NMR methods for the study of protein structure and dynamics.
An understanding of the role played by a protein in cellular function requires a detailed picture of its three-dimensional structure as well as an appreciation of how the structure varies as a function of time as a result of molecular dynamics. Over the past several years, multidimensional, multinuclear solution NMR spectroscopy has become a powerful technology for obtaining both structural and dynamical information on proteins and protein-ligand systems. In the present review, a number of new methodological advances are highlighted that have significantly improved the quality of NMR spectra of biomolecules and have increased the molecular weight limitations previously imposed on NMR-based structural studies of macromolecules. Applications of this technology to a number of protein systems currently studied in my laboratory are presented.
Kay
L E
LE
Department of Medical Genetics, University of Toronto, ON, Canada.
D002247:Carbon Isotopes; D003903:Deuterium; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D011487:Protein Conformation; D013816:Thermodynamics; D018909:src Homology Domains
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D003903:Deuterium