Figure 1 of Vendra, Mol Vis 2024; 30:37-48.


Figure 1. Structural properties of wild-type (black squares) and Y134X mutant human γD- crystallin (brown circles). A: Far-ultraviolet circular dichroism spectra. Protein concentration: 0.1 mg/ml; cell path length: 2 mm; scanning speed: 100 nm/min. Vertical lines at 218, and 206 nm represent β-sheet and α-helix conformations respectively. Each spectrum is an average of three independent scans of three separate samples. B: Intrinsic fluorescence spectra. Protein concentration: 6 μM; λex: 295 nm; excitation emission slits: 5 nm. Vertical lines represent the emission maxima of the proteins. Each spectrum is an average of three independent scans of three separate samples. C: Stern–Volmer plots. Protein concentration: 15 μM; λex: 295 nm; excitation emission slits: 10 nm. The line indicates the fitted data, and the blocks stand for raw data. F0: fluorescence intensity of the protein; F: fluorescence intensity of the protein in the presence of a quencher. The data were acquired from three independent runs of three separate samples.