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Updated: Aug 22, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
New chemical crosslinking methods for the identification of transient protein-protein interactions with multiprotein
1Institut für Mikrobiologie, Biozentrum, Goethe Universität, Marie-Curie-St. 9, N250, 60439 Frankfurt am Main, Germany. k.melcher@ulster.ac.uk.
Abstract:
Most proteins function as multiprotein complexes or interact with multiprotein complexes. Identification of protein-protein interactions in the context of their physiologically relevant complexes is therefore key to fully understand the cellular machinery. Here I discuss advances in chemical crosslinking methods that allow investigators to map direct subunit contacts in transient interactions with multimeric complexes. Methods discussed fall into two categories: (i) in vitro approaches with localized, inducible crosslinking reagents and (ii) in vivo approaches with unlocalized crosslinkers.
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