Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Double Resonance Techniques: Overview01:12

Double Resonance Techniques: Overview

Double resonance techniques in Nuclear Magnetic Resonance (NMR) spectroscopy involve the simultaneous application of two different frequencies or radiofrequency pulses to manipulate and observe two distinct nuclear spins. One important application of double resonance is spin decoupling, which selectively suppresses coupling with one type of nucleus while observing the NMR signal from another nucleus, simplifying the spectrum and enhancing resolution.
Spin decoupling is usually achieved by...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Alternative Splicing of a Structured Partner Alters the Folding-Upon-Binding Trajectory of an Intrinsically Disordered Protein.

Journal of the American Chemical Society·2026
Same author

Structural and functional insights into a mesophilic cold shock protein CspA with enhanced precision.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same author

Correction: Dynamic conformational equilibria in the active states of KRAS and NRAS.

RSC chemical biology·2026
Same author

A <sup>13</sup>C<sup>β</sup> CEST experiment with improved sensitivity for the characterization of protein excited states.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2026
Same author

The dynamic and heterogeneous structure of the non-canonical inflammasome.

bioRxiv : the preprint server for biology·2026
Same author

Two-dimensional NMR from a single pulse: Reconstructing heteronuclear 2D spectra via off-resonance decoupling and deep neural networks.

Proceedings of the National Academy of Sciences of the United States of America·2026

相关实验视频

Updated: Jun 5, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

基于分裂进化的脉冲方案,用于量化蛋白质的交换过程:强大的补充放松分散实验的放松分散实验.

Guillaume Bouvignies1, D Flemming Hansen, Pramodh Vallurupalli

  • 1Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, Canada M5S 1A8.

Journal of the American Chemical Society
|January 20, 2011
PubMed
概括
此摘要是机器生成的。

这项研究引入了一种用于测量毫秒时间尺度上蛋白质化学交换的新方法. 通过分析光谱峰值转移,它为研究蛋白质动态的现有技术提供了一个补充的方法.

更多相关视频

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

相关实验视频

Last Updated: Jun 5, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

科学领域:

  • 生物化学 生物化学
  • 结构生物学 结构生物学
  • 化学物理 化学物理

背景情况:

  • 蛋白质动态对于功能至关重要,涉及化学交换过程.
  • 像卡尔-普尔塞尔-梅布姆-吉尔 (CPMG) 这样的现有方法在研究某些汇率制度方面存在局限性.
  • 量化毫秒时间尺度交换对于理解蛋白质 - 配体相互作用和构造变化至关重要.

研究的目的:

  • 提出一种用于量化毫秒时间尺度蛋白质化学交换的新方法.
  • 扩大可访问的汇率和人口分布范围,以进行动态研究.
  • 为已建立的蛋白质动态分析方法提供一种补充技术.

主要方法:

  • 使用一个2D (15)N, (1)H(N) 核磁共振 (NMR) 实验.
  • 通过使用短旋回声脉冲列车,通过变化的 (15) N 停留时间来测量化学交换率.
  • 分析了光谱峰值位置的变化,而不是放松率.

主要成果:

  • 该方法成功量化了蛋白质 - 连接体系统中的毫秒时间尺度交换.
  • 通过准确确定与替代方法可比的交换参数来证明实用性.
  • 计算显示,与CPMG进行的综合分析扩展了研究,以减缓汇率 (降至20秒) 和偏斜的人口.

结论:

  • 提出的NMR方法提供了一种强大的方法来量化毫秒时间尺度蛋白质交换.
  • 这种技术增强了对蛋白质动态的研究,特别是对于具有具有挑战性交换参数的系统.
  • 结合CPMG,它扩大了NMR的范围,用于研究蛋白质构造格局.