Abstract
Membrane proteins are involved in various cellular processes via interactions between their helices and the surrounding lipid environments. It is energetically favorable for transmembrane (TM) domain to match the hydrophobic thickness of the lipid bilayer. We have utilized a helix tilt restraint potential and the free energy decomposition technique to characterize the microscopic forces governing tilting of various TM peptides in different conditions. To investigate the influence of hydrophobic length of TM helix on its tilting, we used a model peptide called WALP (acetyl-GW2(LA)nLW2A-NH2) by varying systematically the length of the peptide (WALP16, WALP19, WALP23, and WALP27). Also, to study the influence of membrane hydrophobic thickness on TM helix tilting, we used two kind of lipid bilayer (DMPC and POPC). Finally, we used arginine, lysine, and alanine as a flanking residue instead of tryptophan (acetyl-GX2(LA)8LX2A-NH2: X = R, K, and A) to examine the influence of various anchoring residues on TM helix tilting. The detail structural features and energetic contribution from hydrophobic (mis)match between lipid and peptides are presented and discussed.
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