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Structure et dynamique de protéines isolées : approches statistiques

Abstract : We present a theoretical study of the thermodynamical properties of polypeptides in the gas phase. The aim of this work is a better understanding of the fundamental mechanisms involved in protein folding. A statistical approach based on Monte Carlo algorithms applied in generalised ensembles, such as Replica Exchange Method or Wang-Landau method, has been used to sample the rugged energy landscape of those molecules. The peptides were composed of 2 to 20 amino acids and have been modelised by the AMBER 96 forcefield. Simulations have been realised in strong relation with experimental progress of the group. We thus tried to understand the influence of the secondary structure on photofragmentation mechanism, the role of entropy in the stabilisation of beta sheets and the effect of intense electric field on peptide conformation.
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Contributor : Pierre Poulain Connect in order to contact the contributor
Submitted on : Thursday, September 14, 2006 - 7:05:41 PM
Last modification on : Wednesday, April 6, 2022 - 11:16:03 AM
Long-term archiving on: : Friday, November 25, 2016 - 11:34:07 AM


  • HAL Id : tel-00094458, version 2



Pierre Poulain. Structure et dynamique de protéines isolées : approches statistiques. Biophysique []. Université Claude Bernard - Lyon I, 2006. Français. ⟨NNT : ⟩. ⟨tel-00094458v2⟩



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