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Figure 1 | BMC Structural Biology

Figure 1

From: Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy

Figure 1

First order pressure coefficients of the 1HN and of the 15NH chemical shifts taken from the TROSY-HSQC spectra of hu PrP(23–230). Spectra were measured at 293 K at 600 MHz proton frequency. The absolute values of the conformation dependent pressure coefficients |B1*(H)| (a) for the 1HN shifts and of the uncorrected pressure coefficient |B1(N)| (b) for the 15NH chemical shifts are plotted as function of the sequence position. The mean values of |B1*(H)| and |B1(N)| for the structured C-terminal and the unstructured N-terminal part of the protein are shown as solid lines, the mean values plus one standard deviation as dashed lines. The secondary structure is symbolized by arrows (β-strands) and lanyards (α-helices). P marks prolines, X other residues that are not visible or not assigned in the TROSY spectra.

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