Reversible monomer-oligomer transition in human prion protein

Figures & data

Figure 1 Circular dichroism spectra of monomeric oxidized huPrP^C(23–231) (blue) and oligomeric reduced huPrP^C(23–231) (red), recorded at 298 K. Monomeric oxidized huPrP^C(23–231) (0.12 mM) was prepared in a buffer solution containing 10 mM sodium acetate and 10 mM tris-acetate, pH 8.0 and oligomeric reduced huPrP^C(23–231) (1.9 mM) was prepared in a buffer solution containing 10 mM sodium acetate, 10 mM tris-acetate, pH 4.0.

Figure 2 Atomic force microscopic image of oligomeric reduced huPrP^C(23–231), recorded at room temperature.

Figure 3 Trp fluorescence spectra of oligomeric reduced huPrP^C(23–231) recorded at varying pressures and at 298 K.

Figure 4 ¹H-NMR spectral changes of monomeric and oligomeric huPrP^C(23–231) caused by pressure-jump up and down. (A) ¹H NMR spectrum of (¹⁵N-enriched) monomeric huPrP^C(23–231) at 293 K at 0.3 MPa. (B) The same as (A), but at 200 MPa. (C) ¹H NMR spectrum of reduced oligomeric huPrP^oligo(23–231) at 298 K at 0.3 MPa. (D) The same as (C), but 30 min after the pressure-jump from 0.3 MPa to 200 MPa. (E) The same as (C), but 46 h after the pressure-jump from 0.3 MPa to 200 MPa. (F) The same as (C), but 30 min after the pressure-jump back from 200 MPa to 0.3 MPa. (G) The same as (C), but 9.5 h after the pressure-jump back from 200 MPa to 0.3 MPa.

Figure 5 Oligomeric and monomeric of huPrP^{C 1}H NMR recorded at varying pressures. (A) ¹H NMR spectra of huPrP^C(23–230) recorded at 293 K, pH 4.8 and at 0.1 MPa. Resonances of selected protons are labeled: (1) Leu130 H^δ2 (2) Leu125 H^δ2 (3) Ile139 H^δ1 (4) Ile182 H^δ1 (5) Ile182 H^γ2 (6) DSS (internal reference) (7) Leu130 H^δ1 (8) Ile139 H^γ2. (B) ¹H NMR spectra of huPrP^C(23–230) recorded at 293 K, pH 4.8 and at 200 MPa. [(A and B) data were reprinted from ref. 8]. (C) ¹H NMR spectra of huPrP^oligo(23–231) recorded at 298 K, pH 4.0 and at 0.3 MPa. (D) ¹H NMR spectra of huPrP^oligo(23–231) recorded at pressure jump up to 200 MPa after 46 h and at 298 K, pH 4.0. (E) ¹H NMR spectra of huPrP^oligo(23–231) recorded at pressure jump back to 0.3 MPa after 9.5 h and at 298 K, pH 4.0.

Kachel N, Kremer W, Zahn R, Kalbitzer HR. Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy. BMC Structural Biology 2006; 6:16

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