Clore G M, Gronenborn A M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Nat Struct Biol. 1997 Oct;4 Suppl:849-53.
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.
多维核磁共振技术在获取共振归属、质子间距离和扭转角限制以及表征长程有序的限制方面的最新进展,再加上新的结构优化方法,使得超过250个残基的蛋白质溶液结构得以解析。