Das K P, Surewicz W K
Department of Ophtalmology, University of Missouri, Columbia 65212, USA.
FEBS Lett. 1995 Aug 7;369(2-3):321-5. doi: 10.1016/0014-5793(95)00775-5.
alpha-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 alpha-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 50 degrees 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 alpha-crystallin.
α-晶状体蛋白是眼晶状体的主要蛋白质，已知它与小分子热休克蛋白有广泛的相似性，并作为分子伴侣发挥作用。使用疏水探针双-ANS通过荧光光谱法研究了α-晶状体蛋白上疏水表面的暴露情况。加热时，该蛋白质会发生构象转变，这与表面疏水性的显著增加有关。这种转变发生在大约38至50摄氏度之间，且缺乏可逆性。表面疏水性的增加与该蛋白质伴侣活性的增加相关。这些结果表明，疏水相互作用在α-晶状体蛋白的伴侣作用中起主要作用。
