Effect of Deuteration on the Accuracy of HN–HN Distance Constraints

✍ Scribed by Deborah M. Briercheck; Gordon S. Rule

• Publisher: Elsevier Science
• Year: 1998
• Tongue: English
• Weight: 94 KB
• Volume: 134
• Category: Article
• ISSN: 1090-7807
• DOI: 10.1006/jmre.1998.1511

✦ Synopsis

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 H ␣ 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 Å 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.