Advances in techniques such as nuclear magnetic resonance spectroscopy, cryo-electron microscopy, and single-molecule and time-resolved fluorescent approaches are transforming our ability to study co-translational protein folding both in vivo in living cells and in vitro in reconstituted cell-free translation systems. These approaches provide comprehensive information on the spatial organization and dynamics of nascent polypeptide chains and the kinetics of co-translational protein folding. This information has led to an improved understanding of the process of protein folding in living cells and should allow remaining key questions in the field, such as what structures are formed within nascent chains during protein synthesis and when, to be answered. Ultimately, studies using these techniques will facilitate development of a unified concept of protein folding, a process that is essential for proper cell function and organism viability. This review describes current methods for analysis of co-translational protein folding with an emphasis on some of the recently developed techniques that allow monitoring of co-translational protein folding in real-time.

中文翻译：

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解开共翻译蛋白质折叠：概念和方法

核磁共振波谱、冷冻电子显微镜以及单分子和时间分辨荧光方法等技术的进步正在改变我们在活细胞体内和体外重组无细胞中研究共翻译蛋白折叠的能力翻译系统。这些方法提供了关于新生多肽链的空间组织和动力学以及共翻译蛋白质折叠动力学的综合信息。这些信息提高了对活细胞中蛋白质折叠过程的理解，并且应该可以回答该领域中剩余的关键问题，例如蛋白质合成过程中新生链内形成的结构以及何时形成。最终，使用这些技术的研究将促进蛋白质折叠的统一概念的发展，这一过程对于适当的细胞功能和生物体活力至关重要。这篇综述描述了目前用于分析共翻译蛋白折叠的方法，重点介绍了一些最近开发的技术，这些技术允许实时监测共翻译蛋白折叠。