Determining the structures of large proteins and protein complexes by NMR

被引：224
作者：
Clore, GM [1 ]
Gronenborn, AM [1 ]
机构：
[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA
来源：
TRENDS IN BIOTECHNOLOGY | 1998年 / 16卷 / 01期
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1016/S0167-7799(97)01135-9
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
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.
引用
收藏
页码：22 / 34
页数：13
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