Nathalie Colloc'h holds both D.S. and Ph.D. degrees. She has been a French CNRS Researcher for more than 20 years. She is a specialist in protein crystallography and homology modeling. She participated in numerous homology modeling projects, using hydrophobic cluster analysis method, developed by Jean-Mornon (Paris, France), to analyze the sequence similarity. She determined the first crystallographic structure of urate oxidase and participated in the determination of this structure with various inhibitors. She also determined its structure at high pressure, this structure representing a high-energy conformer which occurs during the catalytic mechanism. During these last years, she has specialized in crystallography under gas pressure, in collaboration with Thierry Prangé (Paris, France). For ten years, she worked with Professor Jacques Abraini (Caen, France), where her main research project was to understand the structural effect of gas on proteins, to unravel their neuroprotective mechanisms. She determined the structures of various proteins under inert gas pressure (xenon, nitrous oxide, krypton, and argon) to understand the mechanism underlying the neuroprotection by inert gases. She also determined the structure of various oxidases or globins under oxygen, nitrogen, or carbon monoxide pressurization to determine the gas binding site and understand their mechanism. Since 2012, she has worked with Myriam Bernaudin (Caen, France) and focuses mainly on protein degradation by carbons ions.
Biography Updated on 2 April 2012