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首页> 外文期刊>Journal of Molecular Biology >Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction.
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Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction.

机译：通过低角度X射线衍射观察到，α-晶状蛋白和整个晶状体在加热过程中的结构变化。

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摘要

Whole eye lens and alpha-crystallin gels and solutions were investigated using X-ray scattering techniques at temperatures ranging from 20 degrees C to 70 degrees C. In whole lens isolated in phosphate-buffered saline, the spacing of the dominant X-ray reflection seen with low-angle scattering was constant from 20 degrees C to 45 degrees C but increased at 50 degrees C from 15.2 nm to 16.5 nm. At room temperature, the small-angle X-ray diffraction pattern of the intact lens was very similar to the pattern of alpha-crystallin gels at near-physiological concentration (approximately 300 mg/ml), so it is reasonable to assume that the alpha-crystallin pattern dominates the pattern of the intact lens. Our results therefore indicate that in whole lens alpha-crystallin is capable of maintaining its structural properties over a wide range of temperature. This property would be useful in providing protection for other lens proteins super-aggregating. In the alpha-crystallin gels, a moderate increase in both the spacing and intensity of the reflection was observed from 20 degrees C to 45 degrees C, followed by an accelerated increase from 45 degrees C to 70 degrees C. Upon cooling, this effect was found to be irreversible over 11 hours. Qualitatively similar results were observed for alpha-crystallin solutions at a variety of lower concentrations.
机译：使用X射线散射技术在20摄氏度至70摄氏度的温度范围内研究了整个眼镜镜片和α-晶状体蛋白凝胶和溶液。具有低角度散射的α在20℃至45℃是恒定的，但是在50℃从15.2nm至16.5nm增加。在室温下，完整透镜的小角度X射线衍射图谱与接近生理浓度（约300 mg / ml）的α-晶状体蛋白凝胶图谱非常相似，因此可以合理地假设α -晶状体图案主导完整透镜的图案。因此，我们的结果表明，在整个晶状体中，α-晶状体蛋白能够在很宽的温度范围内保持其结构特性。该性质将有助于为其他晶状体蛋白质的超聚集提供保护。在α-晶状体蛋白凝胶中，观察到反射的间隔和强度从20摄氏度到45摄氏度都有适度增加，然后从45摄氏度到70摄氏度加速增加。冷却后，这种效果是发现在11个小时内不可逆转。在各种较低浓度下，α-晶状体蛋白溶液的定性结果相似。

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