Related Experiment Video
Updated: May 28, 2026

Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
Published on: April 17, 2017
Hydrogen-deuterium exchange coupled to mass spectrometry to investigate ligand-receptor interactions
Jessmi M L Ling1, Leslie Silva, David C Schriemer
1Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, AB, Canada. jling@ambrose.edu
Abstract:
A method for exploring protein-protein interactions using hydrogen/deuterium exchange coupled to mass spectrometry is described. The method monitors the exchange of backbone (amide) hydrogens in solutions of deuterated water that primarily occur on portions of the protein exposed to solvent. In the presence of a protein binding partner, regions that experience reduced exchange are either part of the protein-protein interaction interface or undergo conformational changes to reduce accessibility to solvent. This method has the advantage of being used under physiological conditions with unmodified proteins. In this chapter, we describe an approach suitable for probing interactions among relatively large proteins using conventional mass spectrometry systems. The interaction between human transferrin and the Neisseria meningitidis receptor protein, transferrin binding protein B, provides a challenging system as an example.
Related Concept Videos
¹H NMR of Labile Protons: Deuterium (²H) Substitution
Tandem Mass Spectrometry
2D NMR: Overview of Heteronuclear Correlation Techniques
Mass Spectrometry: Complex Analysis
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)
High-Resolution Mass Spectrometry (HRMS)

