Qin, L., Sharpe, M.A., Garavito, R.M., Ferguson-Miller, S. (2007) Conserved lipid-binding sites in membrane proteins: a
focus on cytochrome c oxidase. Curr. Opin. Struct. Biol. 17:444–450.
Qin, X., Suga, M., Kuang, T., Shen, J.R. (2015) Photosynthesis. Structural basis for energy transfer pathways in the plant
PSI-LHCI supercomplex. Science 348:989–995.
Reynolds, J.A., Gilbert, D.B., Tanford, C. (1974) Empirical correlation between hydrophobic free energy and aqueous
cavity surface area. Proc. Natl. Acad. Sci. USA 71:2925–2927.
Rouse, S.L., Sansom, M.S.P. (2015) Interactions of lipids and detergents with a viral ion channel protein: Molecular
dynamics simulation studies. J. Phys. Chem. B 119:764–772.
Rummel, G., Hardmeyer, A., Widmer, C., Chiu, M.L., Nollert, P., Locher, K.P., Pedruzzi, I.I., Landau, E.M.,
Rosenbusch, J.P. (1998) Lipidic cubic phases: new matrices for the three-dimensional crystallization of membrane
proteins. J. Struct. Biol. 121:82–91.
Sauguet, L., Poitevin, F., Murail, S., Van Renterghem, C., Moraga-Cid, G., Malherbe, L., Thompson, A.W., Koehl, P.,
Corringer, P.-J., Baaden, M., Delarue, M. (2013) Structural basis for ion permeation mechanism in pentameric ligandgated ion channels. EMBO J. 32:728–741.
Sauguet, L., Shahsavar, A., Poitevin, F., Huon, C., Menny, A., Nemecz, À., Haouz, A., Changeux, J.-P., Corringer, P.-J.,
Delarue, M. (2014) Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation.
Proc. Natl. Acad. Sci. USA 111:966–971.
Saxton, M.J. (1989) Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient. Biophys. J.
56:615–622.
Schirmer, T. (1998) General and specific porins from bacterial outer membranes. J. Struct. Biol. 121:101–109.
Shinzawa-Itoh, K., Aoyama, H., Muramoto, K., Terada, H., Kurauchi, T., Tadehara, Y., Yamasaki, A., Sugimura, T.,
Kurono, S., Tsujimoto, K., Mizushima, T., Yamashita, E., Tsukihara, T., Yoshikawa, S. (2007) Structures and
physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase. EMBO J. 26:1713–1725.
Sine, S.M. (2012) End-plate acetylcholine receptor: Structure, mechanism, pharmacology, and disease. Physiol. Rev.
92:1189–1234.
Singer, S.J., Nicolson, G.L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175:720–731.
Smit, A.B., Syed, N.I., Schaap, D., van Minnen, J., Klumpermank, J., Kits, K.S., Lodder, H., van der Schors, R.C., van
Elk, R., Sorgedrager, B., Brejc, K., Sixma, T.K., Geraerts, W.P.M. (2001) A glia-derived acetylcholine-binding
protein that modulates synaptic transmission. Nature 411:261–268.
Smith, A.W. (2012) Lipid-protein interactions in biological membranes: A dynamic perspective. Biochim. Biophys. Acta
1818:172–177.
Song, L., Hobaugh, M.R., Shustak, C., Cheley, S., Bayley, H., Gouaux, J.E. (1996) Structure of α-hemolysin, a
heptameric transmembrane pore. Science 274:1859–1866.
Sonntag, Y., Musgaard, M., Olesen, C., Schiøtt, B., Møller, J.V., Nissen, P., Thøgersen, L. (2011) Mutual adaptation of a
membrane protein and its lipid bilayer during conformational changes. Nat. Commun. 2:304.
