Skip to Main content Skip to Navigation
Theses

Du Désordre Conformationnel des Protéines Structurées et Intrinsèquement Désordonnées par Résonance Magnétique Nucléaire

Abstract : Biological macromolecules are, by essence, dynamical systems. While the importance of this flexibility is nowadays well established, the accurate characterization of the conformational disorder of these systems remains an important challenge. Nuclear magnetic resonance spectroscopy is a unique tool to probe these motions at atomic level, through the analysis of spin relaxation or residual dipolar couplings. The latter allows all motions occurring at timescales faster than the millisecond to be investigated, including physiologically important timescales. The information presents in those couplings is interpreted here using mainly analytical approaches in order to quantify the amounts of dynamics present in folded protein, to determine the direction of those motions and to obtain structural information within this conformational disorder. These analytical approaches are complemented by numerical methods, that allowed the observation of phenomena from a different point of view or the investigation of other systems such as intrinsically disordered proteins. All of these studies demonstrate an important complementarity between structural order and conformational disorder.
Complete list of metadatas

https://tel.archives-ouvertes.fr/tel-00592552
Contributor : Loic Salmon <>
Submitted on : Thursday, May 12, 2011 - 9:58:23 PM
Last modification on : Wednesday, July 15, 2020 - 1:02:02 PM
Long-term archiving on: : Friday, November 9, 2012 - 11:20:14 AM

Identifiers

  • HAL Id : tel-00592552, version 1

Collections

Citation

Loïc Salmon. Du Désordre Conformationnel des Protéines Structurées et Intrinsèquement Désordonnées par Résonance Magnétique Nucléaire. Biophysique [physics.bio-ph]. Université de Grenoble, 2010. Français. ⟨tel-00592552⟩

Share

Metrics

Record views

575

Files downloads

250