093/ww/9780199540884.013.U258346. {{cite encyclopedia}}: More than one of |surname= and |author= specified (help); Unknown parameter |othernames= ignored (help) (Subscription or UK public library membership required.)
  3. ^ a b "Professor James Naismith FMedSci FRS". London: royalsociety.org. Archived from the original on 14 August 2014.
  4. ^ a b "Professor James Naismith FRS FRSE FMedSci". acmedsci.ac.uk. Academy of Medical Sciences.
  5. ^ "Professor James Naismith". Biotechnology and Biological Sciences Research Council. Retrieved 25 January 2019.
  6. ^ Source, Diamond Light. "Diamond welcomes new Director of the Research Complex at Harwell – Diamond Light Source". diamond.ac.uk. Retrieved 10 August 2017.
  7. ^ "EPSRC announces interim leadership team for Rosalind Franklin Institute – EPSRC website". epsrc.ac.uk. Retrieved 10 August 2017.
  8. ^ James Naismith publications indexed by the Scopus bibliographic database. (subscription required)
  9. ^ James Naismith publications from Europe PubMed Central
  10. ^ Tatham, Michael H.; Jaffray, Ellis; Vaughan, Owen A.; Desterro, Joana M. P.; Botting, Catherine H.; Naismith, James H.; Hay, Ronald T. (2001). "Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9". Journal of Biological Chemistry. 276 (38): 35368–35374. doi:10.1074/jbc.M104214200. ISSN 0021-9258. PMID 11451954.
  11. ^ "Professor Jim Naismith biography". Diamond Light Source. Archived from the original on 19 August 2014.
  12. ^ "Jim Naismith, Scientific Advisory Board". Manchester Institute of Biotechnology. Archived from the original on 19 August 2014. Retrieved 15 August 2014.
  13. ^ Naismith, Jim (1992). Structural studies of Concanavalin A and zinc aldolase. manchester.ac.uk (PhD thesis). University of Manchester. OCLC 1055985285. (subscription required)
  14. ^ Naismith, James H. (2016). Structural and chemical studies upon proteins. st-andrews.ac.uk (DSc thesis). University of St Andrews.
  15. ^ Naismith, J. H.; Sprang, S. R. (1995). "Tumor necrosis factor receptor superfamily". Journal of Inflammation. 47 (1–2): 1–7. PMID 8913924.
  16. ^ The Naismith Structural Biology Group: Changing the world, one structure at a time…, University of St Andrews
  17. ^ "UK Government research grants awarded to James Henderson Naismith". Research Councils UK.
  18. ^ "Major honour for St Andrews scientist Jim Naismith". University of St Andrews. 1 May 2014. Archived from the original on 15 August 2014.
  19. ^ Ginger Pinholster (29 November 2016). "2016 AAAS Fellows Honored for Advancing Science to Serve Society | AAAS – The World's Largest General Scientific Society". AAAS. Retrieved 7 June 2017.
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