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. 1987 Jun;84(11):3704–3708. doi: 10.1073/pnas.84.11.3704

Integral membrane proteins significantly decrease the molecular motion in lipid bilayers: a deuteron NMR relaxation study of membranes containing myelin proteolipid apoprotein.

P Meier, J H Sachse, P J Brophy, D Marsh, G Kothe
PMCID: PMC304944  PMID: 3473478

Abstract

The influence of the myelin proteolipid apoprotein on lipid chain order and dynamics was studied by 2H NMR of membranes reconstituted with specifically deuterated dimyristoyl phosphatidylcholines. Quadrupolar echo and saturation recovery experiments were fitted by numerical solution of the stochastic Liouville equation, using a model that includes both inter- and intramolecular motions [Meier, P., Ohmes, E. & Kothe, G. (1986) J. Chem. Phys. 85, 3598-3614]. Combined simulations of both the relaxation times and the quadrupolar echo line shapes as a function of pulse spacing allowed unambiguous assignment of the various motional modes and a consistent interpretation of data from lipids labeled on the C-6, C-13, and C-14 positions of the sn-2 chain. In the fluid phase, the protein has little influence on either the chain order or the population of gauche rotational isomers but strongly retards the chain dynamics. For 1-myristoyl-2-[13-2H2] myristoyl-sn-glycero-3-phosphocholine at 35 degrees C, the correlation time for chain fluctuation increases from 20 nsec to 650 nsec and for chain rotation from 10 nsec to 180 nsec, and the gauche isomer lifetime increases from 0.15 nsec to 1.75 nsec, on going from the lipid alone to a recombinant of protein/lipid ratio 0.073 mol/mol. The results are essentially consistent with spin-label ESR studies on the same system [Brophy, P.J., Horvath, L.I. & Marsh, D. (1984) Biochemistry 23, 860-865], when allowance is made for the different time scales of the two spectroscopies.

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Selected References

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  1. Benjamins J. A., Miller S. L., Morell P. Metabolic relationships between myelin subfractions: entry of galactolipids and phospholipids. J Neurochem. 1976 Aug;27(2):565–570. doi: 10.1111/j.1471-4159.1976.tb12283.x. [DOI] [PubMed] [Google Scholar]
  2. Brophy J. Association of proteolipid apoproteins from bovine myelin with phospholipid in bilayer vesicles. FEBS Lett. 1977 Dec 1;84(1):92–96. doi: 10.1016/0014-5793(77)81064-8. [DOI] [PubMed] [Google Scholar]
  3. Brophy P. J., Horváth L. I., Marsh D. Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance. Biochemistry. 1984 Feb 28;23(5):860–865. doi: 10.1021/bi00300a011. [DOI] [PubMed] [Google Scholar]
  4. DasGupta S. K., Rice D. M., Griffin R. G. Synthesis of isotopically labeled saturated fatty acids. J Lipid Res. 1982 Jan;23(1):197–200. [PubMed] [Google Scholar]
  5. Eibl H., Lands W. E. A new, sensitive determination of phosphate. Anal Biochem. 1969 Jul;30(1):51–57. doi: 10.1016/0003-2697(69)90372-8. [DOI] [PubMed] [Google Scholar]
  6. Jost P., Griffith O. H., Capaldi R. A., Vanderkooi G. Identification and extent of fluid bilayer regions in membranous cytochrome oxidase. Biochim Biophys Acta. 1973 Jun 22;311(2):141–152. doi: 10.1016/0005-2736(73)90261-7. [DOI] [PubMed] [Google Scholar]
  7. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  8. Mason J. T., Broccoli A. V., Huang C. A method for the synthesis of isomerically pure saturated mixed-chain phosphatidylcholines. Anal Biochem. 1981 May 1;113(1):96–101. doi: 10.1016/0003-2697(81)90049-x. [DOI] [PubMed] [Google Scholar]
  9. Pates R. D., Marsh D. Lipid mobility and order in bovine rod outer segment disk membranes. A spin-label study of lipid-protein interactions. Biochemistry. 1987 Jan 13;26(1):29–39. doi: 10.1021/bi00375a005. [DOI] [PubMed] [Google Scholar]
  10. Rice D. M., Meadows M. D., Scheinman A. O., Goñi F. M., Gómez-Fernández J. C., Moscarello M. A., Chapman D., Oldfield E. Protein-lipid interactions. A nuclear magnetic resonance study of sarcoplasmic reticulum Ca2,Mg2+-ATPase, lipophilin, and proteolipid apoprotein-lecithin systems and a comparison with the effects of cholesterol. Biochemistry. 1979 Dec 25;18(26):5893–5903. [PubMed] [Google Scholar]
  11. Smith R., Cook J., Dickens P. A. Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents. J Neurochem. 1984 Feb;42(2):306–313. doi: 10.1111/j.1471-4159.1984.tb02679.x. [DOI] [PubMed] [Google Scholar]

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