Protein Folding and Assembly Team
Team Leader: Professor Keith Willison
Location: Chester Beatty Laboratories, London
Protein folding studies are a branch of biochemistry which is beginning to increase our understanding of many areas of biology, including cancer. It used to be thought that protein folding is an autonomous property of every individual protein but it is now clear that many proteins require help to reach their native and functional states. This ‘help’ is mediated by molecular chaperones - other proteins which assist the folding process but don’t become involved in the final structure. One of the most important molecular chaperones in eukaryotes is CCT (Chaperonin containing TCP-1) because it folds the cytoskeletal elements which form the structure of cells; the actins and tubulins. CCT is a nanomachine composed of around 8500 amino acids and weighs in at a size of 1 million Daltons. We use a multi-disciplinary approach to studying this complicated object; genetics, cell biology, structural biology and biophysics. We hope to understand underlying, fundamental structure in the cell cycle through describing how CCT connects the unfolded and native energetic landscapes of its substrates.
In the Section of Cell and Molecular Biology (including the Cancer Research UK Centre for Cell and Molecular Biology)
