Hydrophobicity and flexibility of alpha A- and alpha B-crystallin are different

Since the discovery that the lens protein alpha-crystallin is also found in non-lenticular tissues and can function as a chaperone, relatively little attention has been paid to differences in properties between alpha A- and alpha B-crystallin, which form mixed aggregates in the lens but have so far never been found together in other tissues. In this study hydrophobicity and flexibility, properties that are thought to be relevant for chaperone function, are compared for alpha A- and alpha B-crystallin. Hydrophobicity was monitored from sodium dodecylsulphate polyacrylamide gel electrophoresis in the absence and presence of (methyl-substituted) ureas. Flexibilities were calculated from primary structures. Based on literature data also some other properties are compared. The results indicate significant difference in hydrophobicity profile, flexibility of the terminal parts and stability of alpha A- and alpha B-crystallin.