Details

Autor(en) / Beteiligte

• Lends, Alons
• Berbon, Mélanie
• Habenstein, Birgit
• Nishiyama, Yusuke
• Loquet, Antoine

Titel

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

Ist Teil von

• Journal of biomolecular NMR, 2021-12, Vol.75 (10-12), p.417-427

Ort / Verlag

Dordrecht: Springer Netherlands

Erscheinungsjahr

2021

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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 ( 1 H) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of 1 H-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) 13 C spectroscopy, detected on 1 H, 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 1 H detected experiments correlating a 13 C DQ dimension respectively to its intra-residue and sequential 15  N- 1 H 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.