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Related Experiment Video

Updated: Jun 5, 2026

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the &#181;s-ms Timescale
08:09

15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale

Published on: April 19, 2021

Divided-evolution-based pulse scheme for quantifying exchange processes in proteins: powerful complement to

Guillaume Bouvignies1, D Flemming Hansen, Pramodh Vallurupalli

  • 1Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, Canada M5S 1A8.

Journal of the American Chemical Society
|January 20, 2011
PubMed
Summary
This summary is machine-generated.

This study introduces a new method for measuring protein chemical exchange on the millisecond timescale. By analyzing spectral peak shifts, it offers a complementary approach to existing techniques for studying protein dynamics.

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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

Published on: September 23, 2021

Area of Science:

  • Biochemistry
  • Structural Biology
  • Chemical Physics

Background:

  • Protein dynamics are crucial for function, involving chemical exchange processes.
  • Existing methods like Carr-Purcell-Meiboom-Gill (CPMG) have limitations in studying certain exchange regimes.
  • Quantifying millisecond timescale exchange is essential for understanding protein-ligand interactions and conformational changes.

Purpose of the Study:

  • To present a novel method for quantifying millisecond timescale chemical exchange in proteins.
  • To extend the accessible range of exchange rates and population distributions for dynamic studies.
  • To provide a complementary technique to established methods for protein dynamics analysis.

Main Methods:

  • Utilizes a 2D (15)N, (1)H(N) nuclear magnetic resonance (NMR) experiment.
  • Scales chemical exchange rates by varying (15)N dwell times using short spin-echo pulse trains.
  • Analyzes spectral peak position shifts instead of relaxation rates.

Main Results:

  • The method successfully quantifies millisecond timescale exchange in a protein-ligand system.
  • Demonstrates utility by accurately determining exchange parameters comparable to alternative methods.
  • Computations show combined analysis with CPMG extends study to slow exchange rates (down to 20 s(-1)) and skewed populations.

Conclusions:

  • The presented NMR method provides a robust way to quantify millisecond timescale protein exchange.
  • This technique enhances the study of protein dynamics, especially for systems with challenging exchange parameters.
  • Combined with CPMG, it expands the scope of NMR for investigating protein conformational landscapes.