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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >High pressure induces the formation of aggregation-prone states of proteins under reducing conditions.
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High pressure induces the formation of aggregation-prone states of proteins under reducing conditions.

机译:高压诱导在还原条件下蛋白质易于聚集的状态的形成。

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摘要

The pressure stability of ribonuclease A and bovine pancreatic trypsin inhibitor has been investigated with Fourier transform infrared spectroscopy in the presence of the disulfide bond reducing agent 2-mercaptoethanol. The secondary structure of the reduced proteins at high pressure (1 GPa) is not significantly different from the pressure-induced conformation of the native form. Upon decompression under reducing conditions, amorphous aggregates are formed. Such aggregates are not formed upon decompression of the native proteins. Our data demonstrate that high pressure populates, and thus allows the potential characterization of highly aggregation-prone conformations. The relevance of these findings with regard to fibril formation is discussed and the possible role of conformational fluctuations of intermediates on the aggregation pathway is emphasized.
机译:在存在二硫键还原剂2-巯基乙醇的情况下,通过傅立叶变换红外光谱法研究了核糖核酸酶A和牛胰胰蛋白酶抑制剂的压力稳定性。在高压(1 GPa)下还原的蛋白质的二级结构与天然形式的压力诱导构象没有显着差异。在还原条件下减压后,形成无定形聚集体。天然蛋白质解压缩时不会形成此类聚集体。我们的数据表明,存在高压,因此潜在地表征了易于聚集的构象。讨论了这些发现与原纤维形成的相关性,并强调了中间体构象波动对聚集途径的可能作用。

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