Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallin

FEBS Letters

Surewicz, Witold K.¹  Das, Kali P.¹ 

[1] Departments of Opthalmology and Biochemistry, University of Missouri, Columbia, MO 65212, USA

关键词: α-Crystallin;    Surface hydrophobicity;    Molecular chaperone;    Thermal transition;   

DOI  :  10.1016/0014-5793(95)00775-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Crystallin, the major protein of the ocular lens, is known to have extensive similarities to small heat shock proteins and to act as a molecular chaperone. The exposure of hydrophobic surfaces on α-crystallin was studied by fluorescence spectroscopy using the hydrophobic probe bis-ANS. Upon heating the protein undergoes a conformational transition which is associated with a marked increase in surface hydrophobicity. This transition, which occurs between approximately 38 and 5-°C, lacks reversibility. The increase in surface hydrophobicity correlates with the increased chaperone activity of the protein. These results indicate that hydrophobic interactions play a major role in the chaperone action of α-crystallin.

【 授权许可】

Unknown