• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利：CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法，用中文像聊天一样搜索，搜遍4000万医学文献。AI智能推荐，让科研检索更轻松。

立即免费搜索

文件翻译

保留排版，准确专业，支持PDF/Word/PPT等文件格式，支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述，25分钟生成高质量综述，智能提取关键信息，辅助科研写作。

立即免费体验

从缺失的氮弛豫数据快速评估蛋白质动力学

Fast evaluation of protein dynamics from deficient N relaxation data.

作者信息

Jaremko Łukasz, Jaremko Mariusz, Ejchart Andrzej, Nowakowski Michał

机构信息

Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology (KAUST), Thuwal, 23955-6900, Kingdom of Saudi Arabia.

Institute of Biochemistry and Biophysics, Polish Academy of Science, Pawinskiego 5A, 02-106, Warszawa, Poland.

出版信息

J Biomol NMR. 2018 Apr;70(4):219-228. doi: 10.1007/s10858-018-0176-3. Epub 2018 Mar 28.

DOI:10.1007/s10858-018-0176-3
PMID:29594733
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5953972/
Abstract

Simple and convenient method of protein dynamics evaluation from the insufficient experimental N relaxation data is presented basing on the ratios, products, and differences of longitudinal and transverse N relaxation rates obtained at a single magnetic field. Firstly, the proposed approach allows evaluating overall tumbling correlation time (nanosecond time scale). Next, local parameters of the model-free approach characterizing local mobility of backbone amide N-H vectors on two different time scales, S and R , can be elucidated. The generalized order parameter, S, describes motions on the time scale faster than the overall tumbling correlation time (pico- to nanoseconds), while the chemical exchange term, R , identifies processes slower than the overall tumbling correlation time (micro- to milliseconds). Advantages and disadvantages of different methods of data handling are thoroughly discussed.

摘要

基于在单一磁场下获得的纵向和横向N弛豫率的比值、乘积和差值，提出了一种从不足的实验N弛豫数据评估蛋白质动力学的简单便捷方法。首先，所提出的方法允许评估整体翻滚相关时间（纳秒时间尺度）。接下来，可以阐明无模型方法的局部参数，这些参数表征了主链酰胺N-H向量在两个不同时间尺度S和R上的局部流动性。广义序参数S描述了比整体翻滚相关时间更快的时间尺度上的运动（皮秒到纳秒），而化学交换项R识别比整体翻滚相关时间更慢的过程（微秒到毫秒）。深入讨论了不同数据处理方法的优缺点。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/f104f2fa96ac/10858_2018_176_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/f04823914d1f/10858_2018_176_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/4cd037f9e182/10858_2018_176_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/37ee787c86d5/10858_2018_176_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/4259904abab2/10858_2018_176_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/44043fd83737/10858_2018_176_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/e047d0903406/10858_2018_176_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/f104f2fa96ac/10858_2018_176_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/f04823914d1f/10858_2018_176_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/4cd037f9e182/10858_2018_176_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/37ee787c86d5/10858_2018_176_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/4259904abab2/10858_2018_176_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/44043fd83737/10858_2018_176_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/e047d0903406/10858_2018_176_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/321c/5953972/f104f2fa96ac/10858_2018_176_Fig7_HTML.jpg

相似文献

1
Fast evaluation of protein dynamics from deficient N relaxation data.从缺失的氮弛豫数据快速评估蛋白质动力学
J Biomol NMR. 2018 Apr;70(4):219-228. doi: 10.1007/s10858-018-0176-3. Epub 2018 Mar 28.
2
Sampling of protein dynamics in nanosecond time scale by 15N NMR relaxation and self-diffusion measurements.通过15N核磁共振弛豫和自扩散测量在纳秒时间尺度上对蛋白质动力学进行采样。
J Biomol Struct Dyn. 1999 Aug;17(1):157-74. doi: 10.1080/07391102.1999.10508348.
3
A comprehensive analysis of multifield 15N relaxation parameters in proteins: determination of 15N chemical shift anisotropies.蛋白质中多场 15N 弛豫参数的综合分析：15N 化学位移各向异性的测定
J Am Chem Soc. 2001 May 16;123(19):4567-76. doi: 10.1021/ja0038676.
4
Recent developments in (15)N NMR relaxation studies that probe protein backbone dynamics.用于探测蛋白质主链动力学的（15）N核磁共振弛豫研究的最新进展。
Top Curr Chem. 2012;326:99-122. doi: 10.1007/128_2011_212.
5
Detection of nano-second internal motion and determination of overall tumbling times independent of the time scale of internal motion in proteins from NMR relaxation data.利用核磁共振弛豫数据检测蛋白质中纳秒级的内部运动，并确定与内部运动时间尺度无关的整体翻滚时间。
J Biomol NMR. 2003 Dec;27(4):291-312. doi: 10.1023/a:1025836018993.
6
A new spin probe of protein dynamics: nitrogen relaxation in 15N-2H amide groups.蛋白质动力学的一种新型自旋探针：15N-2H酰胺基团中的氮弛豫
J Am Chem Soc. 2005 Mar 9;127(9):3220-9. doi: 10.1021/ja040215z.
7
Quantitative analysis of conformational exchange contributions to 1H-15N multiple-quantum relaxation using field-dependent measurements. Time scale and structural characterization of exchange in a calmodulin C-terminal domain mutant.利用场依赖测量对构象交换对1H-15N多量子弛豫的贡献进行定量分析。钙调蛋白C末端结构域突变体中交换的时间尺度和结构表征。
J Am Chem Soc. 2004 Jan 28;126(3):928-35. doi: 10.1021/ja037529r.
8
Protein dynamics by ¹⁵N nuclear magnetic relaxation.通过¹⁵N核磁共振弛豫研究蛋白质动力学
Methods Mol Biol. 2012;831:141-63. doi: 10.1007/978-1-61779-480-3_9.
9
Characterization of micros-ms dynamics of proteins using a combined analysis of 15N NMR relaxation and chemical shift: conformational exchange in plastocyanin induced by histidine protonations.利用¹⁵N NMR弛豫和化学位移的联合分析表征蛋白质的微秒级动力学：组氨酸质子化诱导的质体蓝素构象交换
J Am Chem Soc. 2004 Jan 28;126(3):753-65. doi: 10.1021/ja030366m.
10
General order parameter based correlation analysis of protein backbone motions between experimental NMR relaxation measurements and molecular dynamics simulations.基于广义序参量的实验性核磁共振弛豫测量与分子动力学模拟之间蛋白质主链运动的相关性分析。
Biochem Biophys Res Commun. 2015 Feb 13;457(3):467-72. doi: 10.1016/j.bbrc.2015.01.018. Epub 2015 Jan 17.

