Co-Translational Folding Of Nascent Polypeptides: Multi-Layered Mechanisms For The Efficient Biogenesis Of Functional Proteins

BIOESSAYS(2021)

引用 4|浏览3
暂无评分
摘要
The coupling of protein synthesis and folding is a crucial yet poorly understood aspect of cellular protein folding. Over the past few years, it has become possible to experimentally follow and define protein folding on the ribosome, revealing principles that shape co-translational folding and distinguish it from refolding in solution. Here, we highlight some of these recent findings from biochemical and biophysical studies and their potential significance for cellular protein biogenesis. In particular, we focus on nascent chain interactions with the ribosome, interactions within the nascent protein, modulation of translation elongation rates, and the role of mechanical force that accompanies nascent protein folding. The ability to obtain mechanistic insight in molecular detail has set the stage for exploring the intricate process of nascent protein folding. We believe that the aspects discussed here will be generally important for understanding how protein synthesis and folding are coupled and regulated.
更多
查看译文
关键词
co&#8208, translational protein folding, folding pathways, mechanical force, misfolding, molecular chaperones, nascent protein, ribosome
AI 理解论文
溯源树
样例
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要