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The observation of multiprotein complexes by mass spectrometry formerly relied upon chemical cross-linking to maintain interactions. Recent technological developments have enabled the observation of intact macromolecular complexes without modification. These assemblies, with masses far in excess of those measured previously, can be examined through controlled dissociation in the mass spectrometer, revealing information about their subunit interactions and topology.


Journal article


Curr Opin Struct Biol

Publication Date





135 - 141


Bacterial Proteins, Escherichia coli, Gases, Macromolecular Substances, Mass Spectrometry, Models, Molecular, Prealbumin, Protein Conformation, Proteins, Retinol-Binding Proteins, Ribosomal Proteins