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Figure 1

From: Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins

Figure 1

Comparison of MAS solid-state NMR 1H,13C correlation spectra obtained for protonated and deuterated samples of a microcrystalline α-spectrin SH3 domain. Top: Methyl region of the spectra from protonated (left) and α-ketoisovalerate (CH3) labelled (right) samples33 (recorded with B0 = 11.8 T at 111 kHz MAS frequency). Middle: Methyl region of 1H,13C correlation spectra from 25% (left, recorded with B0 = 20 T at 40 kHz MAS frequency) and 5% (right, recorded with B0 = 14.1 T at 20 kHz MAS frequency) RAP24 labelled samples. Bottom: Backbone Hα,Cα correlation spectra for protonated (left) and 25% RAP (right) labelled samples.

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