Relating helix tilt in a bilayer to lipid disorder: A mean-field theory

Biophysical Chemistry

Volumn 86, Issue 1, 2000, Pages 79-83

  Li, Lewyn ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

Helix tilt; Lipid disorder; Mean field theory; Membrane protein

Indexed keywords

LACTOSE PERMEASE; LIPID;

ARTICLE; BILAYER MEMBRANE; HYDROPHOBICITY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; THEORY;

ALGORITHMS; CHEMISTRY, PHYSICAL; ESCHERICHIA COLI PROTEINS; GRAMICIDIN; ION CHANNELS; LIPID BILAYERS; MEMBRANE TRANSPORT PROTEINS; MOLECULAR CONFORMATION; MONOSACCHARIDE TRANSPORT PROTEINS; PHOSPHATIDYLCHOLINES; SYMPORTERS;

EID: 0033947732     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00163-0     Document Type: Article

References (29)

1. Fattal D.R., Ben-Shaul A. A molecular model for lipid-protein interactions in membranes: the role of hydrophobic mismatch. Biophys. J. 65:1993;1795-1808.
2. Pink D.A., Chapman D. Protein-lipid interactions in bilayer membranes: a lattice model. Proc. Natl. Acad. Sci. USA. 76:1979;1542-1546.
3. Mouritsen O.G., Bloom M. Models of lipid-protein interactions in membranes. Annu. Rev. Biophys. Biomol. Struct. 22:1993;145-171.
4. Park P.J., Sung W. Statistical mechanics of membrane protein conformation: a homopolyer model. Phys. Rev. Lett. 80:1998;5687-5690.
5. Belochorcová K., Davis J.H., Woolf T.B., Roux B. Structure and dynamics of an amphiphilic peptide in a lipid bilayer: a molecular dynamics study. Biophys. J. 73:1997;3039-3055.
6. Milik M., Skolnick J. Spontaneous insertion of polypeptide chains in membranes: a Monte Carlo model. Proc. Natl. Acad. Sci. USA. 89:1992;9391-9395.
7. Wang J., Pullman A. Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase? Biochim. Biophys. Acta. 1070:1991;493-496.
8. Baumgärtner A. Insertion and hairpin formation of membrane proteins: a Monte Carlo study. Biophys. J. 71:1996;1248-1255.
9. Forrest L.R., De Grado W.F., Dieckmann G.R., Sansom M.S.P. Two models of the influenza A M2 channel domain: verification by comparison. Folding Des. 3:1998;443-448.
10. Ben-Tal N., Honig B., Peitzsch R.M., Denisov G., McLaughlin S. Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys. J. 71:1996;561-575.
11. Le Coutre J., Narasimhan L.R., Kumar C., Patel N., Kaback R. The lipid bilayer determines helical tilt angle and function in lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA. 94:1997;10167-10171.
12. Kovacs F.A., Denny J.K., Song Z., Quine J.R., Cross T.A. Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property. J. Mol. Biol. 295:2000;117-125.
13. Opella S.J., Marassi F.M., Gesell J.J., Valente A.P., Kim Y., Oblatt-Montal M., Montal M. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat Struct. Biol. 6:1999;374-379.
14. Booth P.J. Folding α-helical membrane proteins: kinetic studies on bacteriorhodopsin. Folding Des. 2:1997;R85-R92.
15. Rice D., Oldfield E. Deuterium nuclear magnetic resonance studies of the interaction between dimyristoylphosphatidylcholine and gramicidin A. Biochemistry. 18:1979;3272-3279.
16. Jähnig F., Vogel H., Best L. Unifying description of the effect of membrane proteins on lipid order. Verification for the melittin/dimyristoylphosphatidylcholine system. Biochemistry. 21:1982;6790-6798.
17. Hoffmann W., Pink D., Restall C., Chapman D. Intrinsic molecules in fluid phospholipid bilayers: fluorescence probe studies. Eur. J. Biochem. 114:1981;585-589.
18. Meier P., Sachse J.-H., Brophy P.J., Marsh D., Kothe G. Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: a deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein. Proc. Natl. Acad. Sci. USA. 84:1987;3704-3708.
19. 2H NMR and ESR study using designed tranmembrane α-helical peptides and gramicidin A. Biochemistry. 37:1998;9333-9345.
20. Prosser R.S., Davis J.H. Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin. Biophys. J. 66:1994;1429-1440.
21. White S.H., Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28:1999;319-365.
22. VonHeijne G. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:1994;167-192.
23. 13C-MAS NMR spectroscopy. Biochim. Biophys. Acta. 1463:2000;151-161.
24. Grosberg A.Y., Khokhlov A.R. Statistical physics of macromolecules. 1994;American Institute of Physics Press, New York.
25. Seelig J. Deuterium magnetic resonance: theory and application to lipid membranes. Q. Rev. Biophys. 10:1977;353-418.
26. 2H-NMR. Biochim. Biophys. Acta. 600:1980;245-262.
27. Roseman M.A. Hydrophobicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds. J. Mol. Biol. 200:1988;513-522.
28. Knowles P.F., Marsh D. Magnetic resonance of membranes. Biochem. J. 274:1991;625-641.
29. Datta D.B. A comprehensive introduction to membrane biochemistry. 1987;Floral Publishing, Madison.