ArticleMethods in molecular biology (Clifton, N.J.)2026
Hydrogen Exchange Mass Spectrometry (HX-MS) for Mapping Antibody Binding Sites and Conformational Dynamics of ADAMTS13.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Hydrogen exchange mass spectrometry (HX-MS) enables the determination of subtle conformational and dynamic changes in proteins under near-physiological conditions. Exchange of backbone amide hydrogens in proteins with deuterium occurs in solution and is influenced by solvent accessibility, hydrogen bonding, and structural dynamics. In this protocol, we employ HX-MS to investigate conformational dynamics and map antibody binding sites of ADAMTS13 using the N-terminal truncated variant MDTCS (e.g., metalloprotease, disintegrin, thrombospondin type 1 repeat, cysteine-rich, and spacer domain). Deuterium incorporation is monitored over multiple time points and mapped onto known protein structures to reveal protected and flexible regions, which infers the antibody binding epitope on ADAMTS13. This method is applicable to study any other proteins that interact with their ligand or antibodies.
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