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Related Concept Videos

Conformity01:20

Conformity

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Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.
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Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

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In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must...
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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

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The spin state of an NMR-active nucleus can have a slight effect on its immediate electronic environment. This effect propagates through the intervening bonds and affects the electronic environments of NMR-active nuclei up to three bonds away; occasionally, even farther. This phenomenon is called spin–spin coupling or J-coupling. Coupling interactions are mutual and result in small changes in the absorption frequencies of both nuclei involved. While nuclei of the same element are involved...
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Spin–Spin Coupling: One-Bond Coupling01:17

Spin–Spin Coupling: One-Bond Coupling

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Coupling interactions are strongest between NMR-active nuclei bonded to each other, where spin information can be transmitted directly through the pair of bonding electrons. While nuclei polarize their electrons to the opposite spins, the bonding electron pair has opposite spins. Configurations with antiparallel nuclear spins are expected to be lower in energy. When coupling makes antiparallel states more favorable, J is considered to have a positive value. The one-bond coupling constant, 1J,...
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Conformations of Butane02:20

Conformations of Butane

17.7K
Unlike ethane and propane that have only two major conformations, butane has more than two conformers. The staggered form of butane in which the bulky methyl groups on the two carbons are placed on opposite sides, that is, at a dihedral angle of 180°, is the lowest energy, most stable form — called the anti conformer. This conformation is stabilized due to the absence of steric repulsion between the largely spaced out methyl groups. The other two staggered conformations are...
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Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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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...
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Related Experiment Video

Updated: Jan 21, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
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Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

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Identifying Protein Conformational Dynamics Using Spin-label ESR.

Yei-Chen Lai1,2, Yun-Hsuan Kuo1, Yun-Wei Chiang1

  • 1Department of Chemistry, National Tsing Hua University, Hsinchu, 30013, Taiwan.

Chemistry, an Asian Journal
|August 8, 2019
PubMed
Summary
This summary is machine-generated.

Electron spin resonance (ESR) advances protein dynamics research by resolving complex biological processes. New ESR methods capture individual protein dynamics, even in low-populated states, complementing existing biophysical tools.

Keywords:
Allosteric regulationConformational equilibriumDistance measurementsElectron spin resonanceProtein dynamicsSaturation ESR

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Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Protein dynamics are crucial for molecular function.
  • Characterizing dynamic processes in proteins and membranes is challenging.
  • Existing biophysical tools have limitations in resolving complex dynamics.

Purpose of the Study:

  • To highlight recent advances in spin-label electron spin resonance (ESR) for characterizing protein dynamics.
  • To showcase the application of ESR in resolving dynamical components during biological processes.
  • To present ESR as a complementary tool for studying complex protein structural and dynamical aspects.

Main Methods:

  • Spin-label electron spin resonance (ESR) spectroscopy.
  • Application of ESR to study protein dynamics in various biological contexts.
  • Development of ESR methods for resolving individual dynamical components, including low-populated states.

Main Results:

  • ESR can resolve dynamical components during biological processes.
  • ESR has been applied to study protein conformational changes during translocation.
  • ESR effectively analyzes conformational exchange, protein oligomerization, and environmental effects on protein dynamics.

Conclusions:

  • Newly developed ESR methods significantly enhance the characterization of protein dynamics.
  • ESR provides valuable insights into challenging topics like protein-protein interactions and membrane protein dynamics.
  • ESR is a powerful complement to existing biophysical techniques for molecular-level understanding.