These changes are related to partial unfolding as the Trp residues became more exposed. Both intensities increased with HMW formation. The initial partial unfolding of proteins is usually followed by aggregation. In this regard, it would be interesting to see what form of a B-crystallin is expressed in other tissues. A decreased Trp emission intensity and a red shift of emission maximum, along with a decreased near-UV CD, indicate that proteins become partially unfolded at elevated temperatures.
Further aggregation enhances ThT fluorescence.
Another unresolved issue is whether the conformationally less stable a B-crystallin is preferentially insolubilized in the lens. A report by Truscott et al. Groenen PJ, Merck KB, de Jong WW, Bloemendal H. Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Horwitz J. Alpha-crystallin can function as a molecular chaperone.