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¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.8K
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.
1.8K
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.3K
At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
1.3K
Molecular Models02:00

Molecular Models

44.2K
Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
44.2K
VSEPR Theory02:37

VSEPR Theory

15.3K
Valence shell electron-pair repulsion theory (VSEPR theory) enables us to predict the molecular structure around a central atom from an examination of the number of bonds and lone electron pairs in its Lewis structure. The VSEPR model assumes that electron pairs in the valence shell of a central atom will adopt an arrangement that minimizes repulsions between these electron pairs by maximizing the distance between them. The electrons in the valence shell of a central atom form either bonding...
15.3K
Molecular Shapes01:18

Molecular Shapes

62.9K
Molecules have characteristic shapes that are crucial for their function. The arrangement of various electron groups around the central atom dictates their molecular geometry. Electron pairs in the valence shell of a central atom will adopt an arrangement that minimizes repulsions between the electron pairs by maximizing the distance between them. The valence electrons form either bonding pairs, located primarily between bonded atoms, or lone pairs.
Two regions of electron density in a diatomic...
62.9K
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.8K
The coupling interactions of nuclei across four or more bonds are usually weak, with J values less than 1 Hz. While these are usually not observed in spectra, the presence of multiple bonds along the coupling pathway can result in observable long-range coupling.
In alkenes, spin information is communicated via σ–π overlap, as seen in allylic (four-bond) and homoallylic (five-bond) couplings. These coupling interactions are stronger when the σ bond is parallel to the alkene...
2.8K

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Updated: Mar 3, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
10:10

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

5.7K

通过可分辨距离几何问题进行蛋白环建模,使用基于的NMR约束.

Rômulo S Marques1, Michael Souza2, Carlile Lavor1

  • 1Instituto de Matemática, Estatística e Computação Científica (IMECC - Unicamp), Universidade Estadual de Campinas, Campinas 13083-859, Brazil.

ACS omega
|March 2, 2026
PubMed
概括

这项研究通过包括原子来增强蛋白质循环建模,完善蛋白质结构预测. 这种方法提高了准确性和与已知的结构的一致性,这对计算生物学至关重要.

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

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

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相关实验视频

Last Updated: Mar 3, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
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Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures

Published on: December 1, 2020

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

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

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科学领域:

  • 计算生物学 计算生物学
  • 结构生物学 结构生物学
  • 生物物理学的生物物理.

背景情况:

  • 蛋白循环建模是关键的挑战,因为循环的灵活性和功能重要性.
  • 现有的模型经常省略原子,可能会限制准确性.

研究的目的:

  • 通过将原子纳入离散距离几何学来改进蛋白循环建模.
  • 从核磁共振 (NMR) 实验中利用实验上可访问的约束.

主要方法:

  • 使用一个离散距离几何公式,用分支和算法解决.
  • 综合原子与蛋白质骨干中的N和Cα结合,作为几何约束.
  • 进行计算实验,比较含和无模型.

主要成果:

  • 纳入原子减少了构造空间,产生了更受约束的模型.
  • 包括的模型证明了与已知的蛋白质结构有更好的一致性.
  • 这种方法改进了蛋白质构造的表示.

结论:

  • 包括原子在蛋白质循环建模中可以提高结构现实性和准确性.
  • 与制约增强的距离几何方法,对于结构改进有价值.
  • 这项工作为了解蛋白质结构和功能提供了更准确的计算方法.