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- W1987498536 endingPage "502" @default.
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- W1987498536 abstract "The bacterial elongation factor for protein synthesis, EF-Tu, polymerizes into fibrils at pH 6.0. These fibrils are 0.7 microM in diameter, at least 200 microns in length, and are positively birefringent. Electron microscopic observations of negatively stained images demonstrates that the EF-Tu fibrils consist of bundles of individual filaments, approximately 5nm in diameter, aligned parallel to the long axis of the fibril. Polymerized EF-Tu exchanges nucleotide rapidly and interacts with the other elongation factor, EF-Ts. The antibiotic kirromycin induces the polymerization of EF-Tu into fibrils and even larger structures under nonpolymerizing conditions." @default.
- W1987498536 created "2016-06-24" @default.
- W1987498536 creator A5080399997 @default.
- W1987498536 date "1979-07-01" @default.
- W1987498536 modified "2023-10-16" @default.
- W1987498536 title "Polymerization of the Bacterial Elongation Factor for Protein Synthesis, EF-Tu" @default.
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- W1987498536 doi "https://doi.org/10.1111/j.1432-1033.1979.tb13137.x" @default.
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