Proteins are large flexible molecules that can adopt several conformations having different biological function. These conformations are controlled by a set of intramolecular interactions (hydrogen bonds, dispersive and steric forces...) as well as intermolecular interactions (with a solvent molecule or an ion). A full understanding of the structure of small model systems at the molecular scale is needed in order to identify the forces responsible for the molecular folding.



The approach consists of isolating the folded molecules in the gas phase, with or without few molecules of solvent, and analyse their structure by IR and UV spectroscopy. These techniques give a fingerprint of the H-bond network that is precise enough to entirely characterise the shape of the system. These results will help the development of new simulation tools (quantum chemistry, force fields).



The research project will consist of studying short solvated protein sequences in order to assign and analyse their structures, and estimate the solvation effects. The main part of the project will be experimental, and the PhD student will access a set of equipment (OPO laser, UV dye laser, time-of-flight mass spectrometry, molecular beams) and techniques (laser desorption, IR/UV double resonance, formation of solvated systems in the gas phase...). The PhD student will also have the opportunity to carry out quantum chemistry calculations, and lead both the experimental and theoretical sides of the project.