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Results: 8

1.
Figure 4

Figure 4. Ellipticity at 222 nm ([θ]222 nm) as a function of SDS concentration (mM) deduced from the spectra reported in Fig. S3.. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

NN, CC, NC and DC are represented respectively by black triangle up, black triangle down, empty square, empty circle, respectively. SDS dependence curve of aS is also reported (black circle).

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
2.
Figure 1

Figure 1. Far UV CD of aS dimers.. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

The spectra were recorded in PBS buffer pH 7.4 at a protein concentration of 5 µM, using a quartz cuvette with 1 mm of pathlength. NN, CC, NC and DC are represented respectively by a long, medium, short dash and dotted line. Inset: Far UV CD of aS (continuous line).

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
3.
Figure 2

Figure 2. FT-IR spectra of aS dimers at pH* 7.2.. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

Curve fitting was performed with Gaussian and Lorentzian lineshapes and with bandwidths varying between 15 and 20 cm−1. The peak position of the amide band components was deduced from the second derivative spectra (Fig. S2). The sum of the fitted curves is shown as a broken line, closely overlapping the experimental trace, shown as a continuous line.

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
4.
Figure 7

Figure 7. Representative TEM and AFM images of fibrils formed by the NN, CC, NC and DC dimers (rows 1–4) and aS (fifth row) (left and central columns).. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

Right column: distributions of the apparent diameters of the fibrillar aggregates, as measured from AFM images via an automated procedure (see main text). Gaussian fits are shown (solid black lines) where applicable.

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
5.
Figure 8

Figure 8. Scheme of proteolytic sites of aS dimer fibrils by using proteinase K (PK) and trypsin (T).. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

Sequences cleaved off are represented in white, protected regions are indicated in black. The numbers refer to N-terminal of each peptide. As DC is constituted by the sequence 1–104 linked to 29–140 of aS, the sequence notation of its proteolytic fragments refers to the aS sequence numbering. In the case of fragments encompassing the two sequences, these were indicated with numbering of the segments deriving from both sequences separated by a slash.

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
6.
Figure 3

Figure 3. HSQC spectra of NN, CC, NC and DC dimers.. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

aS HSQS spectrum is reported with resonance assignments, where space permits. In red are indicated new peaks of dimers spectra that are not present in aS spectrum. For CC dimer, experiments were performed in the absence and in the presence of 10 mM DTT and the difference maps (CC-dm) was calculated by subtracting the data matrix obtained after 2 hours of incubation in the presence of DTT from the reference.

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
7.
Figure 6

Figure 6. FT-IR spectra of aS dimer fibrils.. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

Protein fibrils obtained after one month of incubation were dissolved in 20 mM Tris·DCl, 150 mM NaCl pH* 7.2. The peak position of the amide band components was deduced from the second derivative spectra (Fig. S4). Curve fitting was performed with Gaussian and Lorentzian lineshapes. The sum of the fitted curves is shown as a thin dashed line, closely overlapping the experimental trace, shown as a continuous bold line.

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.
8.
Figure 5

Figure 5. Time-course analysis of the aggregation process of aS dimers, followed by ThT fluorescence assay (A) and fluorescence polarization (B).. From: Covalent ?-Synuclein Dimers: Chemico-Physical and Aggregation Properties.

The aggregation processes were conducted at a protein concentration of 1 mg/ml. Fluorescence intensity of ThT is reported as percentage of the plateau of emission intensity corresponding to each curve. NN, CC, NC and DC are represented respectively by black triangle up, black triangle down, empty square, empty circle, respectively. aS aggregation curve is indicated by black circles. Error bars were calculated from three independent aggregation experiments. For FP, lag-phase, (white bars) and curve slope at t50 (black bars) for NN, CC and aS were reported. The values of lag phase and slope were deduced from four independent aggregation experiments.

Micaela Pivato, et al. PLoS One. 2012;7(12):e50027.

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