Insights into hydrophobicity and the chaperone-like function of αA-and αB-crystallins: An isothermal titration calorimetric study
α-Crystallin, composed of two subunits, αA and αB, has been shown to function as a
molecular chaperone that prevents aggregation of other proteins under stress conditions.
The exposed hydrophobic surfaces of α-crystallins have been implicated in this process, but
their exact role has not been elucidated. In this study, we quantify the hydrophobic surfaces
of αA-and αB-crystallins by isothermal titration calorimetry using 8-anilino-1-
napthalenesulfonic acid (ANS) as a hydrophobic probe and analyze its correlation to the …
molecular chaperone that prevents aggregation of other proteins under stress conditions.
The exposed hydrophobic surfaces of α-crystallins have been implicated in this process, but
their exact role has not been elucidated. In this study, we quantify the hydrophobic surfaces
of αA-and αB-crystallins by isothermal titration calorimetry using 8-anilino-1-
napthalenesulfonic acid (ANS) as a hydrophobic probe and analyze its correlation to the …
[引用][C] Insights into hydrophobicity and the chaperone-like function of αA-and αB-crystallins: An isothermal titration calorimetric study
M SATISH KUMAR, M KAPOOR… - The Journal of …, 2005 - American Society for Biochemistry …
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