Figure 5 | Scientific Reports

Figure 5

From: Importance of the C-terminal histidine residues of Helicobacter pylori GroES for Toll-like receptor 4 binding and interleukin-8 cytokine production

Figure 5

Far-ultra violet (UV) circular dichroism (CD) analysis of the differences between histidine mutant and WT proteins.

Far-UV CD spectra (190–260 nm) of H100A, H102A, H108A, H113A, H118A and WT proteins were obtained in 25 mM sodium phosphate buffer, pH 7.4, with 1 mm path length of the quartz cuvette at 4 °C. The data collection bandwidth was set to 1 nm. The changes in ellipticity values at 200–210 nm and 220–225 nm range were monitored indicated different secondary structures of histidine mutants and WT in solution. Further secondary structure variations in percentages for each histidine mutant and WT determined using the CDSSTR program are presented in Supplementary Table SII. Data are representative of three independent experiments were subjected to smoothing.

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