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首页> 外文期刊>Journal of cellular biochemistry. >Application of mass spectrometry to the identification and quantification of histone post-translational modifications.
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Application of mass spectrometry to the identification and quantification of histone post-translational modifications.

机译:质谱在组蛋白翻译后修饰的鉴定和定量中的应用。

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摘要

The core histones are the primary protein component of chromatin, which is responsible for the packaging of eukaryotic DNA. The NH(2)-terminal tail domains of the core histones are the sites of numerous post-translational modifications that have been shown to play an important role in the regulation of chromatin structure. In this study, we discuss the recent application of modern analytical techniques to the study of histone modifications. Through the use of mass spectrometry, a large number of new sites of histone modification have been identified, many of which reside outside of the NH(2)-terminal tail domains. In addition, techniques have been developed that allow mass spectrometry to be effective for the quantitation of histone post-translational modifications. Hence, the use of mass spectrometry promises to dramatically alter our view of histone post-translational modifications.
机译:核心组蛋白是染色质的主要蛋白质成分,它负责真核DNA的包装。核心组蛋白的NH(2)末端尾域是许多翻译后修饰的位点,已被证明在染色质结构的调节中起重要作用。在这项研究中,我们讨论了现代分析技术在组蛋白修饰研究中的最新应用。通过使用质谱,已鉴定出大量新的组蛋白修饰位点,其中许多位于NH(2)-末端尾部结构域之外。另外,已经开发了允许质谱有效地定量组蛋白翻译后修饰的技术。因此,质谱的使用有望大大改变我们对组蛋白翻译后修饰的看法。

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