Chris Dobson

Chris Dobson
Born Christopher Martin Dobson
(1949-10-08) October 8, 1949
Residence Cambridge
Alma mater
Thesis The conformation of lysozyme in solution (1975)
Notable awards

Christopher Martin Dobson, FRS, FMedSci (born 8 October 1949)[1] 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.[2][3]


Dobson completed a Bachelor of Arts and D.Phil[4] at the University of Oxford (Keble and Merton Colleges).


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 experiment. The Dobson group based at the Department of Chemistry, University of Cambridge [2] 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.[2] 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.[5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31]


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.[1] 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 poperties 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.[32]

Dobson's other accolades include:


  1. 1 2 DOBSON, Prof. Christopher Martin. Who's Who. 2014 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. (subscription required)
  2. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 Professor Christopher Dobson FRS FMedSci, University of Cambridge
  3. List of publications from Microsoft Academic Search
  4. Dobson, Christopher Martin (2014). The conformation of lysozyme in solution (DPhil thesis). University of Oxford.
  5. Chris Dobson's publications indexed by the Scopus bibliographic database, a service provided by Elsevier. (subscription required)
  6. Radford, S. E.; Dobson, C. M.; Evans, P. A. (1992). "The folding of hen lysozyme involves partially structured intermediates and multiple pathways". Nature. 358 (6384): 302–7. doi:10.1038/358302a0. PMID 1641003.
  7. Miranker, A; Robinson, C. V.; Radford, S. E.; Aplin, R. T.; Dobson, C. M. (1993). "Detection of transient protein folding populations by mass spectrometry". Science. 262 (5135): 896–900. doi:10.1126/science.8235611. PMID 8235611.
  8. Booth, D. R.; Sunde, M; Bellotti, V; Robinson, C. V.; Hutchinson, W. L.; Fraser, P. E.; Hawkins, P. N.; Dobson, C. M.; Radford, S. E.; Blake, C. C.; Pepys, M. B. (1997). "Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis". Nature. 385 (6619): 787–93. doi:10.1038/385787a0. PMID 9039909.
  9. Dobson, C. M. (1999). "Protein misfolding, evolution and disease". Trends in Biochemical Sciences. 24 (9): 329–32. doi:10.1016/S0968-0004(99)01445-0. PMID 10470028.
  10. Vendruscolo, M; Paci, E; Dobson, C. M.; Karplus, M (2001). "Three key residues form a critical contact network in a protein folding transition state". Nature. 409 (6820): 641–5. doi:10.1038/35054591. PMID 11214326.
  11. Fändrich, M; Fletcher, M. A.; Dobson, C. M. (2001). "Amyloid fibrils from muscle myoglobin". Nature. 410 (6825): 165–6. doi:10.1038/35065514. PMID 11242064.
  12. Bucciantini, M; Giannoni, E; Chiti, F; Baroni, F; Formigli, L; Zurdo, J; Taddei, N; Ramponi, G; Dobson, C. M.; Stefani, M (2002). "Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases". Nature. 416 (6880): 507–11. doi:10.1038/416507a. PMID 11932737.
  13. Dobson, C. M. (2002). "Protein-misfolding diseases: Getting out of shape". Nature. 418 (6899): 729–30. doi:10.1038/418729a. PMID 12181546.
  14. Dumoulin, M; Last, A. M.; Desmyter, A; Decanniere, K; Canet, D; Larsson, G; Spencer, A; Archer, D. B.; Sasse, J; Muyldermans, S; Wyns, L; Redfield, C; Matagne, A; Robinson, C. V.; Dobson, C. M. (2003). "A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme". Nature. 424 (6950): 783–8. doi:10.1038/nature01870. PMID 12917687.
  15. Chiti, F; Stefani, M; Taddei, N; Ramponi, G; Dobson, C. M. (2003). "Rationalization of the effects of mutations on peptide and protein aggregation rates". Nature. 424 (6950): 805–8. doi:10.1038/nature01891. PMID 12917692.
  16. Dobson, C. M. (2003). "Protein folding and misfolding". Nature. 426 (6968): 884–90. doi:10.1038/nature02261. PMID 14685248.
  17. Dobson, C. M. (2004). "PROTEIN CHEMISTRY: In the Footsteps of Alchemists". Science. 304 (5675): 1259–62. doi:10.1126/science.1093078. PMID 15166354.
