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Master Thesis

Molecular Simulations of membrane fission mediated by BARS protein

Abstract : The CtBP1/BARS protein has been shown to cause ATP-hydrolysis-independent membrane fission both in Golgi membranes and liposomes. This memoir analyzes how one putative amphipathic 16-residue α-helical fragment from the C-teminal domain of BARS interacts with membranes using in silico Molecular Simulations. To observe these interactions, we used Molecular Dynamics simulations at atomistic and coarsegrained scales. We used several membrane models ranging from very simple homogeneous lipid bilayers to ones mimicking the composition of the Golgi membranes. These membranes were confronted to several models of the protein fragment varying in secondary structure. Our results show that the protein fragment undergoes a lot of structural change. It interacts with model membranes by sticking to them, mostly via electrostatic interactions between positive residues and negative lipids. We cannot confirm that its structure or properties when detached from the rest of the protein are the same as observed in vivo or in vitro. Running more simulations with bigger domaines of the protein or with an increasing concentration of the peptide in the future could provide more insight on how physical properties of membranes are influenced by the protein and help unveil the mechanism behind membrane fission.
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Master Thesis
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Submitted on : Tuesday, November 19, 2019 - 10:01:53 AM
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  • HAL Id : dumas-02369656, version 1



Thomas Le Métayer. Molecular Simulations of membrane fission mediated by BARS protein. Life Sciences [q-bio]. 2019. ⟨dumas-02369656⟩



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