Research groups

Research

Protein folding and chaperone mechanisms

One of the fundamental unsolved problems in biological science is how the sequence of a protein dictates its active 3-dimensional structure. If we can find a solution, two fundamental advances would result. Firstly, we would be able to convert DNA sequence data into their encoded 3-D protein structures and, secondly, we could begin to design protein molecules with new structure. Following on from a successful experimental programme which sought to characterise the folding process, we are now using computer-based studies to model this process with the aim of structure prediction. Ongoing experimental programmes seek to identify the molecular mechanisms of chaperones and their influence on protein folding.

Group

Mike Tyka.

Recent publications

Bigotti M.G. and Clarke A.R. (2005) Cooperativity in the thermosome. Journal of Molecular Biology 348, 13-26.

Khalili-Shirazi, A., Quaratino, S., Londei, M., Summers, L., Tayebi, M., Clarke, A.R., Hawke, S.H., Jackson, G.S., Collinge, J. (2005) Protein conformation significantly influences immune responses to prion protein. Journal of Immunology 174 3256-63.

Jackson, G.S., McKintosh, E., Flechsig, E., Prodromidou, K., Hirsch, P., Linehan, J., Brandner, S., Clarke, A.R., Weissmann, C, and Collinge, J. (2005) An enzyme-detergent method for effective prion decontamination of surgical steel. Journal of General Virology 86 869-78.

Forsyth, J.L., Beaudoin, F., Halford, N.G., Sessions, R.B., Clarke, A.R., and Shewry, P.R. (2005) Design, expression and characterisation of lysine-rich forms of the barley seed protein CI-2. Biochimica Biophysica Acta 1747 221-7