Extended Data Fig. 8: Conformation of monoglutamylated α1A/B(E445) tubulin tail peptides in solution.
From: Tubulin code eraser CCP5 binds branch glutamates by substrate deformation
a, b. Alpha (a) and amide (b) regions of the NOESY spectrum of the unbound α1A/B(E445) peptide. The red-dashed ovals indicate where the contact signals would appear if the peptide were to adopt the conformation observed in the CCP5:Glu-P-peptide 1 structure. Because the residue in the +3 position is a glycine, it has two potential alpha peaks, 2a and 2b. The weak, off-center signal in the region of peak 2b is likely from G(−3), which has alpha resonances similar to G(+3). The off-diagonal NOE cross peaks in (b) were used for assignment of sequential residues, and their moderate intensity rules out beta-strand secondary structure. The splitting of the signals in the x-dimension corresponds to the HNHα J-coupling. c, d. HNHα J-couplings (JHNHα) plot (c) and Sequential to intra HαHN NOE intensity ratios (d) of monoglutamylated α1A/B(E445) tubulin tail peptide. Bars represent estimated errors determined as detailed in legend for panels (a) and (b).
