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Force-Profile Analysis of the Cotranslational Folding of HemK and Filamin Domains: Comparison of Biochemical and Biophysical Folding Assays

机译:麻疹和丝瘤域分类折叠的力分析:生物化学和生物物理折叠测定的比较

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摘要

We have characterized the cotranslational folding of two small protein domains of different folds-the alpha-helical N-terminal domain of HemK and the beta-rich FLN5 filamin domain-by measuring the force that the folding protein exerts on the nascent chain when located in different parts of the ribosome exit tunnel (force-profile analysis, or FPA), allowing us to compare FPA to three other techniques currently used to study cotranslational folding: real-time FRET, photo induced electron transfer, and NMR. We find that FPA identifies the same cotranslational folding transitions as do the other methods, and that these techniques therefore reflect the same basic process of cotranslational folding in similar ways. (C) 2019 Elsevier Ltd. All rights reserved.
机译:我们已经表征了两个不同折叠的两种小蛋白质结构域的分致折叠 - α-螺旋N-末端结构域的α-致脂肪的FLN5菲素域 - 通过测量折叠蛋白在位于新生链上施加的力 核糖体出口隧道的不同部分(力型分析或FPA),允许我们将FPA比较目前用于研究分氯化物折叠的其他技术:实时褶皱,照片诱导电子转移和NMR。 我们发现FPA识别与其他方法相同的配体折叠转换,因此这些技术以类似的方式反映了与双转抗性折叠的相同基本过程。 (c)2019 Elsevier Ltd.保留所有权利。

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