LUE - Analyse des espaces de conformation pour les protéines intrinsèquement désordonnées

école doctorale

équipe

contexte

The enormous development of structural biology has permitted to determine more than 213,000 biomolecular structures at atomic resolution (Protein Data Bank: \url{www.rcsb.org}). These structures, defined by the relative positions of atoms, have been permitting strong advances in understanding the function of the protein molecules, and consequently in understanding essential physiological and pathological processes. The knowledge of protein structures is also instrumental for learning how to interfere with such processes, in particular by designing more powerful antibodies, or small compound inhibitors. Determining the structure of proteins is therefore a key aspect to progress in better management of health and biotechnology problems. Along the last four decades, the development of biochemistry and structural biology has revealed that the proteins are much more mobile than what was expected from the first structures obtained using X-ray diffraction in the fifties. In addition, the discovery of amyloid peptides pointed out the importance of disorder in pathological processes and about twenty years ago, the importance of intrinsic disordered proteins (IDP) in normal physiological processes was recognized.

spécialité

Chimie

laboratoire

LPCT - Laboratoire de Physique et Chimie Théoriques