LENDS, Alons; BERBON, Melanie; HABENSTEIN, Birgit; NISHIYAMA, Yusuke; LOQUET, Antoine

doi:10.1007/s10858-021-00386-6

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LENDS, Alons
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

BERBON, Melanie
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

HABENSTEIN, Birgit
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

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Journal of biomolecular NMR. 2021-12-01, vol. 75, n° 10, p. 417-427

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Solid-state NMR spectroscopy is a powerful technique to study insoluble and non-crystalline proteins and protein complexes at atomic resolution. The development of proton (1H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of 1H-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) 13C spectroscopy, detected on 1H, is proposed for fast MAS regime (> 60 kHz) to perform the sequential assignment of insoluble proteins of small size, without any specific deuteration requirement. By combining two three-dimensional 1H detected experiments correlating a 13C DQ dimension respectively to its intra-residue and sequential 15 N-1H pairs, a sequential walk through DQ (Ca + CO) resonance is obtained. The approach takes advantage of fast MAS to achieve an efficient sensitivity and the addition of a DQ dimension provides spectral features useful for the resonance assignment process.< Réduire

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Fast MAS

Protein NMR

Proton detection

Solid-State NMR

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Protein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS

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