The dynamic dimer structure of the chaperone Trigger Factor
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DOI: 10.1038/s41467-017-02196-7
Abstract: The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear.… read more here.
Keywords: trigger factor; dimer; chaperone trigger; dimer structure ... See more keywords
Dynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in Escherichia coli
Sign Up to like & getrecommendations! Published in 2024 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1101/2024.03.27.586930
Abstract: The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and co-translationally aids the folding of proteins in bacteria. Decades of studies have given a broad, but often conflicting, description of the substrate… read more here.
Keywords: escherichia coli; trigger factor; rnc binding; bacterial chaperone ... See more keywords