Spurny, R., Ramerstorfer, J., Price, K., Brams, M., Ernst, M., Nury, H., Verheije, M., Legrand, P., Bertrand, D., Bertrand,
S., Dougherty, D.A., de Esch, I.J.P., Corringer, P.-J., Sieghart, W., Lummis, S.C.R., Ulens, C. (2012) Pentameric
ligand-gated ion channel ELIC is activated by GABA and modulated by benzodiazepines. Proc. Natl. Acad. Sci. USA
109:E3028-E3034.
Starling, A.P., Dalton, K.A., East, J.M., Oliver, S., Lee, A.G. (1996) Effects of phosphatidylethanolamines on the activity
of the Ca
2+ -ATPase of sarcoplasmic reticulum. Biochem. J. 320:309–314.
Stowell, M.H.B., McPhillips, T.M., Rees, D.C., Soltis, S.M., Abresch, E., Feher, G. (1997) Light-induced structural
changes in photosynthetic reaction center: implication for mechanism of electron-proton transfer. Science
276:812–816.
Stroebel, D., Choquet, Y., Popot, J.-L., Picot, D. (2003) An atypical haem in the cytochrome b 6 f complex. Nature
426:413–418.
Svensson-Ek, M., Abramson, J., Larsson, G., Tornroth, S., Brzezinski, P., Iwata, S. (2002) The X-ray crystal structures of
wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321:329–339.
Sweadner, K.J. (2017) An ion-transport enzyme that rocks. Nature 545:162–164.
Taly, A., Hénin, J., Changeux, J.-P., Cecchini, M. (2014) Allosteric regulation of pentameric ligand-gated ion channels:
an emerging mechanistic perspective. Channels 8:350–360.
Tanford, C. (1980) The Hydrophobic Effect: Formation of Micelles and Biological Membranes. 2nd ed. John Wiley &
Sons, New York, 233 p.
Teng, J., Loukin, S.H., Anishkin, A., Kung, C. (2015) The force-from-lipid (FFL) principle of mechanosensitivity, at
large and in elements. Pflügers Arch. 467:27–37.
Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic
reticulum at 2.6 Å resolution. Nature 405:647–655.
Toyoshima, C., Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium.
Nature 418:605–611.
56
1 Membrane Proteins and Their Natural Environment
focus on cytochrome c oxidase. Curr. Opin. Struct. Biol. 17:444–450.
Qin, X., Suga, M., Kuang, T., Shen, J.R. (2015) Photosynthesis. Structural basis for energy transfer pathways in the plant
PSI-LHCI supercomplex. Science 348:989–995.
Reynolds, J.A., Gilbert, D.B., Tanford, C. (1974) Empirical correlation between hydrophobic free energy and aqueous
cavity surface area. Proc. Natl. Acad. Sci. USA 71:2925–2927.
Rouse, S.L., Sansom, M.S.P. (2015) Interactions of lipids and detergents with a viral ion channel protein: Molecular
dynamics simulation studies. J. Phys. Chem. B 119:764–772.
Rummel, G., Hardmeyer, A., Widmer, C., Chiu, M.L., Nollert, P., Locher, K.P., Pedruzzi, I.I., Landau, E.M.,
Rosenbusch, J.P. (1998) Lipidic cubic phases: new matrices for the three-dimensional crystallization of membrane
proteins. J. Struct. Biol. 121:82–91.
Sauguet, L., Poitevin, F., Murail, S., Van Renterghem, C., Moraga-Cid, G., Malherbe, L., Thompson, A.W., Koehl, P.,
Corringer, P.-J., Baaden, M., Delarue, M. (2013) Structural basis for ion permeation mechanism in pentameric ligandgated ion channels. EMBO J. 32:728–741.
Sauguet, L., Shahsavar, A., Poitevin, F., Huon, C., Menny, A., Nemecz, À., Haouz, A., Changeux, J.-P., Corringer, P.-J.,
Delarue, M. (2014) Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation.
Proc. Natl. Acad. Sci. USA 111:966–971.
Saxton, M.J. (1989) Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient. Biophys. J.
56:615–622.
Schirmer, T. (1998) General and specific porins from bacterial outer membranes. J. Struct. Biol. 121:101–109.
