同核超分辨率核磁共振波谱学

IF 16.1 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Olivia Gampp, Luca Wenchel, Prof. Peter Güntert, Prof. Roland Riek
{"title":"同核超分辨率核磁共振波谱学","authors":"Olivia Gampp,&nbsp;Luca Wenchel,&nbsp;Prof. Peter Güntert,&nbsp;Prof. Roland Riek","doi":"10.1002/anie.202414324","DOIUrl":null,"url":null,"abstract":"<p>In homonuclear <sup>1</sup>H NMR (nuclear magnetic resonance) spectra such as [<sup>1</sup>H,<sup>1</sup>H]-NOESY (Nuclear Overhauser Enhancement spectroscopy), which is a historic cornerstone spectrum for biomolecular NMR structural biology, hundreds to thousands of cross peaks are present within a square of approximately 100 ppm<sup>2</sup> leading to a lot of signal overlap. Spectral resolution is thus a limiting factor for unambiguous chemical shift assignment and data interpretation for dynamics and structure elucidation. Acquiring the spectra at higher magnetic fields such as at a 1.2 GHz <sup>1</sup>H frequency helps to reduce spectral crowding, since resolution scales proportionally to the magnetic field strength. Here, we show that the linewidths of cross peaks in [<sup>1</sup>H,<sup>1</sup>H]-NOESY and [<sup>1</sup>H,<sup>1</sup>H]-TOCSY spectra can be further reduced by a factor of 2–3 in each dimension by super-resolution spectroscopy. In the indirect dimension a composite exponential-cosine weighted number of scans along the time increments are recorded and digitally smoothened by a window function, while in the direct dimension an exponential-cosine window function is applied. Furthermore, measurement time saving by reduced-acquisition super-resolution (RASR) is introduced. Application to the 20 kDa protein KRAS shows that highly resolved NMR spectra suitable for automated analysis can be acquired within less than 3 hours. The method opens an avenue towards automated chemical shift assignment, dynamics and structure determination of unlabeled small and medium size proteins within 24 hours.</p>","PeriodicalId":125,"journal":{"name":"Angewandte Chemie International Edition","volume":"63 50","pages":""},"PeriodicalIF":16.1000,"publicationDate":"2024-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/anie.202414324","citationCount":"0","resultStr":"{\"title\":\"Homonuclear Super-Resolution NMR Spectroscopy\",\"authors\":\"Olivia Gampp,&nbsp;Luca Wenchel,&nbsp;Prof. Peter Güntert,&nbsp;Prof. Roland Riek\",\"doi\":\"10.1002/anie.202414324\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>In homonuclear <sup>1</sup>H NMR (nuclear magnetic resonance) spectra such as [<sup>1</sup>H,<sup>1</sup>H]-NOESY (Nuclear Overhauser Enhancement spectroscopy), which is a historic cornerstone spectrum for biomolecular NMR structural biology, hundreds to thousands of cross peaks are present within a square of approximately 100 ppm<sup>2</sup> leading to a lot of signal overlap. Spectral resolution is thus a limiting factor for unambiguous chemical shift assignment and data interpretation for dynamics and structure elucidation. Acquiring the spectra at higher magnetic fields such as at a 1.2 GHz <sup>1</sup>H frequency helps to reduce spectral crowding, since resolution scales proportionally to the magnetic field strength. Here, we show that the linewidths of cross peaks in [<sup>1</sup>H,<sup>1</sup>H]-NOESY and [<sup>1</sup>H,<sup>1</sup>H]-TOCSY spectra can be further reduced by a factor of 2–3 in each dimension by super-resolution spectroscopy. In the indirect dimension a composite exponential-cosine weighted number of scans along the time increments are recorded and digitally smoothened by a window function, while in the direct dimension an exponential-cosine window function is applied. Furthermore, measurement time saving by reduced-acquisition super-resolution (RASR) is introduced. Application to the 20 kDa protein KRAS shows that highly resolved NMR spectra suitable for automated analysis can be acquired within less than 3 hours. The method opens an avenue towards automated chemical shift assignment, dynamics and structure determination of unlabeled small and medium size proteins within 24 hours.</p>\",\"PeriodicalId\":125,\"journal\":{\"name\":\"Angewandte Chemie International Edition\",\"volume\":\"63 50\",\"pages\":\"\"},\"PeriodicalIF\":16.1000,\"publicationDate\":\"2024-09-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://onlinelibrary.wiley.com/doi/epdf/10.1002/anie.202414324\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Angewandte Chemie International Edition\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/anie.202414324\",\"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":"Angewandte Chemie International Edition","FirstCategoryId":"92","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/anie.202414324","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

