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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, MG, Clarke AR. (2005) Cooperativity in the thermosome. Journal of Molecular Biology. 348: 13-26.

Khalili-Shirazi A, Quaratino S, Londei M, Summers L, Tayebi M, Clarke AR, Hawke SH, Jackson GS, Collinge J. (2005) Protein conformation significantly influences immune responses to prion protein. Journal of Immunology. 174: 3256-3263.

Jackson GS, McKintosh E, Flechsig E, Prodromidou K, Hirsch P, Linehan J, Brandner S, Clarke AR, Weissmann C, Collinge J. (2005) An enzyme-detergent method for effective prion decontamination of surgical steel. Journal of General Virology. 86: 869-878.

Forsyth JL, Beaudoin F, Halford NG, Sessions RB, Clarke AR, Shewry PR. (2005) Design, expression and characterisation of lysine-rich forms of the barley seed protein CI-2. Biochimica Biophysica Acta. 1747: 221-227

View all publications listed on the University of Bristol's publication database