Kudryashova Elena V, Meinders Marcel B J, Visser Antonie J W G, van Hoek Arie, de Jongh Harmen H J
Division of Chemical Enzymology, Chemistry Department, Moscow State University, 119899 Moscow, Russia.
Eur Biophys J. 2003 Sep;32(6):553-62. doi: 10.1007/s00249-003-0301-3. Epub 2003 Apr 23.
The molecular properties of egg white ovalbumin adsorbed at the air/water interface were studied using infrared reflection absorption spectroscopy (IRRAS) and time-resolved fluorescence anisotropy (TRFA) techniques. Ovalbumin adsorbed at the air/water interface adopts a characteristic partially unfolded conformation in which the content of the beta-sheet is 10% lower compared to that of the protein in bulk solution. Adsorption to the interface leads to considerable changes in the rotational dynamics of ovalbumin. The results indicate that the end-over-end mobility of the ellipsoidal protein becomes substantially restricted. This is likely to reflect a preferential orientation of the protein at the interface. Continuous compression of surface layers of ovalbumin causes local aggregation of the protein, resulting in protein-network formation at the interface. The altered protein-protein interactions contribute to the strong increase in surface pressure observed.
利用红外反射吸收光谱（IRRAS）和时间分辨荧光 anisotropy（TRFA）技术研究了吸附在空气/水界面的蛋清卵清蛋白的分子特性。吸附在空气/水界面的卵清蛋白呈现出一种特征性的部分展开构象，其中β-折叠的含量比本体溶液中的蛋白质低10%。吸附到界面会导致卵清蛋白的旋转动力学发生显著变化。结果表明，椭圆形蛋白质的端对端移动性受到了极大限制。这可能反映了蛋白质在界面处的优先取向。卵清蛋白表面层的持续压缩会导致蛋白质局部聚集，从而在界面处形成蛋白质网络。蛋白质-蛋白质相互作用的改变导致了所观察到的表面压力的强烈增加。
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