Interaction of WT and mutant Hsp17 proteins with monomolecular lipid
layers of total polar lipids (A) and SQDG (B) isolated from
heat-treated cells. A, increasing concentrations of Hsp17
proteins (WT, Q16R, and L9P as circles, triangles, and
diamonds, respectively) were injected underneath lipid layers, and
equilibrium surface pressures were recorded. B, 4.2 μg/ml of each
sHsp (WT, Q16R, and L9P as solid, dashed, and dotted lines,
respectively) was injected into the buffer beneath the lipid layer, and
development of protein-lipid binding was monitored by following the surface
pressure increase.