引用本文的文献

1
Structural insights into the DNA-binding mechanism of BCL11A: The integral role of ZnF6.BCL11A与DNA结合机制的结构解析：锌指结构域6的重要作用
Structure. 2024 Dec 5;32(12):2276-2286.e4. doi: 10.1016/j.str.2024.09.022. Epub 2024 Oct 17.
2
Pitfalls in measurements of R relaxation rates of protein backbone N nuclei.蛋白质主链氮原子核R弛豫率测量中的陷阱
J Biomol NMR. 2025 Mar;79(1):1-14. doi: 10.1007/s10858-024-00449-4. Epub 2024 Aug 31.
3
Increased slow dynamics defines ligandability of BTB domains.慢动力学增加定义了 BTB 结构域的配体结合能力。

本文引用的文献

1
Spatial attributes of the four-helix bundle group of bacteriocins - The high-resolution structure of BacSp222 in solution.四螺旋束细菌素的空间属性 - 溶液中 BacSp222 的高分辨率结构。
Int J Biol Macromol. 2018 Feb;107(Pt B):2715-2724. doi: 10.1016/j.ijbiomac.2017.10.158. Epub 2017 Oct 31.
2
Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.利用核磁共振光谱阐明分子运动在酶功能中的作用。
Prog Nucl Magn Reson Spectrosc. 2016 Feb;92-93:1-17. doi: 10.1016/j.pnmrs.2015.11.001. Epub 2015 Dec 7.
3
Protein dynamics from nuclear magnetic relaxation.
Nat Commun. 2022 Nov 16;13(1):6989. doi: 10.1038/s41467-022-34599-6.
4
NMR as a "Gold Standard" Method in Drug Design and Discovery.NMR 作为药物设计和发现的“金标准”方法。
Molecules. 2020 Oct 9;25(20):4597. doi: 10.3390/molecules25204597.
5
A Conformational Switch in the Zinc Finger Protein Kaiso Mediates Differential Readout of Specific and Methylated DNA Sequences.锌指蛋白 Kaiso 中的构象转换介导特定和甲基化 DNA 序列的差异读取。
Biochemistry. 2020 May 26;59(20):1909-1926. doi: 10.1021/acs.biochem.0c00253. Epub 2020 May 12.
6
Characterization of Internal Protein Dynamics and Conformational Entropy by NMR Relaxation.通过核磁共振弛豫表征内部蛋白质动力学和构象熵
Methods Enzymol. 2019;615:237-284. doi: 10.1016/bs.mie.2018.09.010. Epub 2018 Dec 8.
从核磁共振弛豫看蛋白质动力学。
Chem Soc Rev. 2016 May 7;45(9):2410-22. doi: 10.1039/c5cs00832h. Epub 2016 Mar 2.
4
Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.从核磁共振化学交换饱和转移数据快速测定快速蛋白质动力学
Angew Chem Int Ed Engl. 2016 Feb 24;55(9):3117-9. doi: 10.1002/anie.201511711. Epub 2016 Jan 28.
5
The Quest for Simplicity: Remarks on the Free-Approach Models.对简洁性的追求：关于自由进路模型的评论
J Phys Chem B. 2015 Sep 10;119(36):11978-87. doi: 10.1021/acs.jpcb.5b07181. Epub 2015 Aug 28.
6
NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.泛素激活酶第一催化结构域的 NMR 结构研究。
J Struct Biol. 2014 Jan;185(1):69-78. doi: 10.1016/j.jsb.2013.10.020. Epub 2013 Nov 6.
7
Solution NMR structure and dynamics of human apo-S100A1 protein.人源 apo-S100A1 蛋白的溶液 NMR 结构与动力学
J Struct Biol. 2011 May;174(2):391-9. doi: 10.1016/j.jsb.2011.01.011. Epub 2011 Feb 3.
8
Interpretation of biomolecular NMR spin relaxation parameters.生物分子 NMR 自旋弛豫参数的解读。
Biochem Cell Biol. 2010 Apr;88(2):131-42. doi: 10.1139/o09-152.
9
Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements.液晶和交叉相关弛豫测量中小蛋白中特定位置酰胺（15）N 化学位移各向异性张量。
J Am Chem Soc. 2010 Mar 31;132(12):4295-309. doi: 10.1021/ja910186u.
10
On the measurement of 15N-{1H} nuclear Overhauser effects.关于15N-{1H}核Overhauser效应的测量
J Magn Reson. 2008 Jun;192(2):302-13. doi: 10.1016/j.jmr.2008.03.011. Epub 2008 Mar 23.