EMBIO
Coordinator
Prof. Robert Charles Glen, University of Cambridge, Unilever Centre for Molecular Informatics, Department of Chemistry
Participants
- UK: University of Cambridge
- Austria: University of Vienna
- Germany: Friedrich-Schiller-University Jena
- Germany: University of Heidelberg
- Germany: University of Leipzig
- Italy: University of Florence
- Sweden: Chalmers University of Technology
- The Netherlands: University of Groningen
Description
The EMBIO project, part of the NESTPATHFINDER initiative on ‘Tackling complexity in science’, focusing on one of the major challenges in modern biology – protein folding – aims at identifying the fundamental principles governing the emergence of complexity in self-organising biomolecular systems.
Most proteins spontaneously and reproducibly fold from an arbitrary chain of amino acids to a specific 3D structure adapted to their biological function. But although data exists on the chemical compositions and structures of thousands of proteins, it is still not possible to predict accurately or to explain how and why this transition to a folded structure takes place, partly because it is a non-linear, dynamic process influenced by many factors.
The new methodologies developed by EMBIO, underpinned by innovative mathematical approaches and applications software, open the door to an alternative view on protein folding. A greater understanding of how proteins fold is likely to bring strategic benefits and much needed innovation to drug discovery. In addition, misfolded proteins are directly implicated in a number of debilitating conditions such as Alzheimer’s and Creutzfeldt-Jakob disease. The consortium also expects its work on complexity estimation to impact on areas of study involving complicated chaotic dynamics, e.g. heart rhythms, where a better understanding of their chaotic nature could lead to new diagnostic tools for heart disease, and electromagnetic signals, which are generated in photonic devices used for optical communication.