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              Membrane Structure                                                                          367

              (grown on a medium supplemented with specifically  SEE ALSO THE FOLLOWING ARTICLES
              deuterated or perdeuterated fatty acids), cardiolipin- or
              glycerol-auxotroph Escherichia coli (grown in tissue-  BIOENERGETICS • ELECTRON TRANSFER REACTIONS •
              culture medium containing selectively deuterated fatty  ENERGY TRANSFER,INTRAMOLECULAR • ION KINETICS
              acids or phosphatidyl glycerol), and mouse fibrob-  AND ENERGETICS • ION TRANSPORT ACROSS BIO-
              last L-M cells (grown in tissue-culture medium con-  LOGICAL MEMBRANES • LIPOPROTEIN/CHOLESTEROL
              taining selectively deuterated choline or ethanolamine).  METABOLISM • PROTEIN SYNTHESIS
              The membranes of these systems showed very simi-
              lar fatty acid and headgroup motion, ordering, and ori-
              entation as the membranes formed from the extracted  BIBLIOGRAPHY
              lipids without protein. No long-lived lipid–protein com-
              plexes were observed for neutral or negatively charged  Davis, J. H. (1983). “The description of membrane lipid conformation,
              lipids.                                            order and dynamics by 2H-NMR,” Biochim. Biophys. Acta 737, 117–
                                                                 71.
                                                                Devaux, P. F., and Seigneuret, M. (1985). “Specificity of lipid-protein in-
                                                                 teractions as determined by spectroscopic techniques,” Biochim. Bio-
              VII. CONCLUDING REMARKS
                                                                 phys. Acta 822, 63–125.
                                                                Divecha, N., Clarke, J. H., Roefs, M., Halstead, J. R., and D’Santos, C.
              Solid-state NMR measurements have shown that func-  (2000). “Nuclear inositides: inconsistent consistencies,” Cell. Molec.
              tional biological membranes are in the liquid crystal-  Life Sci. 57, 379–393.
              line state and that structural features of lipids in the crys-  Koynova, R., and Caffrey, M. (1998). “Phases and phase transitions of
                                                                 the phosphatidylcholines,” Biochim. Biophys. Acta 1376, 91–145.
              talline phase are essentially carried over into the liquid
                                                                Mitchell, D. C., Gawrisch, K., Litman, B. J., and Salem, N., Jr. (1998).
              crystalline state. An order parameter profile comparable  “Why is docosahexaenoic acid essential for nervous system function?”
              for the most diverse membranes has been established.  Biochem. Soc. Trans. 26, 365–370.
              The absolute values of order parameters may, however,  Muniz, M., and Riezman, H. (2000). “Intracellular transport of GPI-
              vary as much as a factor of two as a consequence of the  anchored proteins,” Embo J. 19, 10–15.
                                                                Op den Kamp, J. A. F., Roelofsen, B., and van Deenen, L. L. M. (1985).
              large variation in lipid composition encountered in bio-
                                                                 “Structural dynamic aspects of phsophatidylcholine in the human ery-
              logical membranes. Membrane ordering decreases upon  throcyte membrane,” Trends Biochem. Sci. 10, 320–323.
              increasing the temperature, introducing one or several  Seelig,J.(1977).“Deuteriummagneticresonance:theoryandapplication
              cis-double bonds into a saturated fatty acyl chain, or  to lipid membranes,” Q. Rev. Biophys. 10, 353–418.
                                                                                             31
                                                                               2
              upon adding an amphiphilic guest molecule. In contrast,  Seelig, J. (1978). “[ H]Hydrogen and [ P]phosphorus nuclear-
                                                                 magnetic-resonance and neutron-diffraction studies of membranes,”
              it increases up to twofold upon addition of 50% choles-
                                                                 Biochem. Soc. Trans. 6, 40–42.
              terol. Transmembrane proteins barely influence the lipid  Seelig, J. (1978). “ P nuclear magnetic resonance and the headgroup
                                                                            31
              order, as they perfectly match the lipid bilayer proper-  structure of phospholipids in membranes,” Biochim. Biophys. Acta
              ties. Due to the action of enzymes (e.g., phospholipases)  515, 105–140.
              the lipid packing density and hence the membrane order  Seelig, J. (1993). “Phospholipid headgroups as sensors of electric
                                                                 charge,” In “New Developments in Lipid–Protein Interactions and
              may vary with time and, in turn, may modulate the func-
                                                                 Receptor and Function” (K. W. A. Wirtz, ed.), Plenum Press, New
              tion of membrane proteins. A conformational change in  York.
              a membrane protein may further be induced by an out-  Seelig, J. (1995). “Metal ion interactions with lipids,” In “Handbook of
              of-plane rotation of the phospholipid headgroup dipole  Metal–Ligand Interactions in Biological Fluids: Bioinorganic Chem-
              resulting in the development of a storage electric field  istry,” Marcel Dekker, New York.
                                                                Seelig, J., and Browning, J. L. (1978). “General features of phospholipid
              across the membrane, which changes the protein struc-
                                                                 conformation in membranes,” FEBS Lett. 92, 41–44.
              ture. NMR measurements have further demonstrated that  Seelig, J., and Macdonald, P. M. (1987). “Phospholipids and proteins
                                                                                   2
              a fast exchange of lipid molecules is observed between  in biological membranes: H-NMR as a method to study structure,
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              lipid phase. At present, no physical–chemical evidence  Seelig, J., and Seelig, A. (1980). “Lipid conformation in model mem-
                                                                 branes and biological membranes,” Q. Rev. Biophys. 13, 19–61.
              for the formation of domains or microdomains with life-  Seelig, J., Seelig, A., and Tamm, L. (1982). “Nuclear magnetic resonance
              times >10 −4  s has been obtained under physiological  and lipid–protein interactions,” In “Lipid-Protein Interactions” (P. Jost
              conditions.                                        and O. H. Griffith, eds.), pp. 127–148, John Wiley & Sons, New York.
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