ESH copper grids and negative emotion rbt With uranyl acetate 1% w Ssrigen. Atomic force microscopy AFM, 5 aliquots of the sample were on a mica substrate fra JTP-74057 YEARS Riger placed divided. After 60 min incubation, the substrate is rinsed with water to remove salt and loosely bound proteins And blown dry with N2. AFM images were obtained with a microscope equipped with more PicoScan MAC mode, wherein the magnetic coated probe oscillates near its resonant frequency in a magnetic alternating field. Probes with a 2nd 8 Newtons / meter constant force and a resonant frequency of 75 kHz were used MAC mode imaging. The imaging was performed at a scan rate of 1 line / s is carried out with 512 data points per line, in a drive current of 10 4 ?. H eh Between 0 5100 nm were protected gesch analysis.
At least four regions of Glimmeroberfl Surface were examined, in order to verify that Similar WZ4002 structures in the sample are provided. No filter treatment was used to modify images to. SPIP fourth 0 has been used to analyze the distribution in H Height, area and volume of the oligomers synuclein. ATR-FTIR spectroscopy attenuated STATEMENTS total reflectance Fourier transform infrared spectra on a FT-IR spectrometer ThermoNicolet Nexus 670 equipped with an MCT detector were recorded. The samples were as thin films above 37.38 hydrated on the surface Che a compartment inner element germanium outof reflectivity like to purchase trapezoidal Manufactured shaped described methods. 512 interferograms were added together, and 1 cm resolution and high produce of 1 for each spectrum.
The spectra were unfolding on the percentages Tze determine the secondary Ren structure GRAMS32 program. Even Fourier deconvolution and second derivatives are used to deconvolute the spectra. The positions of the peaks identified by the two were used in the curve fitting routine. Were found in the curve fitting anf Nglichen positions of the peaks and the peak width was eliminated allowed vary from 15 to 30 cm -1. Peakh Height, width, and Lorentz percentage could vary until the L Solution converges to a minimum when the Restrict Restriction was applied to the positions of the peaks, and curve fitting from continued until the minimum is reached. Percentage points of the secondary Ren structure tasks were as before 37.38 ffentlicht ver. Small angle R Ntgenstreuung measurement SAXS measurements were performed at beamline 4 2 Stanford Synchrotron Radiation Laboratory.
R Ntgen energy was 8980 eV by a pair of multilayer monochromator crystals Mo/B4C Selected 39 Hlt. Dispersion models were by a Positionsz Sensitive proportional counter linear, which was filled with a mixture of 80% CO2 gas Xe/20% registered. Propagation models. Of the incident R Changes ntgenstrahl Ver, Which were measured with an ionization chamber just before the sample normalized The sample to detector distance was calibrated to 230 cm, using a sample of cholesterol myristate. The measurements were carried out in a 1. 3 mm wide capillary cell. Besch at endings Avoid the reputation of the sample in the SAXS measurements, the protein-L Solution moved by it Next in the capillary cell. Background measurements were taken before and after each measurement performed proteins and then averaged before being used for background subtraction. All measurements were carried out at 37 1 SAXS. The radius of gyration was gem the Guinier N approximation 21, wherein Q is calculated