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Updated: Jun 11, 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
When proteomics meets structural biology
1Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ , UK.
Abstract:
Recent progress in proteomics has identified vast arrays of interacting proteins together with knowledge of their post-translational modifications. A key challenge is to integrate this information with homology modelling and structural biology to provide a topological or even an atomic context for these modifications. Mass spectrometry (MS) is ideally placed to bring together these largely independent disciplines, being already established in proteomics and rapidly emerging in structural biology. By using MS-based approaches to probe the subunit stoichiometry of intact complexes, interaction networks and subunit packing can be defined, leading ultimately to 3D models. In this review, we discuss how superimposing proteomics information onto both low-resolution 3D models and high-resolution atomic structures can reveal new insight into function.
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