Characterisation of intrinsically disordered proteins by nuclear magnetic resonance
type: Dataset
description: Around 40% of the human genome does not fold into stable three-dimensional structures but are either unfolded, or contain unfolded regions of significant length. The inherent flexibility of this class of proteins is essential for their function in a vast range of biomolecular process such as molecular recognition. In order to take into account the specificity of these interactions, it has been necessary to invent new approaches to study and interpret their behaviour. Nuclear magnetic resonance spectroscopy is a unique atomic resolution probe which is sensitive to a very large range of time scales. We combine experimental NMR data with a statistical model describing the energy landscape of unfolded state : the explicit ensemble description. This model is a discrete representation of the different states of theses proteins. Combining chemical shifts, residual dipolar couplings and paramagnetic relaxation enhancement, it is then possible to develop a molecular description of the unfolded state caracterising both the local and long-range information of intrinsically disordered proteins.
identifier: NNT: 2012GRENY103
issued: 2026-05-09T11:13:45.691683
language: fr
modified: 2026-05-09T11:13:45.691688
contact point: Organization
  fn: CCSD
keyword: conformational-distribution
keyword: couplages-dipolaires-residuels
keyword: dynamique-des-proteines
keyword: echantillonnage-conformationnel
keyword: infoeu-reposemanticsdoctoralthesis
keyword: instrinsically-unfolded-proteins
keyword: nuclear-magnetic-resonance
keyword: physphysphys-bio-phphysics-physicsphysics-physicsbiological-physics-physicsbio-ph
keyword: protein-dynamics
keyword: protein-tau
keyword: proteine-tau
keyword: proteines-intrinsequement-desordonnees
keyword: residual-dipolar-couplings
keyword: resonance-magnetique-nucleaire
keyword: sdvbbmbslife-sciences-q-biobiochemistry-molecular-biologystructural-biology-q-biobm
keyword: sdvbbmlife-sciences-q-biobiochemistry-molecular-biology
keyword: theses
landing page: https://theses.hal.science/tel-00870515

Characterisation of intrinsically disordered proteins by nuclear magnetic resonance
type: Distribution
format: HTML
issued: 2026-05-09T11:13:45.698406
modified: 2026-05-09T11:13:45.670914
access URL: https://theses.hal.science/tel-00870515

test_moissonnage_selune
type: Agent