title: New methods of structure refinement for macromolecular structure determination by NMR.
abstract: Recent advances in multidimensional NMR methodology have permitted solution structures of proteins in excess of 250 residues to be solved. In this paper, we discuss several methods of structure refinement that promise to increase the accuracy of macromolecular structures determined by NMR. These methods include the use of a conformational database potential and direct refinement against three-bond coupling constants, secondary 13C shifts, 1H shifts, T1/T2 ratios, and residual dipolar couplings. The latter two measurements provide long range restraints that are not accessible by other solution NMR parameters.
authors.affiliation: Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. clore@vger.niddk.nih.gov
authors.forename: G M
authors.initials: GM
authors.lastname: Clore
authors.forename: A M
authors.initials: AM
authors.lastname: Gronenborn
mesh_terms: D000818:Animals; D016208:Databases, Factual; D006801:Humans; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D012984:Software
chemical_list: D046911:Macromolecular Substances