Figure 5 | Scientific Reports

Figure 5

From: Significant influence of four highly conserved amino-acids in lipochaperon-active sHsps on the structure and functions of the Lo18 protein

Figure 5

Impact of Lo18/liposomes interaction on protein secondary structure. (A) Structure modification of Lo18 WT induce by thermal slope (20 °C to 60 °C) on the four main secondary structures α-helix, β-sheet, turns and other secondary structure in presence (black square) or absence (grey dot) of liposomes. The data represent the means and SE of three independent experiments. (B) SRCD spectra on 190–210 nm wavelenght for Lo18 WT (black), E60K (red), T79V (yellow), G82V (green) and R99D (blue) in presence (dark square) or absence (light dot) of liposomes at 25 °C.

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