Fig. 5: NMR spectroscopy to map the Spy binding surface of AnFld.
From: Mechanism of the small ATP-independent chaperone Spy is substrate specific
a A plot of the ratios of intensities of each assigned cross peak in the [1H-15N]–TROSY NMR spectra of AnFld WT in the presence of sub-stoichiometric amount of Spy (0.75×) and in the absence of Spy [I(+Spy) and I(−Spy), respectively]. The asterisks denote unassigned residues in the spectra, and the dashed red line shows the cutoff of average peak broadening for all mapped residues. b, c A red-to-blue color scale has been used to map the NMR peak intensity ratios on the crystal structure of AnFld (Protein Data Bank ID code 1FTG) in b ribbon and c surface representations. Red and blue represent the highest and lowest intensity ratios in the dataset at 0.784 and −0.002, respectively. A lower intensity ratio, i.e., [I(+Spy)/I(−Spy)] is indicative of a higher degree of backbone perturbation in the presence of Spy. The unassigned residues in AnFld are show in gray.
