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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Differential stability of E. coli ribosomal particles and free RNA towards thermal degradation studied by microcalorimetry.
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Differential stability of E. coli ribosomal particles and free RNA towards thermal degradation studied by microcalorimetry.

机译：通过微量量热法研究了大肠杆菌核糖体颗粒和游离RNA对热降解的差异稳定性。

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摘要

We investigated the thermal degradation of E. coli ribosomes by differential scanning microcalorimetry. The 70S particles show two distinctive and irreversible peaks upon thermal degradation. Free rRNA in solution produces, on the contrary, an unstructured denaturation profile. The thermal analysis of 50S particles shows a profile substantially identical to that observed in 70S, while 30S particles produce an unstructured denaturation pattern. Therefore the thermal behavior of the 70S particle is essentially attributable to the denaturation of the 50S subunit. Our data validate previous observations that the 50S has a more rigid structure as compared to 30S, which behaves as a 'floppy' particle. In addition our data suggest that protein/RNA interactions play a significant role to stabilize three-dimensional structures of the ribosome.
机译：我们通过差示扫描量热法研究了大肠杆菌核糖体的热降解。 70S颗粒在热降解时显示出两个独特且不可逆的峰。相反，溶液中的游离rRNA会产生非结构化的变性曲线。 50S颗粒的热分析显示出与70S中观察到的基本相同的轮廓，而30S颗粒则产生了非结构化的变性模式。因此，70S颗粒的热行为基本上可归因于50S亚基的变性。我们的数据验证了先前的观察结果，即50S的行为比30S的行为更为坚硬，后者表现为“松散的”颗粒。另外，我们的数据表明蛋白质/ RNA相互作用在稳定核糖体的三维结构中起着重要作用。

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