skip to content
 

Professor Christopher Dobson FRS

Portrait of cmd44

Our research interests are primarily focused on the investigation of the structures and properties of biological molecules, especially proteins, and their relationship to biological evolution and disease. We have particular interest in the fundamental science underlying disorders such as Alzheimer's and Parkinson's disease. In addition, however, we have recently become involved in the novel utilisation of biological molecules in materials science and nanotechnology.

The methods we use are largely experimental, but do include theoretical and computational approaches. Much of the work is highly interdisciplinary, and people joining the group come from a wide variety of scientific backgrounds ranging from experimental biochemistry to theoretical physics. The research group is based in the Chemistry Department in a newly constructed laboratory located in the Unilever Building. The range of experimental techniques used by the group is very large, including NMR, EM, AFM and X-ray diffraction, as well as a variety of methods based on optical spectroscopy, including fluorescence and circular dichroism. Many, but not all, members of the group also use the techniques of protein chemistry and molecular biology.

The group has close links with the Clinical School, the Genetics Department and the Nanoscience Centre and, indeed, some members of the group are largely based in these departments. New members of the group usually develop a project by discussion with me, along with other members of the research team. Group members are often involved in joint projects with other laboratories and may spend periods of time working with our collaborators in other parts of the world.

More information: Chris Dobson full CV (Microsoft Word);Chris Dobson selected publications list (Microsoft Word).

The following articles provide a general appreciation of our current areas of research:

Reviews

F. Chiti and C.M. Dobson, Amyloid Formation by Globular Proteins under Native Conditions, Nature Chem. Biol. 5, 15-22 (2009)

L.M. Luheshi, D.C. Crowther and C.M. Dobson, Protein Misfolding and Disease: From the Test Tube to the Organism, Curr. Opin. Chem. Biol. 12, 25-31 (2008)

M. Vendruscolo and C.M. Dobson, Dynamic Visions of Enzymatic Reactions, Science 313, 1586- 1587 (2006)

F. Chiti and C.M. Dobson, Protein Misfolding, Functional Amyloid and Human Disease, Annu. Rev. Biochem. 75, 333-366 (2006)

C.M. Dobson, Chemical Space and Biology, Nature 432, 824-882 (2004)

C.M. Dobson, Protein Folding and Misfolding, Nature 426, 884-890 (2003)

C.M. Dobson, Protein Misfolding, Evolution and Disease, Trends Biochem. Sci. 24, 329-332 (1999)

C.M. Dobson, A. Sali and M. Karplus, Protein Folding: A Perspective from Theory and Experiment, Angew. Chem. Int. Ed. Eng. 37, 868-893 (1998)

Selected Publications

T.P.J. Knowles, C.A. Waudby, G.L. Devlin, S.A. Cohen, A. Aguzzi, M. Vendruscolo, E.M. Terentjev, M.E. Welland and C.M. Dobson, An Analytical Solution to the Kinetics of Breakable Filament Assembly, Science 326, 1533-1537 (2009)

S.T. Hsu, L.D. Cabrita, P. Fucini, J. Christodoulou and C.M. Dobson, Probing Side-chain Dynamics of a Ribosome-bound Nascent Chain using Methyl NMR Spectroscopy, J. Am. Chem. Soc., 131 (24), 8366-8367, (2009)

T.P. Knowles, A.W. Fitzpatrick, S. Meehan, H.R. Mott, M. Vendruscolo, C.M. Dobson and M.E. Welland, Role of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils, Science 318, 1900-1903 (2007)

L.M. Luheshi, G.G. Tartaglia, A.C. Brorsson, A.P. Pawar, I.E. Watson, F. Chiti, M. Vendruscolo, D.A. Lomas, C.M. Dobson and D.C. Crowther, Systematic In Vivo Analysis of the Intrinsic Determinants of Amyloid Beta Pathogenicity, PloS Biol. 5(11):e290 (2007)

K. Lindorff-Larsen, R.B. Best, M.A. De Pristo, C.M. Dobson and M. Vendruscolo, Simultaneous Determination of Protein Structure and Dynamics, Nature 433, 129-133 (2005)

