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Related Concept Videos

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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.
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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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Updated: Sep 17, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Extending the detectable time window of fast protein dynamics using 1HN E-CPMG.

Dwaipayan Mukhopadhyay1, Supriya Pratihar1,2, Stefan Becker1

  • 1Department for NMR-based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, 37077, Göttingen, Germany.

Journal of Biomolecular NMR
|June 30, 2025
PubMed
Summary

New NMR methods capture faster protein motions. Extreme power 1H Carr-Purcell-Meiboom-Gill (1H E-CPMG) experiments reveal new dynamics in human ubiquitin, enhancing our understanding of protein function.

Keywords:
Conformational exchangeNMRPeptide flipProtein dynamicsRelaxation dispersionUbiquitin

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Area of Science:

  • Biophysics
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Protein dynamics on the microsecond timescale are vital for biological function.
  • High power NMR relaxation dispersion experiments offer insights into these dynamics.
  • Extending the detectable time window for fast protein motions remains a challenge.

Purpose of the Study:

  • To develop and validate an advanced NMR technique for studying fast protein dynamics.
  • To extend the accessible timescale for observing protein motions.
  • To investigate the dynamics of human ubiquitin with enhanced temporal resolution.

Main Methods:

  • Development of extreme power 1H Carr-Purcell-Meiboom-Gill (1H E-CPMG) experiments.
  • Targeting backbone amide protons (1H_N) for enhanced sensitivity.
  • Acquisition of artifact-free relaxation dispersion profiles under extreme pulsing conditions.

Main Results:

  • The 1H E-CPMG method successfully extended the detectable time window for protein dynamics.
  • Analysis of human ubiquitin revealed a broader influence of peptide flip motion on the protein backbone.
  • A faster dynamic process at residue T09 was directly observed, consistent with pincer mode motion.

Conclusions:

  • The 1H E-CPMG technique is effective for studying fast protein dynamics.
  • This method enhances the temporal resolution for observing biologically relevant motions.
  • The findings provide new insights into the dynamic landscape of human ubiquitin.