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. 2010 Jan 19;107(5):2007–2012. doi: 10.1073/pnas.0910126107

Fig. 2.

Fig. 2.

Time-course of the formation of complexes between HSP18.1 and unfolding Luc. A Incubation with HSP18.1 (≈6,350 m/z) at 42 °C results in a decrease in the abundance of Luc (≈4,100 m/z), and the concomitant appearance of signal at high m/z (> 8,000 m/z) corresponding to sHSP:client complexes. Data are normalised such that the HSP18.1 is displayed at an intensity of 100%. Coloured boxes refer to isolations for tandem-MS experiments in Figure 4. B Quantifying the relative abundances of the different species shows the initial rapid binding of Luc by HSP18.1, followed by further incorporation of HSP18.1 into the resultant complexes. The average mass of these complexes (Red, right-hand y-axis) mirrors this behavior, revealing the presence of distinct “binding” and “augmentation” steps in the chaperone action of HSP18.1.