Relating helix tilt in a bilayer to lipid disorder: a mean-field theory.
We present a mean-field theory relating the helix tilt angle in a bilayer to lipid disorder. The theory provides a method to compare the rotational barriers for different helices in lipid bilayers. The results suggest that the helix tilt angle is strongly affected by both the hydrophobicity of the helix and the average lipid disorder. This leads us to point out future experiments that could shed light on lipid-protein interactions.
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Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA. lewynli@fas.harvard.edu
D000465:Algorithms; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D029968:Escherichia coli Proteins; D006096:Gramicidin / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D026901:Membrane Transport Proteins / Q000737:chemistry; D008968:Molecular Conformation; D009004:Monosaccharide Transport Proteins; D010713:Phosphatidylcholines / Q000737:chemistry; D027981:Symporters
D029968:Escherichia coli Proteins; D007473:Ion Channels; C050221:LacY protein, E coli; D008051:Lipid Bilayers; D026901:Membrane Transport Proteins; D009004:Monosaccharide Transport Proteins; D010713:Phosphatidylcholines; D027981:Symporters; D006096:Gramicidin; C021499:lactose permease