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 Cavendish Laboratory and the Medical School 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. Members of the group 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.
A general appreciation of the areas of research with which we are involved can best be obtained by reading recent articles, including:
Recent Reviews
C.M. Dobson, "In the Footsteps of Alchemists", Science 304, 1259-1262 (2004)
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, "Getting out of Shape - Protein Misfolding Diseases", Nature 418, 729-730 (2002)
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
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)
D.R. Booth, M. Sunde,V. Bellotti, C.V. Robinson, W.L. Hutchinson, P.E. Fraser, P.N. Hawkins, C.M. Dobson, S.E. Radford, C.C.F. Blake and M.B. Pepys, "Instability, Unfolding and Aggregation of Human Lysozyme Variants Underlying Amyloid Fibrillogenesis", Nature 385, 787-793 (1997)