Professor Christopher M. Dobson
Oxford Centre for Molecular Sciences
University of Oxford
Unknown Location

Monday, September 28, 1998
3:00 pm (CT)
3269 Beckman Institute

Abstract

The problem of how proteins fold remains one of the major challenges of structural biology. Understanding folding will not only solve a major intellectual puzzle, but will increase our overall knowledge of the factors that encode and stabilise particular structural features of proteins. This should help to provide a basis for their rational design and modification, aid in the prediction of their three-dimensional structures from the amino acid sequence, and contribute to strategies to combat the increasing number of diseases now being associated with the failure of proteins to fold correctly. A key aspect of understanding how a protein folds is the ability to probe the molecular structure at different stages of its conversion from a random coil polypeptide chain to the fully folded state. This task is complicated by the intrinsic heterogeneity of the folding process, and the rapidity at which it can take place. We have been developing approaches based on a combination of physical techniques to provide a structural description of events that occur during the folding of a range of small proteins. Recent results from our laboratory relate to the structure of the species that form during protein folding and misfolding. These allow speculation on the importance of different factors in driving protein molecules to their native states, and address the consequences of misfolding events and their relationship to amyloid-based diseases.

Tea and coffee will be served in R3151 Beckman Institute at 2:15pm.