Hydrogen-Deuterium Exchange Mass Spectrometry to Study Protein Complexes

Hydrogen-deuterium exchange (HDX) mass spectrometry (MS) can provide valuable information about binding, allostery, and other conformational effects of interaction in protein complexes. For protein-ligand complexes, where the ligand may be a small molecule, peptide, nucleotide, or another protein(s)...

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Bibliographic Details
Published inMethods in molecular biology (Clifton, N.J.) Vol. 1764; p. 153
Main Authors Kochert, Brent A, Iacob, Roxana E, Wales, Thomas E, Makriyannis, Alexandros, Engen, John R
Format Journal Article
LanguageEnglish
Published United States 2018
Subjects
Deuterium Exchange Measurement - methods
Humans
Hydrogen - chemistry
Mass Spectrometry - methods
Protein Binding
Protein Interaction Mapping - methods
Proteins - analysis
Proteins - chemistry
Proteins - metabolism
Binding
LC-MS
Ligand
Dissociation constant
Deuteration
Interactions
Percent bound
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Summary:Hydrogen-deuterium exchange (HDX) mass spectrometry (MS) can provide valuable information about binding, allostery, and other conformational effects of interaction in protein complexes. For protein-ligand complexes, where the ligand may be a small molecule, peptide, nucleotide, or another protein(s), a typical experiment measures HDX in the protein alone and then compares that with HDX for the protein when part of the complex. Multiple factors are critical in the design and implementation of such experiments, including thoughtful consideration of the percent protein bound, the effects of the labeling protocol on the protein complex, and the dynamic range of the analysis method. With careful planning and techniques, HDX MS analysis of protein complexes can be very informative.
ISSN:1940-6029
DOI:10.1007/978-1-4939-7759-8_10