Article ID Journal Published Year Pages File Type
1987180 International Journal of Biological Macromolecules 2012 4 Pages PDF
Abstract

ATP was previously reported to bind to the chaperone α-crystallin resulting in a significant effect on the protein's ability to suppress the aggregation of a thermally denatured protein. Here, we have investigated the binding of GTP to α-crystallin. Unlike ATP, binding of GTP to α-crystallin did not affect its ability to suppress the aggregation of thermally denatured rhodanese. GTP binding induced a conformational change on α-crystallin, however the degree of exposed hydrophobic surfaces, which are believed to be involved in the binding of the chaperone to denaturing proteins did not change. Here, we report that GTP binds to α-crystallin and this results in a decreased stability of the chaperone as indicated by urea denaturation.

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