Tolman J R
Section de Chimie, BCH, Université de Lausanne, Switzerland.
Curr Opin Struct Biol. 2001 Oct;11(5):532-9. doi: 10.1016/s0959-440x(00)00245-1.
The introduction of residual dipolar coupling methodology has increased the scope of structural biological problems that can be addressed by NMR spectroscopy. Conformational changes, the relative orientation of domains, and intermolecular complexes can now be characterized accurately and rapidly using NMR. The development of residual dipolar coupling methodology for the rapid recognition of homologous protein folds and for studies of submillisecond timescale dynamics has also seen considerable progress.
残余偶极耦合方法的引入扩大了核磁共振光谱能够解决的结构生物学问题的范围。现在可以使用核磁共振准确且快速地表征构象变化、结构域的相对取向以及分子间复合物。在用于快速识别同源蛋白质折叠以及研究亚毫秒时间尺度动力学的残余偶极耦合方法的发展方面也取得了显著进展。
