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. 1978 Oct;75(10):4657–4660. doi: 10.1073/pnas.75.10.4657

Deuterium nuclear magnetic resonance investigation of the effects of proteins and polypeptides on hydrocarbon chain order in model membrane systems

E Oldfield *, R Gilmore *, M Glaser *, H S Gutowsky *, J C Hshung †, S Y Kang *, Tsoo E King †, M Meadows *, D Rice *
PMCID: PMC336175  PMID: 16592570

Abstract

Deuterium Fourier-transform nuclear magnetic resonance spectra have been obtained of 1-myristoyl 2-(14,14,14-trideutero)myristoyl phosphatidylcholine bilayers at 34.1 MHz by using the quadrupole echo pulse technique. Thereby, we have investigated the effects upon the deuterated dimyristoyl phosphatidylcholine bilayers of the following proteins and polypeptides: gramicidin A, bacteriophage f1 coat protein, beef brain myelin proteolipid apoprotein, cytochrome b5, and cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1). Above Tc, the transition temperature between the gel and liquid crystal phases, the quadrupole splitting of the deuterium-labeled methyl group is reduced or collapsed in the presence of protein or polypeptide. No evidence has been found for ordered “boundary lipid.” Below Tc, the spectra show that the hydrocarbon chains are prevented from crystallizing by the protein (or polypeptide) incorporated in the membrane. Similar disordering effects above Tc are also seen when an unsaturated lipid, 1-(16,16,16-trideutero)palmitoyl 2-palmitoleyl phosphatidylcholine is complexed with cytochrome oxidase.

Keywords: gramicidin A, bacteriophage f1 coat protein, myelin proteolipid apoprotein, cytochrome b5, cytochrome oxidase

