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- W2036452203 abstract "Although the structure of the bacterial ribosome, with varying resolutions has been uncovered, the subtle dynamics and interactions are to be pursued further. One vital aspect is the intrinsic helicase activity of the ribosome and how it unfolds structured mRNA during translation. The relevancy of the helicase function extends beyond general translation processes into recoding mechanisms such as frameshifting. Such process is found in viruses, bacteria and eukaryotes at varying efficiencies related to both physiological and pathological functions posing an interest to explore it further. Thus, we aim to study this process using single-molecule approaches along with bulk methods. First, we are developing bifluorescent constructs to quantify frameshifting both in vitro and in vivo for bacteria. Also, we are developing an ultrahigh resolution optical tweezers with fluorescence detection capabilities. The tweezers - FRET setup along with different labeling schemes could be used to monitor the ribosome during translation and its interactions with mRNA. This could elucidate further the dynamics and conformational changes intrinsically within the ribosome during the process of unfolding. In addition, it could provide fundamental insight into the variable efficiency of different frameshifting signals whether through the thermodynamic stability or conformational changes of structured elements within the signal." @default.
- W2036452203 created "2016-06-24" @default.
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- W2036452203 date "2014-01-01" @default.
- W2036452203 modified "2023-10-16" @default.
- W2036452203 title "Exploring the Ribosome Helicase Activity in Context of Frameshifting using Single-Molecule Techniques" @default.
- W2036452203 doi "https://doi.org/10.1016/j.bpj.2013.11.2746" @default.
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