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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
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Unveiling protein dynamics in solution with field-cycling NMR relaxometry

Giacomo Parigi1, Enrico Ravera1, Marco Fragai1

  • 1Magnetic Resonance Center (CERM) University of Florence, via Sacconi 6, Sesto Fiorentino, Italy; Department of Chemistry, "Ugo Schiff", University of Florence, via della Lastruccia 3, Sesto Fiorentino, Italy; Consorzio Interuniversitario Risonanze Magnetiche di Metalloproteine (CIRMMP), via Sacconi 6, Sesto Fiorentino, Italy.

Progress in Nuclear Magnetic Resonance Spectroscopy
|September 4, 2021
PubMed
Summary

Field-cycling NMR relaxometry, using nuclear magnetic relaxation dispersion (NMRD) profiles, reveals molecular dynamics in biological systems. This technique is particularly valuable for characterizing paramagnetic proteins and their water interactions.

Keywords:
Correlation timesMobilityNMRDParamagnetic relaxationRelaxation ratesRelaxometer

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