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Nanoflow electrospray ionization has been used to introduce intact Escherichia coli ribosomes into the ion source of a mass spectrometer. Mass spectra of remarkable quality result from a partial, but selective, dissociation of the particles within the mass spectrometer. Peaks in the spectra have been assigned to individual ribosomal proteins and to noncovalent complexes of up to five component proteins. The pattern of dissociation correlates strongly with predicted features of ribosomal protein-protein and protein-RNA interactions. The spectra allow the dynamics and state of folding of specific proteins to be investigated in the context of the intact ribosome. This study demonstrates a potentially general strategy to probe interactions within complex biological assemblies.

Original publication




Journal article


Proc Natl Acad Sci U S A

Publication Date





7391 - 7395


Escherichia coli, Mass Spectrometry, Molecular Weight, Protein Binding, Protein Biosynthesis, Protein Conformation, RNA, Bacterial, Ribosomal Proteins, Ribosomes