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Related Concept Videos

¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

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Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are...
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NMR Spectroscopy: Spin–Spin Coupling01:08

NMR Spectroscopy: Spin–Spin Coupling

3.0K
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...
3.0K
¹H NMR: Long-Range Coupling01:27

¹H NMR: Long-Range Coupling

2.6K
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...
2.6K
Spin–Spin Coupling: One-Bond Coupling01:17

Spin–Spin Coupling: One-Bond Coupling

1.4K
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,...
1.4K
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
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.7K
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.
1.7K

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Updated: Jan 18, 2026

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

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Characterization of intrinsically disordered regions through scalar coupling-based solid-state NMR experiments.

Tong Zeng1, Juan Li1, Chaowei Shi2

  • 1MOE Key Lab for Cellular Dynamics, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230022, China.

Biophysics Reports
|September 11, 2025
PubMed
Summary

Abnormal amyloid fibrils, implicated in neurodegenerative diseases, feature rigid cores and disordered fuzzy coats. New solid-state NMR methods enable structural characterization of these intrinsically disordered regions (IDR) in amyloid fibrils.

Keywords:
Amyloid fibrilsIDRINEPTScalar couplingSolid-state NMR

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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Area of Science:

  • Biochemistry
  • Neuroscience
  • Structural Biology

Background:

  • Abnormal amyloid fibrils are hallmarks of neurodegenerative diseases, causing neuroinflammation and neuronal death.
  • Amyloid fibrils possess a rigid cross-β sheet core and a surrounding "fuzzy coat" of intrinsically disordered regions (IDR).
  • Structural characterization of the rigid core is advanced, but the disordered IDR remains challenging to study.

Purpose of the Study:

  • To apply advanced solid-state NMR techniques for backbone assignment of IDR in amyloid fibrils.
  • To elucidate the conformational dynamics of IDR during ligand binding.
  • To improve understanding of amyloid fibril structure-function relationships in disease.

Main Methods:

  • Utilized two-dimensional (2D) heteronuclear single quantum coherence (HSQC) and three-dimensional (3D) HNCO, HNCA, and HN(CO)CA spectra.
  • Employed scalar coupling-based 1H detection magic angle spinning (MAS) ssNMR techniques.
  • Focused on backbone assignment of intrinsically disordered regions (IDR) within amyloid fibrils.

Main Results:

  • Successfully applied 2D and 3D ssNMR techniques for IDR backbone assignment.
  • Demonstrated the feasibility of characterizing disordered protein conformations in amyloid fibrils.
  • Established a foundation for studying IDR conformational changes upon ligand interaction.

Conclusions:

  • Advanced ssNMR methods provide crucial insights into the structure of IDR in amyloid fibrils.
  • This approach facilitates the study of conformational changes relevant to neurodegenerative disease mechanisms.
  • Enables further investigation into the role of IDR in amyloid fibril function and ligand interactions.