Effect of Deuteration on the Accuracy of HN–HN Distance Constraints
Authors: Briercheck, D.M.; Rule, G.S.
Source: Journal of Magnetic Resonance, Volume 134, Number 1, September 1998 , pp. 52-56(5)
Publisher: Academic Press
Abstract: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 Hα 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.
Document Type: Research Article
Affiliations: Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania
Publication date: September 1998