Clore G M, Gronenborn A M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Healthy, Bethesda, MD 20892-0520, USA.
Trends Biotechnol. 1998 Jan;16(1):22-34. doi: 10.1016/S0167-7799(97)01135-9.
Recent advances in multidimensional 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 structure 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 50-60kDa, thereby bringing into reach numerous systems of considerable biological interest, including a large variety of protein-protein and protein-nucleic-acid complexes.
用于获得¹H、¹⁵N和¹³C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的多维核磁共振方法的最新进展,与新的结构精修方法相结合,使得超过250个残基的蛋白质溶液结构得以解析。这些进展可能使通过核磁共振确定高达50 - 60 kDa的大分子结构成为可能,从而将众多具有重大生物学意义的系统纳入研究范围,包括各种各样的蛋白质 - 蛋白质和蛋白质 - 核酸复合物。