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相关概念视频

¹H NMR of Labile Protons: Deuterium (²H) Substitution00:48

¹H NMR of Labile Protons: Deuterium (²H) Substitution

This lesson illustrates the role of deuterium substitution in simplifying the NMR spectrum of compounds comprising labile protons. One method employed is the use of deuterium. Amongst the three isotopes of hydrogen, deuterium (2H) has a nucleus composed of one proton and one neutron. When the D2O solvent is added to a pure dry ethanol solution, its labile proton is substituted with deuterium.
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...
Two-Dimensional (2D) NMR: Overview01:12

Two-Dimensional (2D) NMR: Overview

The 1D NMR spectrum of large and complex molecules like natural products has complicated splitting patterns and overlapping signals, which can be easily interpreted using 2-dimensional (2D) NMR. Unlike 1D NMR, 2D NMR has two frequency axes that provide the coupling information between the nucleus A and nucleus B in a molecule. The process from which 2D spectra are obtained has four steps.
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR

The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
Applications Of NMR In Biology01:25

Applications Of NMR In Biology

Nuclear magnetic resonance (NMR) spectroscopy is a very valuable analytical technique for researchers. It has been used for more than 50 years as an analytical tool. F. Bloch and E. Purcell formulated NMR in 1946 and won the 1952 Nobel Prize in Physics  for their work. Biological macromolecules such as proteins, nucleic acids, lipids, and organic molecules including pharmaceutical compounds, can be studied using this versatile tool that exploits the magnetic properties of certain nuclei.
The...
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: Jul 16, 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

用于大分子和超分子结构的溶液NMR技术.

Roland Riek1, Jocelyne Fiaux, Eric B Bertelsen

  • 1Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, CH-8093 Zürich, Switzerland.

Journal of the American Chemical Society
|October 10, 2002
PubMed
概括

这项研究将横向放松优化光谱学 (TROSY) 与极化转移技术相结合,使用2D NMR分析大型生物分子. 优化的实验参数使得大分子高达800kDa的高分辨率光谱成为可能.

科学领域:

  • 生物物理化学 生物物理化学
  • 结构生物学 结构生物学
  • 核磁共振 (NMR) 光谱学 核磁共振 (NMR) 光谱学

背景情况:

  • 使用溶液NMR分析大型同类寡合分子大分子 (110-800kDa) 由于信号扩大而存在挑战.
  • 标准的核磁共振技术往往难以为如此大型的生物结构提供高分辨率光谱.

研究的目的:

  • 开发和优化2D核磁共振方法,以获得大型 (15) N,(2) H标记的同类寡合分子宏分子的高质量相关谱.
  • 对大型生物分子结构的TROSY与CRIPT/CRINEPT技术的联合性能进行研究.

主要方法:

  • 结合横向放松优化光谱 (TROSY) 与交叉相关放松诱导极化转移 (CRIPT) 或交叉相关放松增强极化转移 (CRINEPT).
  • 获取的2D溶液NMR相关性光谱为 (15) N, ((2) H标记的同类寡合分子宏分子,范围为110至800kDa.
  • 系统优化极化转移时间,放松延迟和水处理程序.

主要成果:

  • 实现了基于TROSY的光谱,可管理的线宽 (例如,在800kDa时为15N的75Hz).
  • 确定了与分子大小成反比例的最佳极化转移时间 (例如,800kDa的1.4ms).
  • 由于H2O中的快速质子纵向放松,已确定的回收时间短 (<1秒) .

更多相关视频

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions
09:01

Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions

Published on: April 17, 2026

相关实验视频

Last Updated: Jul 16, 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

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions
09:01

Using Solution NMR to Characterize Biomolecular Condensates Under Biphasic Conditions

Published on: April 17, 2026

结论:

  • 结合CRIPT/CRINEPT-TROSY方法有效地为大型同类寡合分子宏分子产生高分辨率的2DNMR光谱.
  • 实验参数的优化,特别是传输时间和水抑制,对于大型结构的成功NMR分析至关重要.
  • 开发的方法显著推进了溶液中的大型生物分子组件的NMR研究.