通过扩展遗传密码扭转赖氨酸的电荷

IF 19.2 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY Nature chemistry Pub Date : 2024-06-03 DOI:10.1038/s41557-024-01536-7
Daniela Danková, Christian A. Olsen
{"title":"通过扩展遗传密码扭转赖氨酸的电荷","authors":"Daniela Danková, Christian A. Olsen","doi":"10.1038/s41557-024-01536-7","DOIUrl":null,"url":null,"abstract":"Posttranslational modifications alter the structure and function of proteins. Now, genetic code expansion enables encoding of ε-N-succinyllysine and ε-N-glutaryllysine residues to decipher the effects of these modifications on enzymatic activity, protein–protein interactions and protein–DNA interactions.","PeriodicalId":18909,"journal":{"name":"Nature chemistry","volume":null,"pages":null},"PeriodicalIF":19.2000,"publicationDate":"2024-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Reversing the charge of lysine by genetic code expansion\",\"authors\":\"Daniela Danková, Christian A. Olsen\",\"doi\":\"10.1038/s41557-024-01536-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Posttranslational modifications alter the structure and function of proteins. Now, genetic code expansion enables encoding of ε-N-succinyllysine and ε-N-glutaryllysine residues to decipher the effects of these modifications on enzymatic activity, protein–protein interactions and protein–DNA interactions.\",\"PeriodicalId\":18909,\"journal\":{\"name\":\"Nature chemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":19.2000,\"publicationDate\":\"2024-06-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature chemistry\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.nature.com/articles/s41557-024-01536-7\",\"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":"Nature chemistry","FirstCategoryId":"92","ListUrlMain":"https://www.nature.com/articles/s41557-024-01536-7","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

翻译后修饰会改变蛋白质的结构和功能。现在,通过扩展遗传密码,可以对ε-N-琥珀酰赖氨酸和ε-N-谷氨酰赖氨酸残基进行编码,从而破译这些修饰对酶活性、蛋白质-蛋白质相互作用以及蛋白质-DNA相互作用的影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

摘要图片

摘要图片

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Reversing the charge of lysine by genetic code expansion
Posttranslational modifications alter the structure and function of proteins. Now, genetic code expansion enables encoding of ε-N-succinyllysine and ε-N-glutaryllysine residues to decipher the effects of these modifications on enzymatic activity, protein–protein interactions and protein–DNA interactions.
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
Nature chemistry
Nature chemistry 化学-化学综合
CiteScore
29.60
自引率
1.40%
发文量
226
审稿时长
1.7 months
期刊介绍: Nature Chemistry is a monthly journal that publishes groundbreaking and significant research in all areas of chemistry. It covers traditional subjects such as analytical, inorganic, organic, and physical chemistry, as well as a wide range of other topics including catalysis, computational and theoretical chemistry, and environmental chemistry. The journal also features interdisciplinary research at the interface of chemistry with biology, materials science, nanotechnology, and physics. Manuscripts detailing such multidisciplinary work are encouraged, as long as the central theme pertains to chemistry. Aside from primary research, Nature Chemistry publishes review articles, news and views, research highlights from other journals, commentaries, book reviews, correspondence, and analysis of the broader chemical landscape. It also addresses crucial issues related to education, funding, policy, intellectual property, and the societal impact of chemistry. Nature Chemistry is dedicated to ensuring the highest standards of original research through a fair and rigorous review process. It offers authors maximum visibility for their papers, access to a broad readership, exceptional copy editing and production standards, rapid publication, and independence from academic societies and other vested interests. Overall, Nature Chemistry aims to be the authoritative voice of the global chemical community.
期刊最新文献
Fused radical SAM and αKG-HExxH domain proteins contain a distinct structural fold and catalyse cyclophane formation and β-hydroxylation A single diiron enzyme catalyses the oxidative rearrangement of tryptophan to indole nitrile Small-molecule properties define partitioning into biomolecular condensates Stereoselective and site-divergent synthesis of C-glycosides Isolation of a NHC-stabilized heavier nitrile and its conversion into an isonitrile analogue
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1