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. 2018 Oct 22;293(51):19511–19521. doi: 10.1074/jbc.RA118.005421

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© 2018 Santhanagopalan et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 3. — Restricting dodecamer dissociation alters sHsp chaperone activity. Light scattering by aggregated MDH mixed with Ta16.9, Ta_CT-ACD, or Ta_dimer under reducing (top left) or oxidizing (bottom left) conditions, and Ps18.1 and Ps_CT-ACD under reducing (top right) or oxidizing (bottom right) conditions. The sHsp monomer: MDH monomer ratio is indicated on the x axis. Scattering values were normalized with respect to that for MDH heated alone, which was assigned a value of 1.0. Means (filled circles) from three replicate experiments (open circles) are plotted with standard deviation. Unheated MDH (4 °C) served as a control for absence of aggregation.