Fig. 4: HMT applied to enhance correlations in folded proteins. | Nature Communications

Fig. 4: HMT applied to enhance correlations in folded proteins.

From: Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids

Fig. 4

Conventional vs HMT NOESY spectra recorded for LA5 a and ubiquitin b samples. Notice how the 23.5 T field is sufficient to resolve almost entirely the amide/amino resonances in these structured peptides (regions between 6.6–9.5 ppm) and enable fast, highly sensitive NOESY experiments by Hadamard MT. Conventional experiments were acquired with 300 ms and 250 ms mixing, respectively (for maximum NOESY cross-peaks); HMT employed 6 × 150 ms and 6 × 140 ms looped encoding. Spectra were acquired at 1 GHz using a Bruker Avance Neo console equipped with a TCI cryoprobe.

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