D.M. Korzhnev, X. Salvatella, M. Vendruscolo, A.A. Di Nardo, A.R. Davison, C.M. Dobson and L.E. Kay, Low Populated Folding Intermediates of the Fyn SH3 Domain Characterized by Relaxation Dispersion NMR, Nature 430, 586-590 (2004)

M. Dumoulin, A.M. Last, A. Desmyter, K. Decanniere, D. Canet, A. Spencer, D.B. Archer, S. Muyldermans, L. Wyns, A. Matagne, C. Redfield, C.V. Robinson and C.M. Dobson, A Camelid Antibody Fragment Inhibits Amyloid Fibril Formation by Human Lysozyme, Nature 424, 783-788 (2003)

F. Chiti, M. Stefani, N. Taddei, G. Ramponi and C.M. Dobson, Rationalisation of Mutational Effects on Protein Aggregation Rates, Nature 424, 805-808 (2003)

M. Fändrich, M.A. Fletcher and C.M. Dobson, Amyloid Fibrils from Muscle Myoglobin, Nature 410, 165-166 (2001)

M. Vendruscolo, E. Paci, C.M. Dobson and M. Karplus, Three Key Residues Form a Critical Contact Network in a Transition State for Protein Folding, Nature 409, 641-646 (2001)

Publications

Spatial propagation of protein polymerization
SI Cohen, L Rajah, CH Yoon, AK Buell, DA White, RA Sperling, M Vendruscolo, EM Terentjev, CM Dobson, DA Weitz, TP Knowles – Phys Rev Lett (2014) 112, 098101
Dynamics and Timekeeping in Biological Systems.
CM Dobson – Annu Rev Biochem (2014)
The Role of Stable α-Synuclein Oligomers in the Molecular Events Underlying Amyloid Formation.
N Lorenzen, SB Nielsen, AK Buell, JD Kaspersen, P Arosio, BS Vad, W Paslawski, G Christiansen, Z Valnickova-Hansen, M Andreasen, JJ Enghild, JS Pedersen, CM Dobson, TP Knowles, DE Otzen – Journal of the American Chemical Society (2014) 136, 3859
A simple lattice model that captures protein folding, aggregation and amyloid formation.
S Abeln, M Vendruscolo, CM Dobson, D Frenkel – PLoS One (2014) 9, e85185
Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.
EP O'Brien, M Vendruscolo, CM Dobson – Nature Communications (2014) 5, 2988
Chemical kinetics for drug discovery to combat protein aggregation diseases
P Arosio, M Vendruscolo, CM Dobson, TPJ Knowles – Trends in Pharmacological Sciences (2014) 35, 127
Chemical kinetics for drug discovery to combat protein aggregation diseases.
P Arosio, M Vendruscolo, CM Dobson, TP Knowles – Trends Pharmacol Sci (2014) 35, 127
Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein by Small Molecules as a Potential Therapeutic Strategy for Parkinson's Disease.
G Tóth, SJ Gardai, W Zago, CW Bertoncini, N Cremades, SL Roy, MA Tambe, JC Rochet, C Galvagnion, G Skibinski, S Finkbeiner, M Bova, K Regnstrom, SS Chiou, J Johnston, K Callaway, JP Anderson, MF Jobling, AK Buell, TA Yednock, TP Knowles, M Vendruscolo, J Christodoulou, CM Dobson, D Schenk, L McConlogue – PLoS One (2014) 9, e87133
A Clear View of Polymorphism, Twist, and Chirality in Amyloid Fibril Formation
LR Volpatti, M Vendruscolo, CM Dobson, TP Knowles – ACS Nano (2013) 7, 10443
Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.
D Pinotsi, AK Buell, C Galvagnion, CM Dobson, GS Kaminski Schierle, CF Kaminski – Nano Lett (2014) 14, 339
  •  
  • 1 of 79
  • >

Research Group

Research Interest Group

Telephone number

01223 763070 (shared)

Email address

cmd44@cam.ac.uk