Figure 8. Aggregation of β-crystallins during kinetic refolding.

(A) Time-course study of the aggregation of β-crystallins with a final concentration of 0.2 mg/ml. The proteins were denatured by 4 M GdnHCl for 12 h, and refolding is initiated by fast manual dilution (1∶40) of the denatured proteins in buffer A. The dead time of the aggregation experiments was 2 s. (B) Characterization of the morphology of the aggregates formed after 10 min refolding by EM. The bars in the pictures represent 100 nm. The positions of typical aggregates are labeled by open squares.