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1.

Figure. From: Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.

Figure 2. Fluorescence microscopy of the peptides at pH 5.0. (A) The peptide (aa 166-175 “B”). (B) The peptide (aa 166-175 “NB”). Staining was done with 7.5 μM ThT.

Evgeny E. Bezsonov, et al. Prion. 2013 March 1;7(2):175-184.
2.

Figure. From: Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.

Figure 6. Analysis of Bgl2p which was extracted from Saccharomyces cerevisiae cell wall in 100 mM TRIS solution, pH 9.2. (A) SDS-PAGE,Coomassie staining. (B) Western blot analysis. Bgl2p was detected with antibodies. 1. Protein marker. 2. Bgl2p preparation.

Evgeny E. Bezsonov, et al. Prion. 2013 March 1;7(2):175-184.
3.

Figure. From: Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.

Figure 4. Bgl2p fibril morphology. (A–E) Immunofluorescent microscopy using anti-Bgl2p antibody. Bgl2p was isolated from the CW, which was either not treated (A–C) or treated (D and E) with trypsin before Bgl2p extraction from Saccharomyces cerevisiae cell wall. (F– J) Transmission electron microscopy. Bgl2p was isolated from trypsin-treated Saccharomyces cerevisiae cell wall and then it was incubated in absence (F–H) or in presence (I and J) of laminarin. Arrows indicate the “aggregation centers.”

Evgeny E. Bezsonov, et al. Prion. 2013 March 1;7(2):175-184.
4.

Figure. From: Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.

Figure 5. Bgl2pGM fibril morphology. Immunofluorescent microscopy of Bgl2pGM fibrils with anti-Bgl2p antibody. Ultrafiltered growth medium of Saccharomyces cerevisiae ssu21/mcd4 mutant contains components which pass through the membrane with a cut-off limit of 100 kDa. Images of these components were collected without Congo red (A) and in presence of 8 µM Congo red (B–D). The growth medium containing components which do not pass through the membrane with a cut-off limit of 10 kDa (E).

Evgeny E. Bezsonov, et al. Prion. 2013 March 1;7(2):175-184.
5.

Figure. From: Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.

Figure 3. Fibrillation kinetics of Bgl2p at different pH values measured by thioflavin T fluorescence at 480 nm at pH 5.0 (solid line) and pH 7.6 (dashed line). The fibrillation kinetics was measured at 35°C and using 600 rpm of shaking for 240 sec during each cycle of 400 sec. The excitation wavelength was 450 nm. The plotted data curves are an average of the three individually measured fibrillation kinetics.

Evgeny E. Bezsonov, et al. Prion. 2013 March 1;7(2):175-184.
6.

Figure. From: Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation.

Figure 1. Potential amyloidogenic determinants in Saccharomyces cerevisiae cell wall glucantransferase Bgl2p (UniProtKB/TrEMBL entry number P15703). The amino acids predicted by computational algorithms to be a part of potential amyloidogenic determinants are marked with (*) opposite the name of the corresponding algorithm. The confluences of positive amyloidogenic determinant prediction results are surrounded by frames. Bgl2p N-terminal cell wall transport signal (in gray letters); peptide sequences, which were synthesized and investigated, are saturated gray. Abbreviations: aa, amino acid number; seq, amino acid sequence.

Evgeny E. Bezsonov, et al. Prion. 2013 March 1;7(2):175-184.

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