  18. Korzhnev, D. M.; Salvatella, X.; Vendruscolo, M.; Di Nardo, A. A.; Davidson, A. R.; Dobson, C. M.; Kay, L. E. (2004). "Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR". Nature. 430 (6999): 586–90. doi:10.1038/nature02655. PMID 15282609.
  19. Lindorff-Larsen, K.; Best, R. B.; Depristo, M. A.; Dobson, C. M.; Vendruscolo, M. (2005). "Simultaneous determination of protein structure and dynamics". Nature. 433 (7022): 128–32. doi:10.1038/nature03199. PMID 15650731.
  20. Carulla, N. L.; Caddy, G. L.; Hall, D. R.; Zurdo, J. S.; Gairí, M.; Feliz, M.; Giralt, E.; Robinson, C. V.; Dobson, C. M. (2005). "Molecular recycling within amyloid fibrils". Nature. 436 (7050): 554–8. doi:10.1038/nature03986. PMID 16049488.
  21. Wright, C. F.; Teichmann, S. A.; Clarke, J.; Dobson, C. M. (2005). "The importance of sequence diversity in the aggregation and evolution of proteins". Nature. 438 (7069): 878–81. doi:10.1038/nature04195. PMID 16341018.
  22. Knowles, T. P.; Fitzpatrick, A. W.; Meehan, S.; Mott, H. R.; Vendruscolo, M.; Dobson, C. M.; Welland, M. E. (2007). "Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils". Science. 318 (5858): 1900–3. doi:10.1126/science.1150057. PMID 18096801.
  23. Chiti, F.; Dobson, C. M. (2009). "Amyloid formation by globular proteins under native conditions". Nature Chemical Biology. 5 (1): 15–22. doi:10.1038/nchembio.131. PMID 19088715.
  24. Knowles, T. P.; Waudby, C. A.; Devlin, G. L.; Cohen, S. I.; Aguzzi, A; Vendruscolo, M; Terentjev, E. M.; Welland, M. E.; Dobson, C. M. (2009). "An analytical solution to the kinetics of breakable filament assembly". Science. 326 (5959): 1533–7. doi:10.1126/science.1178250. PMID 20007899.
  25. De Simone, A.; Dhulesia, A.; Soldi, G.; Vendruscolo, M.; Hsu, S. -T. D.; Chiti, F.; Dobson, C. M. (2011). "Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility". Proceedings of the National Academy of Sciences. 108 (52): 21057–21062. doi:10.1073/pnas.1112197108.
  26. Cremades, N; Cohen, S. I.; Deas, E; Abramov, A. Y.; Chen, A. Y.; Orte, A; Sandal, M; Clarke, R. W.; Dunne, P; Aprile, F. A.; Bertoncini, C. W.; Wood, N. W.; Knowles, T. P.; Dobson, C. M.; Klenerman, D (2012). "Direct observation of the interconversion of normal and toxic forms of α-synuclein". Cell. 149 (5): 1048–59. doi:10.1016/j.cell.2012.03.037. PMC 3383996Freely accessible. PMID 22632969.
  27. Cohen, S. I. A.; Linse, S.; Luheshi, L. M.; Hellstrand, E.; White, D. A.; Rajah, L.; Otzen, D. E.; Vendruscolo, M.; Dobson, C. M.; Knowles, T. P. J. (2013). "Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism". Proceedings of the National Academy of Sciences. 110 (24): 9758–9763. doi:10.1073/pnas.1218402110.
  28. Fitzpatrick, A. W. P.; Debelouchina, G. T.; Bayro, M. J.; Clare, D. K.; Caporini, M. A.; Bajaj, V. S.; Jaroniec, C. P.; Wang, L.; Ladizhansky, V.; Muller, S. A.; MacPhee, C. E.; Waudby, C. A.; Mott, H. R.; De Simone, A.; Knowles, T. P. J.; Saibil, H. R.; Vendruscolo, M.; Orlova, E. V.; Griffin, R. G.; Dobson, C. M. (2013). "Atomic structure and hierarchical assembly of a cross- amyloid fibril". Proceedings of the National Academy of Sciences. 110 (14): 5468–5473. doi:10.1073/pnas.1219476110.
  29. Knowles, T. P. J.; Vendruscolo, M.; Dobson, C. M. (2014). "The amyloid state and its association with protein misfolding diseases". Nature Reviews Molecular Cell Biology. 15 (6): 384–96. doi:10.1038/nrm3810. PMID 24854788.
  30. Chiti, F.; Dobson, C. (2006). "Protein misfolding, functional amyloid, and human disease". Annual Review of Biochemistry. 75: 333–366. doi:10.1146/annurev.biochem.75.101304.123901. PMID 16756495.
  31. Stefani, M.; Dobson, C. M. (2003). "Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution". Journal of Molecular Medicine. 81 (11): 678–99. doi:10.1007/s00109-003-0464-5. PMID 12942175.
  32. "EC/1996/06: Dobson, Christopher Martin". London: The Royal Society. Archived from the original on 2014-09-30.
Academic offices
Preceded by
Richard Perham
Master of St John's College, Cambridge
Succeeded by
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