High-resolution solid-state MAS NMR of proteins-Crh as an example.
Solid-state NMR spectroscopy provides unique possibilities for the structural investigation of insoluble molecules at the atomic level. Recent efforts aim at solving the complete structures of biological macromolecules using high-resolution magic angle spinning NMR. Structurally homogenous samples of [(13)C,(15)N]-labeled proteins have to be used in this type of studies. Microcrystalline model proteins present valuable tools for the developments of methods towards this goal. This review discusses recent progress in the field, using the Crh protein as an illustrative example. We discuss strategies for resonance assignments and for the determination of structure and dynamics, as well as techniques for the detection of protein interaction partners and folding mechanisms by solid-state NMR methods.
Böckmann
Anja
A
IFR 128 BioSciences Lyon-Gerland, IBCP UMR 5086 CNRS/Université de Lyon Claude Bernard, 7 passage du Vercors, 69367 Lyon, France. a.bockmann@ibcp.fr
D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D003460:Crystallization; D006018:Glycols / Q000737:chemistry; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D006018:Glycols; D009587:Nitrogen Isotopes; D011092:Polyethylene Glycols; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr; C011480:hexylene glycol