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Updated: Dec 30, 2025

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Hydrogen-exchange kinetics studied through analysis of self-decoupling of nuclear magnetic resonance
Ridvan Nepravishta1, Binhan Yu1, Junji Iwahara1
1Department of Biochemistry & Molecular Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555-1068, USA.
Abstract:
Hydrogen exchange between solute and water molecules occurs across a wide range of timescales. Rapid hydrogen-exchange processes can effectively diminish 1H-15N scalar couplings. We demonstrate that the self-decoupling of 15N nuclear magnetic resonance can allow quantitative investigations of hydrogen exchange on a micro- to millisecond timescale, which is relatively difficult to analyze with other methods. Using a Liouvillian matrix incorporating hydrogen exchange as a mechanism for scalar relaxation, the hydrogen exchange rate can be determined from 15N NMR line shapes recorded with and without 1H decoupling. Self-decoupling offers a simple approach to analyze the kinetics of hydrogen exchange in a wide range of timescale.
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