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Kühlbrandt, W., Wang, D.N., Fujiyoshi, Y. (1994) Atomic model of plant light-harvesting complex. Nature
367:614–621.
Kurisu, G., Zhang, H., Smith, J.L., Cramer, W.A. (2003) Structure of the cytochrome b 6 f complex of oxygenic
photosynthesis: tuning the cavity. Science 302:1009–1014.
Landau, E.M., Rosenbusch, J.P. (1996) Lipid cubic phases: A novel concept for the crystallization of membrane proteins.
Proc. Natl. Acad. Sci. USA 93:14532–14535.
Lange, C., Nett, J.H., Trumpower, B.L., Hunte, C. (2001) Specific roles of protein-phospholipid interactions in the yeast
cytochrome bc 1 complex structure. EMBO J. 20:6591–6600.
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Biochim. Biophys. Acta 1101:13–22.
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1612:1–40.
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Lee, A.G. (2011b) How to understand lipid-protein interactions in biological membranes, in: Yeagle, P., ed., Structure of
Biological Membranes. 3rd edition, Taylor and Francis, Boca Raton, Florida, USA, pp. 273–313.
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bacteriorhodopsin in lipid nanodiscs. Biophys. J. 109:1899–1906.
Lehnert, U., Réat, V., Weik, M., Zaccai, G., Pfister, C. (1998) Thermal motions in bacteriorhodopsin at different
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Biophys. J. 75:1945–1952.
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Biol. 356:600–612.
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MacKenzie, K.R., Prestegard, J.H., Engelman, D.M. (1997) A transmembrane helix dimer: structure and implications.
Science 276:131–133.
Marčelja, S. (1974) Chain ordering in liquid crystals. II. Structure of bilayer membranes. Biochim. Biophys. Acta
367:165–176.
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Martfeld, A.N., Rajagopalan, V., Greathouse, D.V., Koeppe, R.E., II (2015) Dynamic regulation of lipid-protein
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McMorran, L.M., Brockwell, D.J., Radford, S.E. (2014) Mechanistic studies of the biogenesis and folding of outer
membrane proteins in vitro and in vivo: What have we learned to date? Arch. Biochem. Biophys. 564:265–280.
Merino, J.M., Møller, J.V., Gutiérrez-Merino, C. (1994) Thermal unfolding of monomeric Ca
2+ ,Mg
2+ -ATPase from
sarcoplasmic reticulum of rabbit skeletal muscle. FEBS Lett. 343:155–159.
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Mitsuoka, K., Hirai, T., Miyazawa, A., Kidera, A., Kimura, Y., Fujiyoshi, Y. (1999) The structure of bacteriorhodopsin
at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J. Mol. Biol.
286:861–882.
Møller, J.V., Lind, K.E., Andersen, J.P. (1980) Enzyme kinetics and substrate stabilization of detergent-solubilized and
membraneous (Ca
2+ + Mg
2+ )-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions.
J. Biol. Chem. 255:1912–1920.
Møller, J.V., Olesen, C., Winther, A.M.L., Nissen, P. (2010) The sarcoplasmic Ca
2+ -ATPase: design of a perfect chemiosmotic pump. Q. Rev. Biophys. 43:501–566.
Morales-Perez, C.L., Noviello, C.M., Hibbs, R.E. (2016) X-ray structure of the human α4β2 nicotinic receptor. Nature
538:411–415.
Nemecz, Á., Prévost, M.S., Menny, A., Corringer, P.-J. (2016) Emerging molecular mechanisms of signal transduction in
pentameric ligand-gated ion channels. Neuron 90:452–470.
Neutze, R., Pebay-Peyroula, E., Edman, K., Royant, A., Navarro, J., Landau, E.M. (2002) Bacteriorhodopsin: a highresolution structural view of vectorial proton transport. Biochim. Biophys. Acta 1565:144–167.
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1 Membrane Proteins and Their Natural Environment
Kühlbrandt, W. (2015) Structure and function of mitochondrial membrane protein complexes. BMC Biol. 13:89.
Kühlbrandt, W., Wang, D.N., Fujiyoshi, Y. (1994) Atomic model of plant light-harvesting complex. Nature
367:614–621.
Kurisu, G., Zhang, H., Smith, J.L., Cramer, W.A. (2003) Structure of the cytochrome b 6 f complex of oxygenic
photosynthesis: tuning the cavity. Science 302:1009–1014.
Landau, E.M., Rosenbusch, J.P. (1996) Lipid cubic phases: A novel concept for the crystallization of membrane proteins.
Proc. Natl. Acad. Sci. USA 93:14532–14535.
Lange, C., Nett, J.H., Trumpower, B.L., Hunte, C. (2001) Specific roles of protein-phospholipid interactions in the yeast
cytochrome bc 1 complex structure. EMBO J. 20:6591–6600.
