Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward.
Starting only a few years ago, many solid-state NMR spectroscopy laboratories have become engaged in solving the complete structures of biological macromolecules using high-resolution methods based on magic angle spinning. These efforts typically involve structurally homogeneous samples, and utilize recently developed pulse sequences for the sequential correlation of resonances, the detection of tertiary contacts and the characterization of torsion angles. Thereby, systems have been studied that evaded other, more established, structure determination methods.
McDermott
Ann E
AE
Columbia University, Department of Chemistry, MC 3113, 3000 Broadway, New York, New York 10027, USA. aem5@columbia.edu
D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins