Conformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive gene
Fig 1
ASR1 secondary structure in different environments.
CD spectra of ASR1 (10 μM). A) At different TFE concentrations from 0 (thick line) to 50%, inset: Mean Residual Molar Ellipticity at 222 and % of calculated α-helix as a function of TFE concentration. The solid line corresponds to the fit of 1:1 binding model (Eq 4) B) At different GdnCl concentrations (0 M in thick line); inset, differential spectrum between 6 M and 0 M. C) At increasing temperatures (from 5 to 90°C); inset, differential spectrum between 5°C and 90°C. D) At pH 2, 3, 4, 5, 6, 7 and 8; inset, differential spectrum between pH 5 and pH 8. E) At increasing amounts of NaCl; inset, difference spectrum between 1 M and 0 M. F) Without any stabilizing or denaturant agents (full line) in the presence of crowding agents: 40% of PEG 4000 (dash line) or 50% glycerol (dotted line). More noticeable spectral changes are shown in arrowheads in the inset figures.