Lanyi, J.K. (2004) Bacteriorhodopsin. Annu. Rev. Physiol. 66:665–688.
Lanyi, J.K., Luecke, H. (2001) Bacteriorhodopsin. Curr. Opin. Struct. Biol. 11:415–419.
Lavergne, J., Bouchaud, J.-P., Joliot, P. (1992) Plastoquinone compartmentation in chloroplasts. II. Theoretical aspects.
Biochim. Biophys. Acta 1101:13–22.
Lee, A.G. (2003) Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta
1612:1–40.
Lee, A.G. (2004) How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 1666:62–87.
Lee, A.G. (2011a) Biological membranes: the importance of molecular detail. Trends Biochem. Sci. 36:493–500.
Lee, A.G. (2011b) How to understand lipid-protein interactions in biological membranes, in: Yeagle, P., ed., Structure of
Biological Membranes. 3rd edition, Taylor and Francis, Boca Raton, Florida, USA, pp. 273–313.
Lee, T.-Y., Yeh, V., Chuang, J., Chan, J.C.C., Chu, L.-K., Yu, T.-Y. (2015) Tuning the photocycle kinetics of
bacteriorhodopsin in lipid nanodiscs. Biophys. J. 109:1899–1906.
Lehnert, U., Réat, V., Weik, M., Zaccai, G., Pfister, C. (1998) Thermal motions in bacteriorhodopsin at different
hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes.
Biophys. J. 75:1945–1952.
Li, E., You, M., Hristova, K. (2006) FGFR3 dimer stabilization due to a single amino acid pathogenic mutation. J. Mol.
Biol. 356:600–612.
Locher, K.P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J.P., Moras, D. (1998) Transmembrane
signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal
allosteric changes. Cell 95:771–778.
Lundbaek, J.A., Koeppe, R.E., 2nd., Andersen, O.S. (2010) Amphiphile regulation of ion channel function by changes in
the bilayer spring constant. Proc. Natl. Acad. Sci. USA 107:1527–1530.
MacKenzie, K.R., Prestegard, J.H., Engelman, D.M. (1997) A transmembrane helix dimer: structure and implications.
Science 276:131–133.
Marčelja, S. (1974) Chain ordering in liquid crystals. II. Structure of bilayer membranes. Biochim. Biophys. Acta
367:165–176.
Marsh, D. (1996) Lateral pressure in membranes. Biochim. Biophys. Acta 1286:183–223.
Marsh, D. (2008) Protein modulation of lipids, and vice-versa, in membranes. Biochim. Biophys. Acta 1778:1545–1575.
Martfeld, A.N., Rajagopalan, V., Greathouse, D.V., Koeppe, R.E., II (2015) Dynamic regulation of lipid-protein
interactions. Biochim. Biophys. Acta 1848:1849–1859.
McMorran, L.M., Brockwell, D.J., Radford, S.E. (2014) Mechanistic studies of the biogenesis and folding of outer
membrane proteins in vitro and in vivo: What have we learned to date? Arch. Biochem. Biophys. 564:265–280.
Merino, J.M., Møller, J.V., Gutiérrez-Merino, C. (1994) Thermal unfolding of monomeric Ca
2+ ,Mg
2+ -ATPase from
sarcoplasmic reticulum of rabbit skeletal muscle. FEBS Lett. 343:155–159.
Miller, P.S., Aricescu, A.R. (2014) Crystal structure of a human GABA A receptor. Nature 512:270–275.
Mitsuoka, K., Hirai, T., Miyazawa, A., Kidera, A., Kimura, Y., Fujiyoshi, Y. (1999) The structure of bacteriorhodopsin
at 3.0 Å resolution based on electron crystallography: implication of the charge distribution. J. Mol. Biol.
286:861–882.
Møller, J.V., Lind, K.E., Andersen, J.P. (1980) Enzyme kinetics and substrate stabilization of detergent-solubilized and
membraneous (Ca
2+ + Mg
2+ )-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions.
J. Biol. Chem. 255:1912–1920.
Møller, J.V., Olesen, C., Winther, A.M.L., Nissen, P. (2010) The sarcoplasmic Ca
2+ -ATPase: design of a perfect chemiosmotic pump. Q. Rev. Biophys. 43:501–566.
Morales-Perez, C.L., Noviello, C.M., Hibbs, R.E. (2016) X-ray structure of the human α4β2 nicotinic receptor. Nature
538:411–415.
Nemecz, Á., Prévost, M.S., Menny, A., Corringer, P.-J. (2016) Emerging molecular mechanisms of signal transduction in
pentameric ligand-gated ion channels. Neuron 90:452–470.
Neutze, R., Pebay-Peyroula, E., Edman, K., Royant, A., Navarro, J., Landau, E.M. (2002) Bacteriorhodopsin: a highresolution structural view of vectorial proton transport. Biochim. Biophys. Acta 1565:144–167.
54
1 Membrane Proteins and Their Natural Environment