Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins

2009/07/16 by Victoria A. Higman, Victoria Ann Higman, Jeremy Flinders +8 · 2 citations
Chemistry · Medicine · Physics and Astronomy · #Advanced MRI Techniques and Applications #Advanced NMR Techniques and Applications #NMR spectroscopy and applications

paper · doi:10.1007/s10858-009-9338-7

openalex publication_date 2009/07/16 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/02

Citations

• Solid state NMR sequential resonance assignments and conformational analysis of the 2×10.4 kDa dimeric form of the Bacillus subtilis protein Crh
• Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins

Cited by

• Structural characterization of supramolecular assemblies by 13C spin dilution and 3D solid-state NMR
• Segmental isotope labelling and solid-state NMR of a 12 × 59 kDa motor protein: identification of structural variability