Determining the structures of large proteins and protein complexes by NMR
Determining the structures of large proteins and protein complexes by NMR
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DOI：
10.1016/s0167-7799(97)01135-9
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发表时间：
1998-01-01
影响因子：
17.3
通讯作者：
Gronenborn, AM
中科院分区：
文献类型：
--
作者：
Clore, GM;Gronenborn, AM
获得 H-1、N-15 和 C-13 共振分配、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 NMR 方法的最新进展，再加上新的结构细化方法，使得能够解析超过 250 个残基的蛋白质的溶液结构。这些进展可能允许通过 NMR 测定高达 50-60 kDa 的大分子结构，从而实现许多具有重要生物学意义的系统，包括多种蛋白质-蛋白质和蛋白质-核酸复合物。
Recent advances in multidimensional NMR methodology to obtain H-1, N-15 and C-13 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.