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Default Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.

Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.

Related Articles Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.

J Magn Reson. 2014 Sep 20;248C:8-12

Authors: Krushelnitsky A, Zinkevich T, Reif B, Saalwächter K

Abstract
(15)N NMR relaxation rate R1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s-ms timescale range. On the basis of a comparison of 2D site-resolved with 1D integrated (15)N spectral intensities, we demonstrate that the significant fraction of broad signals in the 2D spectrum exhibits the most pronounced slow mobility. We show that (15)N R1?'s in proton-diluted protein samples are practically free from the coherent spin-spin contribution even at low MAS rates, and thus can be analysed quantitatively. Moderate MAS rates (10-30kHz) can be more advantageous in comparison with the rates >50-60kHz when slow dynamics are to be identified and quantified by means of R1? experiments.


PMID: 25282442 [PubMed - as supplied by publisher]



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