In 1996 researchers in Oxford, Groningen, EMBL, Rome and Granada together established a TMR network to address fundamental aspects of protein folding. This proved highly successful and lead to several significant scientific advances. This application is to fund the expansion of the network into the 5th framework. The goals are :
i) to build on the achievements of the previous network;
ii) to continue the progress in understanding the mechanism of protein folding and iii) to exploit our collective expertise to tackle the developing question of protein misfolding and disease. Specifically, the aim of the new network is to understand how interactions between amino acid residues lead to the kinetic and thermodynamic control of protein folding in order to develop the ability to predict which peptide sequences will fold a unique structure, which will not, and which may form toxic high order aggregates such as amyloid fibrils.
1. To understand in detail the mechanisms of the folding of several small proteins, with particular emphasis on the relationship between folding kinetics, folding mechanism and structure.
2. To explore the evolutionary basis of naturally occurring protein sequences in terms of their folding behavior, with emphasis on the importance of the avoidance of aggregation and fibril formation.
3. To structurally characterize folding intermediates and explore the relationship between folding intermediates and species involved in initiating aggregation in peptides or proteins. To achieve these objectives the network will use a coordinated approach combining biophysical , protein engineering and computational techniques that is the strength of the Folding Network.
Funding SchemeNET - Research network contracts
CB2 1EW Cambridge