Figure 1: Chemical shift and cross peak volume perturbation by xenon binding. | Scientific Reports

Figure 1: Chemical shift and cross peak volume perturbation by xenon binding.

From: Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain

Figure 1

Maximum combined chemical shift changes Δδcomb (A) and relative changes of the cross peak volumes −ΔVmax/V0 = (V0 − V(cmax))/V0 (B) observed in the [1H, 15N]-HSQC spectra of 15N enriched huPrP(23–230) are plotted as a function the residue number j at 293 K. V0 is the cross peak volume in the absence of xenon and V(cmax) the volume at the maximum xenon concentration cmax of 61.6 mM. Solid line, standard deviation σ0 to zero, dotted line, 2σ0. P marks prolines, X other residues that are not visible or are not assigned in the spectra, 0 residues where satisfactory values could not be obtained. The error bars correspond to the standard errors. White bars represent residues that do not show saturation behaviour at the highest xenon concentration.

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