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- W3130519255 abstract "Abstract In vivo proteins fold mainly as they emerge from the ribosome or as they emerge from a membrane translocon. Membrane translocation in particular poses technical challenges to the study of the associated protein folding processes. Recently we have developed a single-molecule methodology that allows the capture of a single protein molecule through a membrane translocon with biotinylated oligonucleotides covalently bound at its N- and C- terminus using streptavidin. The resulting rotaxane can be driven forwards and backwards changing the voltage polarity, and carefully planned experiments allow inference of the folding pathway. Here we will discuss the details of a simplified methodological approach." @default.
- W3130519255 created "2021-03-01" @default.
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- W3130519255 date "2021-01-01" @default.
- W3130519255 modified "2023-10-16" @default.
- W3130519255 title "Use of pore-forming toxins to study co-translocational protein folding" @default.
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- W3130519255 doi "https://doi.org/10.1016/bs.mie.2021.01.018" @default.
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