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. Author manuscript; available in PMC: 2017 Jun 28.
Published in final edited form as: J Mol Biol. 2010 Mar 31;398(5):730–746. doi: 10.1016/j.jmb.2010.03.047

Fig. 3.

Fig. 3

Syndecan1 and Caspr4 peptides induce distinct changes in 1H-15N heteronuclear single quantum coherence spectra of the Tiam1 PDZ domain. The ligand-free protein (black peaks) was titrated with either (a) the Syndecan1 or (b) the Caspr4 peptide (red peaks) to a final PDZ to peptide molar ratio of 1:3. (c and d) The weighted changes in chemical shift upon titration; residues with a chemical shift change >σ above the average are colored red, and residues with a chemical shift change between the average and 1σ are colored yellow. Residues that did not have a significant change in chemical shift are colored gray. The changes in chemical shift for (e) Syndecan1 and (f) Caspr4 are mapped onto the spacefilling model of the Tiam1 PDZ/Model crystal structure. Residues colored red and yellow follow the convention described above. Unassigned residues are black and residues unchanged during the titration are colored gray.