Shinzawa-Itoh, K., Aoyama, H., Muramoto, K., Terada, H., Kurauchi, T., Tadehara, Y., Yamasaki, A., Sugimura, T.,
Kurono, S., Tsujimoto, K., Mizushima, T., Yamashita, E., Tsukihara, T., Yoshikawa, S. (2007) Structures and
physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase. EMBO J. 26:1713–1725.
Sine, S.M. (2012) End-plate acetylcholine receptor: Structure, mechanism, pharmacology, and disease. Physiol. Rev.
92:1189–1234.
Singer, S.J., Nicolson, G.L. (1972) The fluid mosaic model of the structure of cell membranes. Science 175:720–731.
Smit, A.B., Syed, N.I., Schaap, D., van Minnen, J., Klumpermank, J., Kits, K.S., Lodder, H., van der Schors, R.C., van
Elk, R., Sorgedrager, B., Brejc, K., Sixma, T.K., Geraerts, W.P.M. (2001) A glia-derived acetylcholine-binding
protein that modulates synaptic transmission. Nature 411:261–268.
Smith, A.W. (2012) Lipid-protein interactions in biological membranes: A dynamic perspective. Biochim. Biophys. Acta
1818:172–177.
Song, L., Hobaugh, M.R., Shustak, C., Cheley, S., Bayley, H., Gouaux, J.E. (1996) Structure of α-hemolysin, a
heptameric transmembrane pore. Science 274:1859–1866.
Sonntag, Y., Musgaard, M., Olesen, C., Schiøtt, B., Møller, J.V., Nissen, P., Thøgersen, L. (2011) Mutual adaptation of a
membrane protein and its lipid bilayer during conformational changes. Nat. Commun. 2:304.
Spurny, R., Ramerstorfer, J., Price, K., Brams, M., Ernst, M., Nury, H., Verheije, M., Legrand, P., Bertrand, D., Bertrand,
S., Dougherty, D.A., de Esch, I.J.P., Corringer, P.-J., Sieghart, W., Lummis, S.C.R., Ulens, C. (2012) Pentameric
ligand-gated ion channel ELIC is activated by GABA and modulated by benzodiazepines. Proc. Natl. Acad. Sci. USA
109:E3028-E3034.
Starling, A.P., Dalton, K.A., East, J.M., Oliver, S., Lee, A.G. (1996) Effects of phosphatidylethanolamines on the activity
of the Ca
2+ -ATPase of sarcoplasmic reticulum. Biochem. J. 320:309–314.
Stowell, M.H.B., McPhillips, T.M., Rees, D.C., Soltis, S.M., Abresch, E., Feher, G. (1997) Light-induced structural
changes in photosynthetic reaction center: implication for mechanism of electron-proton transfer. Science
276:812–816.
Stroebel, D., Choquet, Y., Popot, J.-L., Picot, D. (2003) An atypical haem in the cytochrome b 6 f complex. Nature
426:413–418.
Svensson-Ek, M., Abramson, J., Larsson, G., Tornroth, S., Brzezinski, P., Iwata, S. (2002) The X-ray crystal structures of
wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321:329–339.
Sweadner, K.J. (2017) An ion-transport enzyme that rocks. Nature 545:162–164.
Taly, A., Hénin, J., Changeux, J.-P., Cecchini, M. (2014) Allosteric regulation of pentameric ligand-gated ion channels:
an emerging mechanistic perspective. Channels 8:350–360.
Tanford, C. (1980) The Hydrophobic Effect: Formation of Micelles and Biological Membranes. 2nd ed. John Wiley &
Sons, New York, 233 p.
Teng, J., Loukin, S.H., Anishkin, A., Kung, C. (2015) The force-from-lipid (FFL) principle of mechanosensitivity, at
large and in elements. Pflügers Arch. 467:27–37.
Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic
reticulum at 2.6 Å resolution. Nature 405:647–655.
Toyoshima, C., Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium.
Nature 418:605–611.
56
1 Membrane Proteins and Their Natural Environment