27kDa荧光蛋白mCherry的骨架1H、15N和13C共振定位

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2023-09-09 DOI:10.1007/s12104-023-10149-z

Marco Sette, Laura Anne Johnson, Ralph Jimenez, Frans A.A. Mulder

{"title":"27kDa荧光蛋白mCherry的骨架1H、15N和13C共振定位","authors":"Marco Sette, Laura Anne Johnson, Ralph Jimenez, Frans A.A. Mulder","doi":"10.1007/s12104-023-10149-z","DOIUrl":null,"url":null,"abstract":"<div><p>mCherry is one of the most successfully applied monomeric red fluorescent proteins (RFPs) for in vivo and in vitro imaging. However, questions pertaining to the photostability of the RFPs remain and rational further engineering of their photostability requires information about the fluorescence quenching mechanism in solution. To this end, NMR spectroscopic investigations might be helpful, and we present the near-complete backbone NMR chemical shift assignment to aid in this pursuit.</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"243 - 247"},"PeriodicalIF":0.8000,"publicationDate":"2023-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry\",\"authors\":\"Marco Sette, Laura Anne Johnson, Ralph Jimenez, Frans A.A. Mulder\",\"doi\":\"10.1007/s12104-023-10149-z\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>mCherry is one of the most successfully applied monomeric red fluorescent proteins (RFPs) for in vivo and in vitro imaging. However, questions pertaining to the photostability of the RFPs remain and rational further engineering of their photostability requires information about the fluorescence quenching mechanism in solution. To this end, NMR spectroscopic investigations might be helpful, and we present the near-complete backbone NMR chemical shift assignment to aid in this pursuit.</p></div>\",\"PeriodicalId\":492,\"journal\":{\"name\":\"Biomolecular NMR Assignments\",\"volume\":\"17 2\",\"pages\":\"243 - 247\"},\"PeriodicalIF\":0.8000,\"publicationDate\":\"2023-09-09\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomolecular NMR Assignments\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s12104-023-10149-z\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomolecular NMR Assignments","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s12104-023-10149-z","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}

引用次数: 0

摘要

mCherry是应用最成功的单体红色荧光蛋白（RFPs），用于体内和体外成像。然而，与RFP的光稳定性有关的问题仍然存在，对其光稳定性进行合理的进一步工程需要有关溶液中荧光猝灭机制的信息。为此，核磁共振波谱研究可能会有所帮助，我们提出了近乎完全的骨架核磁共振化学位移分配来帮助这一研究。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry

查看原文本刊更多论文

Backbone 1H, 15N and 13C resonance assignments of the 27kDa fluorescent protein mCherry

mCherry is one of the most successfully applied monomeric red fluorescent proteins (RFPs) for in vivo and in vitro imaging. However, questions pertaining to the photostability of the RFPs remain and rational further engineering of their photostability requires information about the fluorescence quenching mechanism in solution. To this end, NMR spectroscopic investigations might be helpful, and we present the near-complete backbone NMR chemical shift assignment to aid in this pursuit.

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

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.