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- W2912495938 abstract "The ribosome is the complex molecular machine found in all living cells that is responsible for the synthesis of all proteins. The ribosome is associated with various protein factors, including the GTPase Elongation Factor G (EF-G). EF-G is responsible for catalyzing tRNA and mRNA translocation on the ribosome, however, the mechanism of this translocation remains elusive. A recent crystallographic study has implied large conformational changes of EF-G during translocation. Previous studies observed only the elongated, post-conformational state; however, a compact, pre-translocation state has recently been seen. The question regarding the biological relevance of these conformational changes remains. To answer this, we have generated double-cysteine EF-G that is internally crosslinked, to itself, with various lengths of crosslinkers. If the large conformational change does occur in solution, then translocation will be affected by the crosslinking. To determine if crosslinking was successful, crosslinked samples were run on SDS-PAGE gels until band separation was observed. A purification protocol for large scale preparation of crosslinked EF-G was also developed using differences between crosslinked and non-crosslinked EF-G. We have done preliminary biophysical measurements on the crosslinked EF-G that implies large conformational change in EF-G may indeed occur." @default.
- W2912495938 created "2019-02-21" @default.
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- W2912495938 date "2019-02-01" @default.
- W2912495938 modified "2023-09-30" @default.
- W2912495938 title "Measuring the Mechanical Forces during Ribosome Translocation via Ef-G Crosslinking" @default.
- W2912495938 doi "https://doi.org/10.1016/j.bpj.2018.11.1964" @default.
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