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Chapman D., Cornell B. A., Ellasz A. W., Perry A. Interactions of helical polypepetide segments which span the hydrocarbon region of lipid bilayers. Studies of the gramicidin A lipid-water system. J Mol Biol. 1977 Jul 5;113(3):517–538. doi: 10.1016/0022-2836(77)90236-4. [DOI] [PubMed] [Google Scholar]
  2. Curatolo W., Sakura J. D., Small D. M., Shipley G. G. Protein-lipid interactions: recombinants of the proteolipid apoprotein of myelin with dimyristoyllecithin. Biochemistry. 1977 May 31;16(11):2313–2319. doi: 10.1021/bi00630a001. [DOI] [PubMed] [Google Scholar]
  3. Dahlquist F. W., Muchmore D. C., Davis J. H., Bloom M. Deuterium magnetic resonance studies of the interaction of lipids with membrane proteins. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5435–5439. doi: 10.1073/pnas.74.12.5435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dehlinger P. J., Jost P. C., Griffith O. H. Lipid binding to the amphipathic membrane protein cytochrome b5. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2280–2284. doi: 10.1073/pnas.71.6.2280. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dufourcq J., Faucon J. F. Intrinsic fluorescence study of lipid-protein interactions in membrane models. Binding of melittin, an amphipathic peptide, to phospholipid vesicles. Biochim Biophys Acta. 1977 May 16;467(1):1–11. doi: 10.1016/0005-2736(77)90236-x. [DOI] [PubMed] [Google Scholar]
  6. Folch-Pi J., Stoffyn P. J. Proteolipids from membrane systems. Ann N Y Acad Sci. 1972 Jun 20;195:86–107. [PubMed] [Google Scholar]
  7. Grant C. W., McConnell H. M. Glycophorin in lipid bilayers. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4653–4657. doi: 10.1073/pnas.71.12.4653. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gupta C. M., Radhakrishnan R., Khorana H. G. Glycerophospholipid synthesis: improved general method and new analogs containing photoactivable groups. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4315–4319. doi: 10.1073/pnas.74.10.4315. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Haberkorn R. A., Griffin R. G., Meadows M. D., Oldfield E. Deuterium nuclear magnetic resonance investigation of the dipalmitoyl lecithin-cholesterol-water system. J Am Chem Soc. 1977 Oct 26;99(22):7353–7355. doi: 10.1021/ja00464a043. [DOI] [PubMed] [Google Scholar]
  10. Jost P. C., Griffith O. H., Capaldi R. A., Vanderkooi G. Evidence for boundary lipid in membranes. Proc Natl Acad Sci U S A. 1973 Feb;70(2):480–484. doi: 10.1073/pnas.70.2.480. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ladbrooke B. D., Williams R. M., Chapman D. Studies on lecithin-cholesterol-water interactions by differential scanning calorimetry and X-ray diffraction. Biochim Biophys Acta. 1968 Apr 29;150(3):333–340. doi: 10.1016/0005-2736(68)90132-6. [DOI] [PubMed] [Google Scholar]
  12. Makino S., Woolford J. L., Jr, Tanford C., Webster R. E. Interaction of deoxycholate and of detergents with the coat protein of bacteriophage f1. J Biol Chem. 1975 Jun 10;250(11):4327–4332. [PubMed] [Google Scholar]
  13. Oldfield E., Chapman D., Derbyshire W. Deuteron resonance: A novel approach to the study of hydrocarbon chain mobility in membrane systems. FEBS Lett. 1971 Aug 1;16(2):102–104. doi: 10.1016/0014-5793(71)80343-5. [DOI] [PubMed] [Google Scholar]
  14. Oldfield E., Chapman D., Derbyshire W. Lipid mobility in Acholeplasma membranes using deuteron magnetic resonance. Chem Phys Lipids. 1972 Jul;9(1):69–81. doi: 10.1016/0009-3084(72)90034-5. [DOI] [PubMed] [Google Scholar]
  15. Oldfield E., Meadows M., Glaser M. Deuterium magnetic resonance spectroscopy of isotopically labeled mammalian cells. J Biol Chem. 1976 Oct 10;251(19):6147–6149. [PubMed] [Google Scholar]
  16. Oldfield E., Meadows M., Rice D., Jacobs R. Spectroscopic studies of specifically deuterium labeled membrane systems. Nuclear magnetic resonance investigation of the effects of cholesterol in model systems. Biochemistry. 1978 Jul 11;17(14):2727–2740. doi: 10.1021/bi00607a006. [DOI] [PubMed] [Google Scholar]
  17. Ozols J. Cytochrome b5 from microsomal membranes of equine, bovine, and porcine livers. Isolation and properties of preparations containing the membranous segment. Biochemistry. 1974 Jan 29;13(3):426–434. doi: 10.1021/bi00700a005. [DOI] [PubMed] [Google Scholar]
  18. Seelig A., Seelig J. Effect of a single cis double bond on the structures of a phospholipid bilayer. Biochemistry. 1977 Jan 11;16(1):45–50. doi: 10.1021/bi00620a008. [DOI] [PubMed] [Google Scholar]
  19. Seelig J. Deuterium magnetic resonance: theory and application to lipid membranes. Q Rev Biophys. 1977 Aug;10(3):353–418. doi: 10.1017/s0033583500002948. [DOI] [PubMed] [Google Scholar]
  20. Tardieu A., Luzzati V., Reman F. C. Structure and polymorphism of the hydrocarbon chains of lipids: a study of lecithin-water phases. J Mol Biol. 1973 Apr 25;75(4):711–733. doi: 10.1016/0022-2836(73)90303-3. [DOI] [PubMed] [Google Scholar]
  21. Warren G. B., Toon P. A., Birdsall N. J., Lee A. G., Metcalfe J. C. Reconstitution of a calcium pump using defined membrane components. Proc Natl Acad Sci U S A. 1974 Mar;71(3):622–626. doi: 10.1073/pnas.71.3.622. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Wickner W. Asymmetric orientation of phage M13 coat protein in Escherichia coli cytoplasmic membranes and in synthetic lipid vesicles. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1159–1163. doi: 10.1073/pnas.73.4.1159. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yu C., Yu L., King T. E. Studies on cytochrome oxidase. Interactions of the cytochrome oxidase protein with phospholipids and cytochrome c. J Biol Chem. 1975 Feb 25;250(4):1383–1392. [PubMed] [Google Scholar]

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