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相关概念视频

NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

When magnetic nuclei in a sample achieve resonance and undergo relaxation, the signal detected in NMR is an approximately exponential free induction decay. Fourier transform of an exponential decay yields a Lorentzian peak in the frequency domain. Lorentzian peaks in an NMR spectrum are defined by their amplitude, full width at half maximum, and position, where the peak width is governed by the spin-spin relaxation time alone. In real experiments, however, the applied magnetic field is rendered...
2D NMR: Overview of Homonuclear Correlation Techniques01:16

2D NMR: Overview of Homonuclear Correlation Techniques

Homonuclear correlation spectroscopy (COSY) is a powerful technique used in Nuclear Magnetic Resonance (NMR) spectroscopy to study the correlations between nuclei of the same type within a molecule. It provides information about scalar couplings between adjacent nuclei, which helps determine connectivity and structural information. There are several COSY variants, each with its unique strengths and experimental parameters.
COSY90 is the standard two-dimensional (2D) COSY experiment that...
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...
2D NMR: Homonuclear Correlation Spectroscopy (COSY)01:06

2D NMR: Homonuclear Correlation Spectroscopy (COSY)

Homonuclear correlation spectroscopy, or COSY, is a 2-dimensional NMR technique that provides information about coupled protons. Typically, the geminal and vicinal coupling are observed. For example, consider the COSY spectrum of ethyl acetate, where its 1D proton NMR spectrum is plotted along the vertical and horizontal axes with their corresponding chemical shift scale. Three spots on the diagonal corresponding to the three peaks in the 1D proton spectrum are called diagonal peaks. The COSY...
NMR and Mass Spectroscopy of Carboxylic Acids01:30

NMR and Mass Spectroscopy of Carboxylic Acids

In ¹H NMR spectroscopy, acidic protons (–COOH) of carboxylic acids are highly deshielded and absorb far downfield, at around 9–12 ppm. The chemical shift value depends on the concentration and solvent used.
While α protons of carboxylic acids absorb at 2–2.5 ppm, β protons absorb further upfield.
Carboxylic acids are easily identified by dissolving them in deuterium oxide, which results in a rapid exchange of the acidic protons with deuterium. This leads to the disappearance of the acidic...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...

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相关实验视频

Updated: Jun 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

一种针对蛋白质的定向样本固态NMR的共振分配方法.

Robert W Knox1, George J Lu, Stanley J Opella

  • 1Department of Chemistry, North Carolina State University, 2620 Yarbrough Drive, Raleigh, North Carolina 27695-8204, USA.

Journal of the American Chemical Society
|June 1, 2010
PubMed
概括
此摘要是机器生成的。

这项研究引入了一种新的方法,用于对均的-15标记膜蛋白的固态NMR光谱进行分配. 该技术证实了现有的赋值,并有助于确定蛋白质结构,而不需要专门的标签.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

相关实验视频

Last Updated: Jun 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

科学领域:

  • 结构生物学 结构生物学
  • 生物物理学的生物物理.
  • 核磁共振 (NMR) 光谱学 核磁共振 (NMR) 光谱学

背景情况:

  • 赋予膜蛋白的固态NMR光谱对于结构确定至关重要.
  • 单轴对齐的蛋白质提供了独特的见解,但也带来了分配挑战.
  • 现有的方法通常需要选择性标记样本,限制了广泛的适用性.

研究的目的:

  • 为均 (15)N标记的单轴对齐的膜蛋白提出一个一般的顺序分配策略.
  • 为了证明该方法的有效性,使用磁对齐的Pf1菌体外衣蛋白.
  • 通过固态NMR促进膜蛋白的结构确定.

主要方法:

  • 采用不匹配的哈特曼-哈恩磁化转移,用于15N脊柱旋转之间的质子介导相关性.
  • 获取和叠加交换和非交换的分离局部场谱.
  • 使用单轴对齐的膜蛋白,特别是Pf1菌体外层蛋白.

主要成果:

  • 从文献中成功确认了大多数原始任务,而不需要选择性标记样本.
  • 通过比较不同的频谱收购来区分跨峰和主要峰.
  • 证明适用于任意拓的蛋白质.

结论:

  • 拟议的顺序分配策略对均 (15)N标记的单轴对齐的膜蛋白有效.
  • 这种方法简化了光谱分配,减少了复杂标签策略的需要.
  • 该技术对未来基于固态NMR的膜蛋白结构确定具有价值.