Mass spectrometry of ribosomes and ribosomal subunits Journal Article


Authors: Benjamin, D. R.; Robinson, C. V.; Hendrick, J. P.; Hartl, F. U.; Dobson, C. M.
Article Title: Mass spectrometry of ribosomes and ribosomal subunits
Abstract: 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.
Keywords: nonhuman; protein conformation; mass spectrometry; protein assembly; protein protein interaction; molecular dynamics; protein binding; escherichia coli; protein biosynthesis; protein folding; structure analysis; molecular weight; protein determination; ribosomal proteins; ribosome protein; ribosomes; rna, bacterial; protein rna binding; ribosome; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 95
Issue: 13
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1998-06-23
Start Page: 7391
End Page: 7395
Language: English
DOI: 10.1073/pnas.95.13.7391
PUBMED: 9636159
PROVIDER: scopus
PMCID: PMC22627
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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  1. F. Ulrich Hartl
    75 Hartl