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Related Experiment Video

Updated: May 7, 2026

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

CPMG relaxation dispersion.

Rieko Ishima1

  • 1Department of Structural Biology, University of Pittsburgh, Pittsburgh, PA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 25, 2013
PubMed
Summary
This summary is machine-generated.

This study details a protocol for (15)N Carr-Purcell-Meiboom-Gill (CPMG) R2 dispersion measurements. This technique characterizes protein conformational equilibria on the millisecond timescale, offering insights into energy landscapes.

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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
  • Biophysics

Background:

  • Nuclear Magnetic Resonance (NMR) relaxation probes protein dynamics.
  • Standard NMR experiments elucidate sub-nanosecond dynamics.
  • Millisecond timescale dynamics are crucial for understanding protein function and energy landscapes.

Purpose of the Study:

  • To present a detailed protocol for (15)N Carr-Purcell-Meiboom-Gill (CPMG) R2 dispersion measurements.
  • To enable characterization of protein equilibrium conformations interconverting on the millisecond timescale.
  • To provide a foundation for analyzing local conformational equilibria and protein energy landscapes.

Main Methods:

  • (15)N Carr-Purcell-Meiboom-Gill (CPMG) R2 dispersion experiments in solution.
  • Detailed protocol covering protein preparation.
  • Step-by-step experimental parameter settings and initial data analysis.

Main Results:

  • A comprehensive protocol for performing (15)N CPMG R2 dispersion measurements is described.
  • The protocol facilitates the study of millisecond-timescale protein dynamics.
  • The described method aids in understanding protein conformational equilibria.

Conclusions:

  • The presented protocol provides a standardized approach for (15)N CPMG R2 dispersion measurements.
  • This technique is valuable for investigating protein energy landscapes and conformational heterogeneity.
  • The study facilitates deeper insights into molecular recognition mechanisms through the study of protein dynamics.