Determining the structures of large proteins and protein complexes by NMR

摘要

Recent advances in mutlidimensional NMR methodology to obtain ~1H, ~15N and ~13C resonance assignments, interproton-distance and torsion-angle restraints, and restraints that characterize long-range order have, coupled with new methods of structure refinement, permitted solution structures of proteins in excess of 250 residues to be solved. These developments may permit the determination by NMR of the structures of macromolecules up to 50-60 kDa thereby bringing into reach numerous systems of considerable biological interest, including a large variety of protein-protein and protein-nucleic-acid complexes.