Ding Keyang, Gronenborn Angela M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 130, Bethesda, MD 20892-0520, USA.
J Magn Reson. 2003 Aug;163(2):208-14. doi: 10.1016/s1090-7807(03)00081-8.
Sensitivity-enhanced versions of the IPAP, TROSY-anti-TROSY, and E.COSY experiments for measuring one-bond 15N-1HN couplings are presented. Together with the previously developed sensitivity-enhanced E.COSY-type HSQC experiment they comprise a suite of sensitivity-enhanced experiments that allows one to chose the optimal spectrum for accurate measurement of one-bond 15N-1HN residual dipolar couplings in proteins. Since one-bond 15N-1HN residual dipolar couplings play uniquely important roles in structural NMR, these additional methods provide further tools for improving structure determination of proteins and other biological macromolecules.
本文介绍了用于测量单键¹⁵N-¹Hᴺ偶合的IPAP、TROSY-反TROSY和E.COSY实验的灵敏度增强版本。它们与之前开发的灵敏度增强的E.COSY型HSQC实验一起，构成了一套灵敏度增强实验，使人们能够选择最佳光谱，以准确测量蛋白质中的单键¹⁵N-¹Hᴺ剩余偶极偶合。由于单键¹⁵N-¹Hᴺ剩余偶极偶合在结构核磁共振中起着独特的重要作用，这些额外的方法为改进蛋白质和其他生物大分子的结构测定提供了更多工具。
