Abstract
Membrane proteins play vital and diverse roles in the cell, e.g., in membrane transport, signal transduction and molecular recognition, and inter-cellular communication in higher organisms. The membrane's lipid composition affects membrane protein helix insertion, positioning and oligomerization, but molecular mechanisms of these effects are largely unknown. We employ our novel highly mobile membrane mimetic (HMMM) model combined with molecular dynamics simulations to investigate structural and dynamic properties determining these lipid-protein interactions during insertion, hydrophobically driven positioning and dimer formation of transmembrane helices of glycophorin A (GpA).
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