蛋白质 L 非受力区的突变影响了受力折叠行为

IF 16.4 1区化学 Q1 CHEMISTRY, MULTIDISCIPLINARY

Accounts of Chemical Research Pub Date : 2024-04-12 DOI:10.1088/1674-1056/ad3dcd

Huanjie Jiang, Yanwei Wang, Jiayuan Chen, Dan Hu, Hai Pan, Zilong Guo, Hu Chen

{"title":"蛋白质 L 非受力区的突变影响了受力折叠行为","authors":"Huanjie Jiang, Yanwei Wang, Jiayuan Chen, Dan Hu, Hai Pan, Zilong Guo, Hu Chen","doi":"10.1088/1674-1056/ad3dcd","DOIUrl":null,"url":null,"abstract":"\n Single-molecule magnetic tweezers (MT) have revealed multiple transition barriers along the unfolding pathway of several two-state proteins, such as GB1 and Csp. In this study, we utilized MT to measure the force-dependent folding and unfolding rates of both the Protein L (PLWT) and its Y47W mutant (PLY47W) where the mutation point is not at the force-bearing β-strands. The measurements were conducted within a force range of 3 to 120 pN. Notably, the unfolding rates of both PLWT and PWY47W exhibit distinct force sensitivities below 50 pN and above 60 pN, implying a two-barrier free energy landscape. Both PLWT and PLY47W share the same force-dependent folding rate and the same transition barriers, but the unfolding rate of PLY47W is faster than PLWT. Our finding demonstrates that the residue outside of the force-bearing region will also affect the force-induced unfolding dynamics.","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":"65 2","pages":""},"PeriodicalIF":16.4000,"publicationDate":"2024-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Mutation in a Non-Force-Bearing Region of Protein L Influences Force-Dependent Unfolding Behavior\",\"authors\":\"Huanjie Jiang, Yanwei Wang, Jiayuan Chen, Dan Hu, Hai Pan, Zilong Guo, Hu Chen\",\"doi\":\"10.1088/1674-1056/ad3dcd\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"\\n Single-molecule magnetic tweezers (MT) have revealed multiple transition barriers along the unfolding pathway of several two-state proteins, such as GB1 and Csp. In this study, we utilized MT to measure the force-dependent folding and unfolding rates of both the Protein L (PLWT) and its Y47W mutant (PLY47W) where the mutation point is not at the force-bearing β-strands. The measurements were conducted within a force range of 3 to 120 pN. Notably, the unfolding rates of both PLWT and PWY47W exhibit distinct force sensitivities below 50 pN and above 60 pN, implying a two-barrier free energy landscape. Both PLWT and PLY47W share the same force-dependent folding rate and the same transition barriers, but the unfolding rate of PLY47W is faster than PLWT. Our finding demonstrates that the residue outside of the force-bearing region will also affect the force-induced unfolding dynamics.\",\"PeriodicalId\":1,\"journal\":{\"name\":\"Accounts of Chemical Research\",\"volume\":\"65 2\",\"pages\":\"\"},\"PeriodicalIF\":16.4000,\"publicationDate\":\"2024-04-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Accounts of Chemical Research\",\"FirstCategoryId\":\"101\",\"ListUrlMain\":\"https://doi.org/10.1088/1674-1056/ad3dcd\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"101","ListUrlMain":"https://doi.org/10.1088/1674-1056/ad3dcd","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

摘要

单分子磁镊（MT）揭示了几种双态蛋白质（如 GB1 和 Csp）在展开路径上的多重转换障碍。在这项研究中，我们利用 MT 测定了蛋白质 L（PLWT）及其 Y47W 突变体（PLY47W）随力折叠和展开的速率。测量在 3 至 120 pN 的力范围内进行。值得注意的是，PLWT 和 PWY47W 的展开率在低于 50 pN 和高于 60 pN 时表现出不同的力敏感性，这意味着存在双屏障自由能景观。PLWT 和 PLY47W 都具有相同的随力折叠率和相同的转换壁垒，但 PLY47W 的解折率比 PLWT 快。我们的发现表明，受力区域外的残基也会影响力诱导的解折动力学。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文本刊更多论文

Mutation in a Non-Force-Bearing Region of Protein L Influences Force-Dependent Unfolding Behavior

Single-molecule magnetic tweezers (MT) have revealed multiple transition barriers along the unfolding pathway of several two-state proteins, such as GB1 and Csp. In this study, we utilized MT to measure the force-dependent folding and unfolding rates of both the Protein L (PLWT) and its Y47W mutant (PLY47W) where the mutation point is not at the force-bearing β-strands. The measurements were conducted within a force range of 3 to 120 pN. Notably, the unfolding rates of both PLWT and PWY47W exhibit distinct force sensitivities below 50 pN and above 60 pN, implying a two-barrier free energy landscape. Both PLWT and PLY47W share the same force-dependent folding rate and the same transition barriers, but the unfolding rate of PLY47W is faster than PLWT. Our finding demonstrates that the residue outside of the force-bearing region will also affect the force-induced unfolding dynamics.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Accounts of Chemical Research 化学-化学综合

CiteScore

31.40

自引率

1.10%

发文量

312

审稿时长

2 months

期刊介绍： Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.