Résonance magnétique nucléaire
Résonance Magnétique Nucléaire – Aspects conceptuels
Les observables RMN: Une source d’informations structurales et dynamiques pour les biomacromolécules - Carine van Heijenoort (ICSN, Gif sur Yvette) - Présentation au format pdf
After a rapid introduction on NMR spectroscopy principles, the key NMR parameters valuable for the analysis of biomolecules structure and dynamics will be presented: Chemical shifts will be analyzed as a source of secondary structure element and a tool to decipher the localization of interacting partners, together with binding constant parameters. Relaxation will be introduced as a tool to analyze ps-to-ns motions, as well as ms--to-us dynamics. Scalar couplings and dipolar interactions will finally be described as a source to extract orientational restraints and dynamical information.
Contributions of NMR to structural biology: multi-scale spatial and temporal approaches – Nathalie Sibille (CBS, Montpellier) - Présentation au format pdf
In a context of deciphering, understanding and predicting the function of biological macromolecules, NMR probes the electronic environment of nuclei and their time evolution over a uniquely wide range of time-scale and at atomic resolution. The relevant NMR parameters and motional time scales will be described through the study of biological processes such as protein folding, functional disorder, catalytic, regulatory or signalization processes, or molecular recognition.
Introduction to biomolecular solid-state NMR spectroscopy - Marie Renault (IPBS, Toulouse) - Présentation au format pdf
Biomolecular applications of NMR spectroscopy are often merely associated with soluble molecules or magnetic resonance imaging. However, since the late 1970s, solid-state NMR (ssNMR) spectroscopy has demonstrated its ability to provide atomic-level insight into complex biomolecular systems ranging from lipid bilayers to complex biomaterials. The perspectives of gaining atomic-resolution insight into objects that were so far out of reach for solution-state NMR or crystallography have been a major driving force for the development of the technique. Protein structures of increasing size and complexity are nowadays being determined by ssNMR, and interactions can be probed in complex environments, including entire cells and cell walls. This lecture reports on current approaches to study the structure and dynamics of biosolids and highlights recent progress in using ssNMR spectroscopy at the interface of structural and cellular biology.
Résonance Magnétique Nucléaire – Aspects pratiques
TP : Etudes de cas en RMN en phase liquide: Le spectre 15N HSQC pour la caractérisation rapide et simple de la structure/dynamique de biomacromolécules
Une aide à la prise en main de CCPNMR et le tutorial du TP
TP : Etude de cas en RMN du solide