Briercheck D M, Rule G S
Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania, USA.
J Magn Reson. 1998 Sep;134(1):52-6. doi: 10.1006/jmre.1998.1511.
The effect of deuteration on the measurement of HN-HN distances in moderately sized (15 kDa) proteins is discussed. Data are presented for a 15 kDa protein which is 95% deuterated on the Halpha position, and partially (70%) deuterated at other aliphatic sites. Deuteration of the protein increases the signal intensity of HN-HN cross peaks in NOESY spectra such that dipolar couplings between protons 4-5 A apart are readily detected. Experimental data and computer simulations show that either perdeuteration or partial deuteration of the protein increases the accuracy of amide-amide distance constraints. Thus, partial deuteration can be used to obtain more accurate long-range distance constraints for structure determination by NMR.
讨论了氘代对中等大小（15 kDa）蛋白质中HN-HN距离测量的影响。给出了一种15 kDa蛋白质的数据，该蛋白质在Hα位置95%氘代，在其他脂肪族位点部分（70%）氘代。蛋白质的氘代增加了NOESY谱中HN-HN交叉峰的信号强度，使得相距4-5 Å的质子之间的偶极耦合易于检测。实验数据和计算机模拟表明，蛋白质的全氘代或部分氘代均可提高酰胺-酰胺距离约束的准确性。因此，部分氘代可用于获得更准确的长程距离约束，以通过核磁共振确定结构。
