Étude historique de la visualisation des protéines

The history of the visualization of proteins is inseparable from that of structural biology that studies the structure and spatial organization of biological macromolecules. The ancients had initially imagined proteins as organic nitrogen nuclei surrounded by a mineral copula. The determination at the atomic scale of the 3D structure of proteins uses biophysical approach techniques developed in the first half of the twentieth century. Crystallography by X-ray diffraction provides an electron density map. Nuclear magnetic resonance spectroscopy defines a map inter-proton distances and angles of torsion of the backbone of the protein. Electron cryomicroscopy gives a direct image of the input molecule in its aqueous medium. These three families of techniques are evolving dramatically to grow in accuracy, resolution and spatial and temporal analysis. Today these methods converge with interactive databases and dynamic modeling bioinformatics tools towards defining models of «protein ligands» bounds, the discovery of pharmacological inhibitors, the prediction of macromolecular structure and an increased understanding of folding diseases abnormal proteins.