Vander Kooi C W, Kupce E, Zuiderweg E R, Pellecchia M
Department of Chemistry, University of Michigan, Ann Arbor 48109, USA.
J Biomol NMR. 1999 Dec;15(4):335-8. doi: 10.1023/a:1008387305293.
Residual heteronuclear dipolar couplings obtained from partially oriented protein samples can provide unique NMR constraints for protein structure determination. However, partial orientation of protein samples also causes severe 1H line broadening resulting from residual 1H-1H dipolar couplings. In this communication we show that band-selective 1H homonuclear decoupling during data acquisition is an efficient way to suppress residual 1H-1H dipolar couplings, resulting in spectra that are still amenable to solution NMR analysis, even with high degrees of alignment. As an example, we present a novel experiment with improved sensitivity for the measurement of one-bond 1HN-15N residual dipolar couplings in a protein sample dissolved in magnetically aligned liquid crystalline bicelles.
从部分取向的蛋白质样品中获得的残留异核偶极耦合可为蛋白质结构测定提供独特的核磁共振（NMR）约束条件。然而，蛋白质样品的部分取向也会因残留的1H-1H偶极耦合导致严重的1H谱线展宽。在本通讯中，我们表明在数据采集过程中进行带选择性1H同核去耦是抑制残留1H-1H偶极耦合的有效方法，即使在高度取向的情况下，所得光谱仍适用于溶液NMR分析。例如，我们展示了一个新颖的实验，该实验提高了在溶解于磁取向液晶双分子层中的蛋白质样品中测量一键1HN-15N残留偶极耦合的灵敏度。