同核 1H NMR(核磁共振)光谱,如[1H,1H]-NOESY(核超豪瑟增强光谱),对于生物分子结构生物学至关重要。然而,该光谱包含数百至数千个交叉峰,这意味着在大约 100 ppm2 的范围内存在大量信号重叠。因此,光谱分辨率是动态和结构阐释数据解读的限制因素。在较高磁场(如 1.2 GHz 1H 频率)下获取光谱有助于减少光谱拥挤,因为分辨率与磁场强度成比例。在这里,我们展示了通过超分辨率光谱法,[1H,1H]-NOESY 和 [1H,1H]-TOCSY 光谱中交叉峰的线宽可以在每个维度上进一步缩小 2-3 倍。在间接维度上,沿时间增量记录指数余弦加权的复合扫描次数,并通过窗口函数进行数字平滑处理。此外,还引入了减少获取超分辨率(RASR)来节省测量时间。对 20 kDa 蛋白质 KRAS 的应用表明,适合自动分析的高分辨率 NMR 图谱可在 3 小时内获得。该方法为在 24 小时内对未标记的中小型蛋白质进行自动化学位移分配、动力学和结构测定开辟了一条途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Homonuclear Super-Resolution NMR Spectroscopy

Homonuclear Super-Resolution NMR Spectroscopy

In homonuclear 1H NMR (nuclear magnetic resonance) spectra such as [1H,1H]-NOESY (Nuclear Overhauser Enhancement spectroscopy), which is a historic cornerstone spectrum for biomolecular NMR structural biology, hundreds to thousands of cross peaks are present within a square of approximately 100 ppm2 leading to a lot of signal overlap. Spectral resolution is thus a limiting factor for unambiguous chemical shift assignment and data interpretation for dynamics and structure elucidation. Acquiring the spectra at higher magnetic fields such as at a 1.2 GHz 1H frequency helps to reduce spectral crowding, since resolution scales proportionally to the magnetic field strength. Here, we show that the linewidths of cross peaks in [1H,1H]-NOESY and [1H,1H]-TOCSY spectra can be further reduced by a factor of 2–3 in each dimension by super-resolution spectroscopy. In the indirect dimension a composite exponential-cosine weighted number of scans along the time increments are recorded and digitally smoothened by a window function, while in the direct dimension an exponential-cosine window function is applied. Furthermore, measurement time saving by reduced-acquisition super-resolution (RASR) is introduced. Application to the 20 kDa protein KRAS shows that highly resolved NMR spectra suitable for automated analysis can be acquired within less than 3 hours. The method opens an avenue towards automated chemical shift assignment, dynamics and structure determination of unlabeled small and medium size proteins within 24 hours.

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
CiteScore
26.60
自引率
6.60%
发文量
3549
审稿时长
1.5 months
期刊介绍: Angewandte Chemie, a journal of the German Chemical Society (GDCh), maintains a leading position among scholarly journals in general chemistry with an impressive Impact Factor of 16.6 (2022 Journal Citation Reports, Clarivate, 2023). Published weekly in a reader-friendly format, it features new articles almost every day. Established in 1887, Angewandte Chemie is a prominent chemistry journal, offering a dynamic blend of Review-type articles, Highlights, Communications, and Research Articles on a weekly basis, making it unique in the field.
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信