Fig. 3: Application of the frame-selection methodology to the high-LPR (A–C) and low-LPR (D–F) datasets.
From: Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces
A, D Histograms of the RSS values of all the MD-frames up to RSS = 50 (left), with a zoom-in on the best-matching ensemble (right; in dark-blue/dark-red) for which the calculated standard deviation is equal to the experimental standard deviations of the datasets composed from taking the averages of 10–50 spectra recorded with 5-min acquisition times each. This leads to RSS thresholds of 2.045 for the high-LPR experiment and 1.559 for the low-LPR experiment. B, E Experimental (rugged, thin lines) and calculated spectra for the best-matching frame (filled areas indicate the intensity range of all spectra within the best-matching ensemble, and the smooth, thick lines indicate the average spectrum of the best-matching ensemble). C, F Selections of typical structures found in the best-matching ensembles of the high- and low-LPR experiments, again with the N-terminal region (residues 1–60) in blue, the NAC region (61–95) in yellow, and the C-terminal region (96–140) in red. Structural inspection of the ensembles derived from this approach reveals a transition from flat-lying αS at low αS concentrations to an upright orientation at high-αS concentrations. Source data are provided in the Source Data file.
