Comparison of the chaperone activities of WT and the various αB-crystallin protein constructs used in this study with different client proteins.

Numbers shown are normalised values of protein aggregation as determined by light scattering. Aggregation was calculated as (light scattering in the presence of chaperone)/(light scattering in the absence of chaperone) for the relevant client proteins. Where normalised values became greater than 1.00, this indicates increased protein aggregation. The results summarized here for the various αB-crystallin protein constructs are from previously published work (αAβ3 and CEβ3 see reference [17]; αAβ8 and CEβ8 see reference [16]; Δ155 see reference [14]). Median number of subunits was determined by size exclusion chromatography. Data from far- and near-UVCD spectroscopy were used to analyze secondary and tertiary structure of the αB-crystallin protein constructs. All αB-crystallin proteins consisted of large polydisperse oligomers and had far- and near-UVCD spectra unchanged (UC) from wild type (WT) αB-crystallin at 37°C and 50°C.