20 research outputs found
Porcelli et al 2016 JEB dryad
Data files used for data analysis presented in Porcelli et al JEB Local adaptation of reproductive performance during thermal stres
Changes in PRH structure at high temperature.
<p>(A) PRH was incubated with ANS before emission fluorescence spectra were collected between 20°C and 75°C. (B) PRH was incubated with ANS and emission fluorescence spectra were collected between 400 nm and 600 nm at 20°C and 75°C and after heating to 75°C and then cooling to 20°C (HC). (C) Fluorescence emission spectroscopy was performed to monitor intrinsic tryptophan fluorescence between 20°C and 75°C.</p
Changes in PRH structure in the presence of chemical denaturant.
<p>(A) Fluorescence emission spectroscopy was performed in the presence of increasing concentrations of GITC. (B) The intensity size distribution of PRH particles in the presence of 4 M GITC determined using DLS. (C) The ratio of the maximum intensities of the major PRH peaks obtained using DLS in the presence of increasing concentrations of GITC.</p
PRH oligomers are thermostable.
<p>(A) Circular dichroism was used to examine the secondary structure of the full length PRH protein at the temperatures shown. The insert shows the near-UV circular dichroism spectra at the temperatures shown. (B) The far-UV circular dichroism signal at 200 nm measured while increasing (black line) and then decreasing (grey line) the temperature. (C) The mean diameter of PRH particles at increasing temperature determined using DLS.</p
PRH oligomers predominate in solution.
<p>(A) A schematic representation of the PRH protein and its functional domains. Proline Rich indicates the transcriptional repression domain, HD indicates the homeodomain and C indicates the C-terminal domain. The PRH HDC protein lacks the N-terminal domain. The intensity size distribution of PRH particles (B) and PRH HDC particles (C) in solution determined using DLS.</p
