with the cytoskeleton. Due to the binding of the cytoskeleton, the lateral diffusion of the transmembrane proteins may be greatly restricted or even become immobilized. Using a coarse-grained MARTINI model, we examined the effects of length and the distributing states of the immobilized WALP peptides on the domain formation of a ternary lipid bilayer. We found that, due to the position and tilt restrictions imposed on the peptides, the effect of hydrophobic mismatch between the peptides and membranes has a significant influence on both the domain formation of membrane and peptide sorting in the membrane.
growing list of amphitropic proteins that target cell and organelle membranes by sensing lipid packing defects via amphipathic a-helices, suggesting a pathway by which lipid homeostasis regulates mitochondrial function.
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