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- W2560434103 abstract "Recent work has demonstrated that cotranslational folding of proteins or protein domains in, or in the immediate vicinity of, the ribosome exit tunnel generates a pulling force on the nascent polypeptide chain that can be detected using a so-called translational arrest peptide (AP) engineered into the nascent chain as a force sensor. Here, we show that AP-based force measurements combined with systematic Ala and Trp scans of a zinc-finger domain that folds in the exit tunnel can be used to identify the residues that are critical for intraribosomal folding. Our results suggest a general approach to characterize the folded state(s) that may form as a protein domain moves progressively down the ribosome exit tunnel." @default.
- W2560434103 created "2016-12-16" @default.
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- W2560434103 date "2016-12-20" @default.
- W2560434103 modified "2023-09-26" @default.
- W2560434103 title "Mutational analysis of protein folding inside the ribosome exit tunnel" @default.
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- W2560434103 doi "https://doi.org/10.1002/1873-3468.12504" @default.
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