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Related Concept Videos

Atomic Nuclei: Types of Nuclear Relaxation01:28

Atomic Nuclei: Types of Nuclear Relaxation

634
Nuclear relaxation restores the equilibrium population imbalance and can occur via spin–lattice or spin–spin mechanisms, which are first-order exponential decay processes.
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers...
634
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

1.1K
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...
1.1K
NMR Spectrometers: Resolution and Error Correction01:14

NMR Spectrometers: Resolution and Error Correction

944
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...
944
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

1.3K
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...
1.3K
¹H NMR of Conformationally Flexible Molecules: Variable-Temperature NMR01:15

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

1.4K
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.
1.4K
¹H NMR of Labile Protons: Temporal Resolution01:10

¹H NMR of Labile Protons: Temporal Resolution

1.5K
Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
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Related Experiment Video

Updated: Nov 28, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Protein Dynamics revealed by NMR Relaxation Methods.

Fa-An Chao1, R Andrew Byrd1

  • 1Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702-1201.

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|November 26, 2020
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Summary

Nuclear Magnetic Resonance (NMR) spectroscopy reveals biomolecular dynamics crucial for function, extending beyond static structures. Advanced NMR methods and analysis tools enhance our understanding of protein dynamics and biological molecular functions.

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Area of Science:

  • Structural biology
  • Biophysics
  • Molecular dynamics

Background:

  • The Protein Data Bank (PDB) primarily archives static, three-dimensional structures of macromolecules.
  • Understanding biological function requires knowledge of molecular dynamics, conformational changes, and interactions occurring over various timescales.
  • Static structures alone are insufficient for comprehensive functional annotation.

Purpose of the Study:

  • To review the current state of Nuclear Magnetic Resonance (NMR) spectroscopy for studying biomolecular dynamics.
  • To highlight advancements in NMR methodology and analysis tools for interpreting molecular motions.
  • To emphasize the role of NMR in integrated structural biology.

Main Methods:

  • Utilizing Nuclear Magnetic Resonance (NMR) spectroscopy, particularly spin relaxation methods.
  • Sampling molecular motions across a wide range of timescales (picoseconds to seconds) at atomic resolution.
  • Employing physiologically relevant conditions for experiments.

Main Results:

  • NMR spectroscopy is uniquely capable of probing biomolecular dynamics across diverse timescales.
  • New experimental techniques and expanded analysis tools provide more detailed insights into molecular motions.
  • Enhanced interpretation methods improve functional annotation of PDB data.

Conclusions:

  • NMR spectroscopy is essential for understanding the dynamic nature of biomolecules.
  • Advancements in NMR methodology and computational tools are crucial for future discoveries in structural biology.
  • NMR plays a key role in integrated structural biology, complementing computational molecular dynamics.