• 1971 BA (First Class)
• 1971 BSc
• 1974 MA
• 1976 D.Phil.

• 1975-1977 Research Fellow in Chemistry, University of Oxford
• 1977-1980 Assistant Professor of Chemistry, Harvard University Visiting Scientist, Massachusetts Institute of Technology
• 1980-1995 University Lecturer in Chemistry, University of Oxford
• 1995-1996 Reader (Aldrichian Praelector) in Chemistry, University of Oxford
• 1996-2001 Professor of Chemistry, University of Oxford
• 1998-2001 Director, Oxford Centre for Molecular Sciences
• 2001- John Humphrey Plummer Professor of Chemical and Structural Biology, University of Cambridge

• 1983 Corday Morgan Medal and Prize, Royal Society of Chemistry
• 1992 Howard Hughes International Research Scholar
• 1996 Brunauer Award, American Ceramic Society
• 1996 Fellow of the Royal Society
• 1997 Dewey and Kelly Award, University of Nebraska
• 1998 National Lecturer, American Biophysical Society
• 1999 Member of the European Molecular Biology Organisation
• 1999-2001 President, The Protein Society
• 1999 Interdisciplinary Award, Royal Society of Chemistry
• 2001 Doctor Honoris Causa, University of Leuven, Belgium
• 2002 Bijvoet Medal, University of Utrecht, The Netherlands
• 2002 SBI Medal, Italian Society of Biochemistry
• 2003 Royal Society Bakerian Lecturer
• 2003 Stein and Moore Award, Protein Society

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 through to theoretical physics. Most have some basic knowledge of biology, but this is by no means always the case.

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 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 Biochemistry Department 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.

1. Kammerer, R.A., Kostrewa, D., Zurdo, J., Detken, A., Garcia-Echeverria, C., Green, J.D., Muller, S.A., Meier, B.H., Winkler, F.K., Dobson, C.M. and Steinmetz, M.O. (2004)
   Exploring amyloid formation by a de novo design.
   Proc. Natl. Acad. Sci. USA [Epub ahead of print]
2. Jaroniec, C.P., MacPhee, C.E., Bajaj, V.S., McMahon, M.T., Dobson, C.M. and Griffin, R.G. (2004)
   High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.
   Proc. Natl. Acad. Sci. USA 101, 711-716.
3. Dobson, C.M. (2003)
   Protein folding and misfolding.
   Nature 426, 884-890.
4. Chiti, F., Stefani, M., Taddei, N., Ramponi, G. and Dobson, C.M. (2003)
   Rationalization of the effects of mutations on peptide and protein aggregation rates.
   Nature 424, 805-808.
5. 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. and Dobson, C.M. (2003)
   A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.
   Nature 424, 783-788.
6. Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C.M. and Stefani, M. (2002)
   Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.
   Nature 416, 507-511.
7. Canet, D., Last, A.M., Tito, P., Sunde, M., Spencer, A., Archer, D.B., Redfield, C., Robinson, C.V. and Dobson, C.M. (2002)
   Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
   Nature Structural Biol. 9, 308-315.
8. Chiti, F., Taddei, N., Baroni, F., Capanni, C., Stefani, M., Ramponi, G. and Dobson, C.M. (2002)
   Kinetic partitioning of protein folding and aggregation.
   Nature Structural Biol. 9, 137-143.
9. Fandrich, M., Fletcher, M.A. and Dobson, C.M. (2001)
   Amyloid fibrils from muscle myoglobin.
   Nature 410, 165-166.