Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy.
Susceptibility of different proteins to flow-induced conformational changes monitored with Raman spectroscopy.
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DOI：
10.1016/j.bpj.2009.10.010
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发表时间：
2010-02
影响因子：
3.4
通讯作者：
L. Ashton;J. Dusting;Eboshogwe Imomoh;S. Balabani;E. Blanch
中科院分区：
文献类型：
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作者：
L. Ashton;J. Dusting;Eboshogwe Imomoh;S. Balabani;E. Blanch
通过拉曼光谱直接监测搅拌后的蛋白质溶液，研究了几种不同结构性质和相对分子质量的天然蛋白质在流体剪切作用下的可逆展开过程。虽然没有观察到完全变性，但不同蛋白质发生了广泛的光谱差异，表明微妙的构象变化似乎是蛋白质特有的。从这项研究中可以明显看出许多重大的总体趋势。对于球状蛋白质，光谱变化的总体程度随着蛋白质大小和β结构比例的增加而增加。对于两种结构较差的蛋白质，胎球蛋白和α-酪蛋白，观察到的变化幅度相对较小，尽管这些蛋白质的分子结构流动性较大。这意味着其他蛋白质特有的因素，如翻译后修饰，也可能是重要的。还详细讨论了在每个单独蛋白质的光谱轮廓中发生的单独条带的变化。
By directly monitoring stirred protein solutions with Raman spectroscopy, the reversible unfolding of proteins caused by fluid shear is examined for several natural proteins with varying structural properties and molecular weight. While complete denaturation is not observed, a wide range of spectral variances occur for the different proteins, indicating subtle conformational changes that appear to be protein-specific. A number of significant overall trends are apparent from the study. For globular proteins, the overall extent of spectral variance increases with protein size and the proportion ofβ-structure. For two less structured proteins, fetuin andα-casein, the observed changes are of relatively low magnitude, despite the greater molecular structural mobility of these proteins. This implies that other protein-specific factors, such as posttranslational modifications, may also be significant. Individual band changes occurring in the spectral profiles of each individual protein are also discussed in detail.