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Fig. 1 | BMC Molecular and Cell Biology

Fig. 1

From: The binding affinity of PTPN13’s tandem PDZ2/3 domain is allosterically modulated

Fig. 1

Superposition of 2D 1H-15N-HSQC NMR spectra recorded on the 15N-enriched single PDZ2 domain (12 kDa) recorded at 600 MHz proton frequency at 298 K and pH 7.4 upon titration with the C-terminal peptide PRK2. a 2D 1H-15N-HSQC NMR spectra of PDZ2 upon titration with PRK2 at various molar ratios up to 1:30 [Black (ligand free), red (1:1), green (1:3), blue (1:5), yellow (1:7), magenta (1:10), cyan (1:20), and red (1:30)]. b Weighted chemical shift perturbation (CSP) of residue T30 from PDZ2 as a function of PRK2 peptide concentration. Curve fitting was carried out in ORIGIN (www.originlab.com). c 2D 1H-15N-HSQC NMR spectra of PDZ3 upon titration with PRK2 at various molar ratios up to 1:10 recorded at 700 MHz proton frequency at 298 K and pH 7.4 [Black (ligand free), red (1:2), green (1:4), blue (1:6), magenta (1:8), and cyan (1:10)]

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