Abstract
The bacterial mechanosensitive channel of small conductance, MscS, has been extensively studied to understand how mechanical forces are converted into the conformational changes that underlie mechanosensitive (MS) channel gating. We recently demonstrated that lipid removal by β-cyclodextrin can mimic membrane tension in membrane-scaffold protein-based lipid nanodiscs, providing novel insights into the structural rearrangements that underlie MscS channel gating in response to membrane tension. Here, we show that all cyclodextrins (CDs) can activate reconstituted E.
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