Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 75, Issue 10-12, Pages 417-427Publisher
SPRINGER
DOI: 10.1007/s10858-021-00386-6
Keywords
Solid-State NMR; Proton detection; Fast MAS; Protein NMR
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Funding
- European Research Council (ERC) under the European Unions Horizon 2020 research and innovation program (ERC-2015-StG) [639020]
- FranceAgriMer
- CNIV through the program PNDV (project ATOMIVINE) [297772]
- IdEx Bordeaux (Chaire d'Installation) [ANR-10-IDEX-03-02]
- Swiss National Science Foundation [P2EZP2_184258]
- JSPS KAKENHI [20K05483]
- JST-Mirai Program (Japan) [JPMJMI17A2]
- Swiss National Science Foundation (SNF) [P2EZP2_184258] Funding Source: Swiss National Science Foundation (SNF)
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The approach combines double-quantum C-13 spectroscopy and fast MAS to achieve sequential assignment of insoluble proteins, providing efficient sensitivity and useful spectral features for resonance assignment process.
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 (H-1) detection at fast magic-angle spinning (MAS) has considerably increased the analytical capabilities of the technique, enabling the acquisition of H-1-detected fingerprint experiments in few hours. Here an approach based on double-quantum (DQ) C-13 spectroscopy, detected on H-1, 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 H-1 detected experiments correlating a C-13 DQ dimension respectively to its intra-residue and sequential (15) N-H-1 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.
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