Effect of deuteration on the accuracy of HN-HN distance constraints.
| Autor: | Briercheck DM; Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania, USA., Rule GS |
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| Jazyk: | angličtina |
| Zdroj: | Journal of magnetic resonance (San Diego, Calif. : 1997) [J Magn Reson] 1998 Sep; Vol. 134 (1), pp. 52-6. |
| DOI: | 10.1006/jmre.1998.1511 |
| Abstrakt: | 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. (Copyright 1998 Academic Press.) |
| Databáze: | MEDLINE |
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