Abstract
Alpha A and alpha B crystallins are key members of the small heat-shock protein family. In addition to being a major structural protein of the lens, they are constitutively found in many other cells, where their function is not completely understood. Alpha B crystallin is also known to be over-expressed in many neurological diseases. To date, all efforts to crystallize alpha A or alpha B have failed. Thus, high-resolution data on the tertiary and quaternary structures of alpha crystallin is not available. The main reason for this failure seems to be the polydisperse nature of alpha crystallin. This review deals mainly with the polydisperse properties of alpha crystallin and the influence of post-translational modification, chemical modifications, truncations and mutation on its quaternary structure.