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Back Cover: Mapping the Interactions of Selective Biochemical Probes of Antibody Conformation by Hydrogen–Deuterium Exchange Mass Spectrometry (ChemBioChem 11/2017)
Author(s) -
Leurs Ulrike,
Beck Hermann,
Bonnington Lea,
Lindner Ingo,
Pol Ewa,
Rand Kasper
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700245
Subject(s) - hydrogen–deuterium exchange , chemistry , surface plasmon resonance , mass spectrometry , deuterium , cover (algebra) , antibody , biophysics , nanotechnology , chromatography , materials science , mechanical engineering , physics , quantum mechanics , engineering , nanoparticle , immunology , biology
The back cover picture shows the structure of an IgG1 antibody that is undergoing environmental stress (e.g., oxidation). Three Fab biochemical probes were generated to detect the resulting conformational changes in a therapeutic IgG1 antibody by local hydrogen–deuterium‐exchange mass spectrometry (HDX‐MS). Surface plasmon resonance (SPR) experiments show that these domain‐selective Fab probes are sensitive to conformational changes in a full‐length therapeutic antibody upon oxidation. More information can be found in the full paper by K. Rand et al. on page 1016 in Issue 11, 2017 (DOI: 10.1002/cbic.201600670).