期刊
METHODS
卷 137, 期 -, 页码 71-81出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2017.11.007
关键词
Co-translational protein folding; Ribosome-bound nascent chain complexes (RNCs); Protein folding pathway; Reconstituted cell-free translation systems; Real-time measurements
资金
- International Human Frontier Science Program Organization [RGP0024/2010]
- National Institutes of Health [HL121779-01A1]
- Center for Gene Regulation in Health and Disease (GRHD) at CSU
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R15HL121779] Funding Source: NIH RePORTER
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. (C) 2017 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据