Protein folding, stability, redesign and therapeutic intervention
24/06/2014 - Room Garden Room at 14:00 - External Seminar
(University of Cambridge)
A major goal of our research is to define, using a battery of techniques spanning single-molecule methods, biophysics, chemical biology, and analysis in cellulo and in silico, the processes that constitute the life cycle of a protein in the cell - biosynthesis, folding, localisation, macromolecular assembly and degradation - and how they are directed by the cellular machinery. In order to achieve our aims we focus on a class of proteins known as tandem-repeat proteins. We have shown that their simple, modular architecture affords them distinctive properties compared with globular proteins and makes it uniquely straightforward to map structure-function relationships and to rationally redesign their properties. We are also interested in exploiting the exquisite design-ability of repeat proteins to create a toolkit of self-assembling modules with which to build a diverse range of artificial proteins and protein-based biomaterials.