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- W2912116930 endingPage "1779" @default.
- W2912116930 startingPage "1770" @default.
- W2912116930 abstract "TisB is a short amphiphilic α-helical peptide from Escherichia coli that induces a breakdown of the pH gradient across the inner membrane when the bacteria are under stress and require to form persister cells to turn into a biofilm. A computational–experimental approach combining all-atom and coarse-grained molecular dynamics simulation with circular dichroism spectroscopy and gel electrophoresis was used to reveal its structure and oligomeric assembly in a phospholipid bilayer. TisB is found to be inserted upright in the membrane as a tetrameric bundle with a left-handed sense of supercoiling, best described as an antiparallel dimer-of-dimers. The tetramer is stabilized by means of a regular but dynamically interchanging pattern of salt bridges and hydrogen bonds, in accordance with the recently proposed “charge-zipper” motif." @default.
- W2912116930 created "2019-02-21" @default.
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- W2912116930 date "2019-02-01" @default.
- W2912116930 modified "2023-10-18" @default.
- W2912116930 title "Tetrameric Charge-Zipper Assembly of the TisB Peptide in Membranes—Computer Simulation and Experiment" @default.
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- W2912116930 doi "https://doi.org/10.1021/acs.jpcb.8b12087" @default.
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