Phosphorylation Dependence of Hsp27 Multimeric Size and Molecular Chaperone Function.

The article reports on research conducted to determine whether the chaperone Hsp27 or the triple Ser-to-Asp phosphomimic mutant is the more active molecular chaperone in vitro. Researchers correlated chaperone activity with Hsp27 as monitored by analytical ultracentrifugation. They found that the most active chaperone of insulin and α-lactalbumin was the Hsp27 dimer and that the efficient inhibition of insulin aggregation by Hsp27 dimer led to the proposal of two models for chaperone activity.