NMR structures of proteins and protein complexes beyond 20,000 M(r).
Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.
Clore
G M
GM
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA. clore@vger.niddk.nih.gov
Gronenborn
A M
AM
D046911:Macromolecular Substances; D008433:Mathematics; D008961:Models, Structural; D008970:Molecular Weight; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D046911:Macromolecular Substances; D011506:Proteins