Chris Dobson

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Chris Dobson
Born
Christopher Martin Dobson

(1949-10-08) 8 October 1949 (age 74)
Alma mater
Awards
Scientific career
Fields
Institutions
ThesisThe conformation of lysozyme in solution (1975)
Notable studentsCarol V. Robinson
Websitewww.ch.cam.ac.uk/person/cmd44

Sir Christopher Martin Dobson, FRS, FMedSci (born 8 October 1949) is a British chemist, who is the John Humphrey Plummer Professor of Chemical and Structural Biology in the Department of Chemistry at the University of Cambridge, and Master of St John's College, Cambridge.[1][2]

Early life and education

Dobson was born on 8 October 1949.[3] He was educated at Hereford Cathedral Junior School, and then Abingdon School from 1960 until 1967.[4] He completed a Bachelor of Arts and D.Phil[5] at the University of Oxford (Keble and Merton Colleges).

Research

Dobson's research is largely concerned with protein folding and misfolding, and its links with medical disorders particularly Alzheimer's and Parkinson's diseases. His research interests are focused on protein molecules, and particularly on defining the fundamental principles by which they fold to generate function and biological activity, and yet can misfold to generate toxicity and disease. His studies are highly interdisciplinary and collaborative, and make use of a very wide range of techniques, encompassing theory as well as experiment. The Dobson group based at the Department of Chemistry, University of Cambridge [1] is particularly interested in the discovery of the nature, properties, mechanism of formation and biological significance of the ‘misfolded’ amyloid state of proteins. Amyloid-related diseases include whole-body disorders such as the systemic amyloidoses, neuronal disorders such as Alzheimer's and Parkinson's diseases, and other organ-specific disorders such as type II diabetes. The major goals are the elucidation of the general molecular principles that underlie this whole family of medical conditions, which are now becoming a major threat to human health and social harmony across the modern world, and the generation of a firm foundation for the rational and effective prevention and treatment of these debilitating and usually fatal conditions.[1] Dobson is an author or co-author of nearly 700 papers and review articles, including more than 30 in Nature and Science, which have been cited over 50,000 times. His current h-index is 110.[6]

Career

Dobson held Research Fellowships at Merton College and then Linacre College before working at Harvard University. He returned to Oxford in 1980 as a Fellow of Lady Margaret Hall, Oxford and as a University Lecturer in Chemistry, later receiving promotions to Reader, then Professor, of Chemistry.[3] Dobson has been at Cambridge since 2001 and has been Master of St John's College, Cambridge since 2007.

Awards and honours

In 2009 Dobson was awarded the Royal Medal by the Royal Society "for his outstanding contributions to the understanding of the mechanisms of protein folding and mis-folding, and the implications for disease", and in 2014 he received both the Heineken Prize for Biochemistry and Biophysics and the Feltrinelli International Prize for Medicine. Dobson was elected a Fellow of the Royal Society (FRS) in 1996. His nomination reads:

Dobson is distinguished for his studies, principally using NMR methods, of the structures and dynamics of proteins in solution. Such studies include those on lysozyme, with which he demonstrated many methodological advances, interleukin-4, with which he established for the first time the topology of the important family of haemopoietic helical cytokines, and urokinase-type plasminogen activator, with which he elucidated the dynamic characteristics of multidomain fibrinolytic proteins, Dobson is a pioneer in the application of NMR methods to the problem of protein folding, which is now the major theme of his work. His studies on lysozyme are resulting in one of the most detailed descriptions of a folding pathway for a protein. Dobson has explored the properties and reactions of molecules in solids by means of NMR spectroscopy, including proteins, organometallic compounds, inorganic paramagnets and the silicaceous components of hydraulic materials. Notable here are analyses of the nature and origin of dynamic properties in molecular solids, and their relationship to structure and reactivity.[7]

Dobson's other accolades include:

References

  1. ^ a b c d e f g h i j k l m n o p q r s t u v w x y z aa ab ac ad ae af ag http://www.ch.cam.ac.uk/person/cmd44 Chris Dobson CV
  2. ^ Chris Dobson publications indexed by Microsoft Academic
  3. ^ a b DOBSON. "DOBSON, Prof. Christopher Martin". Who's Who. Vol. 2014 (online Oxford University Press ed.). A & C Black. {{cite encyclopedia}}: Unknown parameter |othernames= ignored (help) (Subscription or UK public library membership required.) (subscription required)
  4. ^ "Chemistry Prizes" (PDF). The Abingdonian.
  5. ^ Dobson, Christopher Martin (2014). The conformation of lysozyme in solution (DPhil thesis). University of Oxford.
  6. ^ Chris Dobson's publications indexed by the Scopus bibliographic database. (subscription required)
  7. ^ "EC/1996/06: Dobson, Christopher Martin". London: The Royal Society. Archived from the original on 30 September 2014. Retrieved 30 September 2014. {{cite web}}: Unknown parameter |deadurl= ignored (|url-status= suggested) (help)
  8. ^ "Bijvoet Medal". Bijvoet Center for Biomolecular Research. Retrieved 12 September 2017.
  9. ^ "Master receives Honorary Degree from King's College London | StJohns".
  10. ^ "Fellows & Scholars : Trinity College Dublin, the University of Dublin, Ireland".
  11. ^ "2013 NAS Members and Foreign Associates Elected".
  12. ^ "Christopher M. Dobson — KNAW".
  13. ^ "Feltrinelli International Prize awarded to Chris Dobson | Department of Chemistry".
  14. ^ "Election of New Members at the 2018 Spring Meeting | American Philosophical Society".
Academic offices
Preceded by Master of St John's College, Cambridge
2007–present
Succeeded by
Incumbent