Ancestral ribonucleases back in motion for evolutionary-dynamics guided protein design

IF 11.6 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Trends in Biochemical Sciences Pub Date : 2024-08-01 DOI:10.1016/j.tibs.2024.06.005

引用次数: 0

Abstract

The dynamics behavior of a protein is essential for its functionality. Here, Doucet et al. demonstrate how the evolutionary analysis of conformational pathways within a protein family serves to identify common core scaffolds that accommodate branch-specific functional regions controlled by flexibility switches, offering a model for evolutionary-dynamics based protein design.

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祖先核糖核酸酶重新启动，以进化动力学为指导设计蛋白质。

蛋白质的动力学行为对其功能至关重要。在本文中，Doucet 等人展示了如何通过对蛋白质家族内构象途径的进化分析来确定共同的核心支架，从而容纳由灵活性开关控制的特定分支功能区，为基于进化动力学的蛋白质设计提供了一个模型。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Trends in Biochemical Sciences 生物-生化与分子生物学

CiteScore

22.90

自引率

0.70%

发文量

148

审稿时长

6-12 weeks

期刊介绍： For over 40 years, Trends in Biochemical Sciences (TIBS) has been a leading publication keeping readers informed about recent advances in all areas of biochemistry and molecular biology. Through monthly, peer-reviewed issues, TIBS covers a wide range of topics, from traditional subjects like protein structure and function to emerging areas in signaling and metabolism. Articles are curated by the Editor and authored by top researchers in their fields, with a focus on moving beyond simple literature summaries to providing novel insights and perspectives. Each issue primarily features concise and timely Reviews and Opinions, supplemented by shorter articles including Spotlights, Forums, and Technology of the Month, as well as impactful pieces like Science & Society and Scientific Life articles.