Saturday, March 17, 2012

Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for structure and dynamics

This article is not directly related to DNP-enhanced NMR spectroscopy. However, since deuteration of the sample material plays an important role in DNP spectroscopy, this article could be of great interest to researchers in the field.

Bernd, R., Ultra-high resolution in MAS solid-state NMR of perdeuterated proteins: Implications for structure and dynamics. J. Magn. Reson., 2012. 216(0): p. 1-12.


High resolution proton spectra are obtained in MAS solid-state NMR in case samples are prepared using perdeuterated protein and D2O in the recrystallization buffer. Deuteration reduces drastically 1H, 1H dipolar interactions and allows to obtain amide proton line widths on the order of 20 Hz. Similarly, high-resolution proton spectra of aliphatic groups can be obtained if specifically labeled precursors for biosynthesis of methyl containing side chains are used, or if limited amounts of H2O in the bacterial growth medium is employed. This review summarizes recent spectroscopic developments to access structure and dynamics of biomacromolecules in the solid-state, and shows a number of applications to amyloid fibrils and membrane proteins.