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首页> 外文期刊>Annals of the American Thoracic Society >The Recent Progresses in Chemical Synthesis of Proteins with Site-specific Lysine Post-translational Modifications
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The Recent Progresses in Chemical Synthesis of Proteins with Site-specific Lysine Post-translational Modifications

机译:近期蛋白质化学合成的进展,具有特异性特异性赖氨酸的翻译后修饰

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摘要

In the past two decades, a plethora of lysine (Lys) posttranslational modifications (PTMs) has been discovered on proteins, major groups are acylation, alkylation, and ubiquitination. Although considered biologically important, functional annotation of proteins with Lys PTMs has largely fallen behind the discovery. One grand challenge of characterizing proteins with PTMs is the procurement of homogenously modified proteins. To resolve this obstacle, sophisticated methods have been developed. These include total synthesis, semisynthesis that is based on native chemical ligation, expressed protein ligation, and enzyme-catalyzed peptide ligation, and the amber-suppression based noncanonical amino acid mutagenesis technique that may need to couple with follow-up bioorthogonal chemistry. This review summarizes currently identified significant PTMs and chemical biology methods for their installation in proteins. We hope that the current review will provide helpful insights and critical perspectives to this important research frontier.
机译:在过去的二十年中,已经在蛋白质上发现了一种赖氨酸(Lys)后翻译(PTMS),主要基团是酰化,烷基化和泛素。虽然被认为是生物学上重要的,用Lys PTMS的蛋白质功能注释在很大程度上落后于发现。用PTMS表征蛋白质的一个大挑战是均质改性蛋白质的采购。解决这种障碍,已经开发了复杂的方法。这些包括总合成,基于本机化学结扎,表达蛋白质连接和酶催化的肽连接的半合成,以及基于琥珀抑制的非甘露酸氨基酸诱变技术,其可能需要与后续生物正交化学加耦合。本综述总结了目前确定了在蛋白质中安装的重要的PTM和化学生物学方法。我们希望目前的审查将为这一重要的研究前沿提供有用的见解和批判性观点。

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