Zhu Guang, Xia Youlin, Lin Donghai, Gao Xiaolian
Department of Biochemistry, The Hong Kong University of Science and Technology, Hong Kong, SAR People's Republic of China.
Methods Mol Biol. 2004;278:161-84. doi: 10.1385/1-59259-809-9:161.
Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.
基于横向弛豫优化谱（TROSY）的核磁共振（NMR）实验可用于获得化学位移归属以及J耦合常数、残余偶极耦合和核Overhauser效应（NOE）的值，以用于蛋白质的结构研究，如第5章所述。此外，基于TROSY的NMR实验的应用可扩展到分子动力学、酰胺质子交换率和氢键的测量。本章将描述这些实验。
