Figure 4. Solution NMR characterization of the fusion peptide.

(A) Superimposed 900 MHz ¹H-¹⁵N HSQC spectra of ¹⁵N-labeled fusion peptide bound to unlabeled TAZ1 (blue) and free in solution (coral). Representative amide cross peaks that undergo large shifts in position upon complex formation are labeled. (B) Intensities of backbone amide cross peaks from ¹H-¹⁵N HSQC spectra of ¹⁵N-labeled fusion peptide in complex with unlabeled TAZ1. Intensities are normalized to the intensity of the backbone amide cross peak of the C-terminal fusion peptide residue (N67). Boxes above the plot indicate the positions of the CITED2 α_A and HIF1α α_B and α_C binding motifs. Residues for which backbone amide cross peaks are broadened beyond detection are denoted by blue circles.