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Related Concept Videos

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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¹H NMR of Labile Protons: Temporal Resolution01:10

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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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¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

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

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

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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.
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Updated: Feb 28, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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Revealing protein dynamics with high-pressure NMR.

Julien Roche1, Christian Roumestand2, Catherine A Royer3

  • 1Roy J. Carver Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, USA.

Quarterly Reviews of Biophysics
|February 26, 2026
PubMed
Summary

Predicting protein functional dynamics requires more experimental data. High hydrostatic pressure can perturb protein structures locally, enabling the study of functionally important, high-energy states.

Keywords:
NMRhigh pressurehydrationprotein dynamicsvolume

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Protein structure prediction from sequence is advanced, but predicting functional dynamics remains a challenge.
  • Understanding protein dynamics is crucial for function and turnover, but key states are difficult to access experimentally.
  • Existing methods like high temperatures or chemical denaturants have limitations in probing these states.

Purpose of the Study:

  • To explore methods for accessing and characterizing high-energy protein dynamic states.
  • To investigate the utility of high hydrostatic pressure as a perturbation tool for protein dynamics.

Main Methods:

  • Utilizing high hydrostatic pressure as a variable to perturb protein structure.
  • Analyzing local structural disruption around internal cavities within proteins.
  • Characterizing populated higher free energy states through pressure-induced perturbations.

Main Results:

  • High hydrostatic pressure can locally perturb protein structure near internal cavities.
  • This perturbation leads to partial structural disruption and populates higher energy states.
  • Pressure provides a method to access and characterize states not typically populated.

Conclusions:

  • High hydrostatic pressure is a valuable tool for studying protein functional dynamics.
  • It offers a way to access and characterize transient, high-energy conformational states.
  • This approach can contribute to building a larger experimental database for sequence-dynamics-function relationships.