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3 results for “MscL”
CT, XRF, MSCL data and reconstructions in support of Reilly et al., (2019) Holocene break-up and reestablishment of the Petermann Ice Tongue, Northwest Greenland
<p>Data sets include X-Ray Fluorescence (XRF), Computed Tomography (CT), and Multi-Sensor Core Logger (MSCL) data for cores collected from Petermann Fjord during the PETERMANN15 expedition of the Swedish Icebreaker Oden. Also, included are Fjord Ice-Rafted Debris (IRD) stacks and reconstructed Petermann Ice Tongue extents.</p> <p> </p> <p>XRF data includes data for OD1507 cores, 02UW, 03UW, 03PC, 03TC, 04GC, 06PC, 10PC, 40TC, 40PC.</p> <p>CT number data and CT derived IRD counts includes data for OD1507 cores, 02UW, 03UW, 03PC, 03TC, 04GC, 06PC, 08GC, 10PC, 40TC, 40PC.</p> <p>MSCL data includes data for OD1507 cores, 01UW, 02UW, 03UW, 01GC, 03PC, 03TC, 04GC, 06PC, 06TC, 08GC, 10PC, 10TC, 11GC, 12GC, 14GC, 37PC, 37TC, 40PC, 40TC, 41GC</p>
Data from: Force transduction and lipid binding in MscL: a continuum-molecular approach
The bacterial mechanosensitive channel MscL, a small protein mainly activated by membrane tension, is a central model system to study the transduction of mechanical stimuli into chemical signals. Mutagenic studies suggest that MscL gating strongly depends on both intra-protein and interfacial lipid-protein interactions. However, there is a gap between this detailed chemical information and current mechanical models of MscL gating. Here, we investigate the MscL bilayer-protein interface through molecular dynamics simulations, and take a combined continuum-molecular approach to connect chemistry and mechanics. We quantify the effect of membrane tension on the forces acting on the surface of the channel, and identify interactions that may be critical in the force transduction between the membrane and MscL. We find that the local stress distribution on the protein surface is largely asymmetric, particularly under tension, with the cytoplasmic side showing significantly larger and more localized forces, which pull the protein radially outward. The molecular interactions that mediate this behavior arise from hydrogen bonds between the electronegative oxygens in the lipid headgroup and a cluster of positively charged lysine residues on the amphipathic S1 domain and the C-terminal end of the second trans-membrane helix. We take advantage of this strong interaction (estimated to be 10–13 kT per lipid) to actuate the channel (by applying forces on protein-bound lipids) and explore its sensitivity to the pulling magnitude and direction. We conclude by highlighting the simple motif that confers MscL with strong anchoring to the bilayer, and its presence in various integral membrane proteins including the human mechanosensitive channel K2P1 and bovine rhodopsin.
Data from: Force transduction and lipid binding in MscL: a continuum-molecular approach
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