Développement de nouvelles sondes pour l'analyse par RMN des fonctions cellulaires des biomolécules

Abstract : Most NMR studies are carried out in vitro, but the structure and dynamics of some biomolecules inside cells differ from those in vitro. It thus becomes interesting to analyze biomolecules such as proteins in their natural environment: the cell. Recent progress of in cell NMR allowed to better understand the behaviour of proteins: their dynamics and their interactions with other biomolecules in the cell. But the low concentration of proteins leads to low signal intensity. Moreover, the viscosity of the environment induces faster transverse relaxation, resulting in line broadening for proteins signals. The use of the Long-Lived States and Coherences (LLS and LLC, respectively) as well as dissolution Dynamic Nuclear Polarization (dissolution-DNP) can improve NMR observations in cells. LLS were used to understand and characterize the structure of the N-terminal domain of c-Src, which is intrinsically disordered. To follow the phosphorylation of proteins, a first preliminary study of a 21-aa peptides derived from IKBα electroporated into HepG2 cell lines was carried out.
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Laetitia Fernandes. Développement de nouvelles sondes pour l'analyse par RMN des fonctions cellulaires des biomolécules. Chimie analytique. Université Sorbonne Paris Cité, 2015. Français. ⟨NNT : 2015USPCB095⟩. ⟨tel-01535676⟩

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