Chiu, Y.H., Jin, X., Medina, C., Leonhardt, S.A., Kiessling, V., Bennett, B.C., Shu, S., Tamm, L.K., Yeager, M.,
Ravichandran, K.S., Bayliss, D.A. (2017) A quantized mechanism for activation of pannexin channels. Nat.
Commun. 8:14324.
Choutko, A., Glättli, A., Fernández, C., Hilty, C., Wüthrich, K., van Gunsteren, W.F. (2011) Membrane protein
dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a
micelle. Eur. Biophys. J. 40:39–58.
Constantine, M., Liew, C.K., Lo, V., Macmillan, A., Cranfield, C.G., Sunde, M., Whan, R., Graham, R.M., Martinac,
B. (2016) Heterologously-expressed and liposome-reconstituted human transient receptor potential melastatin 4 channel (TRPM4) is a functional tetramer. Sci. Rep. 6:19352.
Corcelli, A., Colella, M., Mascolo, G., Fanizzi, F.P., Kates, M. (2000) A novel glycolipid and phospholipid in the purple
membrane. Biochemistry 39:3318–3326.
Corringer, P.-J., Baaden, M., Bocquet, N., Delarue, M., Dufresne, V., Nury, H., Prevost, M., Van Renterghem, C. (2010)
Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues.
J. Physiol. 588:565–572.
Cuevas Arenas, R., Danielczak, B., Martel, A., Porcar, L., Breyton, C., Ebel, C., Keller, S. (2017) Fast collisional lipid
transfer among polymer-bounded nanodiscs. Sci. Rep. 7:45875.
Cvetkov, T.L., Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2011) Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. J. Biol. Chem. 286:38168–38176.
daCosta, C.J.B., Baenziger, J.E. (2009) A lipid-dependent uncoupled conformation of the acetylcholine receptor. J. Biol.
Chem. 284:17819–17825.
Dahmane, T. (2007) Protéines membranaires et amphipols : stabilisation, fonction, renaturation, et développement
d'amphipols sulfonatés pour la RMN des solutions. Thèse de Docorat, Université Paris-7, Paris, 229 p.
Dahmane, T., Damian, M., Mary, S., Popot, J.-L., Banères, J.-L. (2009) Amphipol-assisted in vitro folding of G proteincoupled receptors. Biochemistry 48:6516–6521.
Dahmane, T., Giusti, F., Catoire, L.J., Popot, J.-L. (2011) Sulfonated amphipols: Synthesis, properties and applications.
Biopolymers 95:811–823.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
Damian, M., Marie, J., Leyris, J.-P., Fehrentz, J.-A., Verdié, P., Martinez, J., Banères, J.-L., Mary, S. (2012) High
constitutive activity is an intrinsic feature of ghrelin receptor protein: a study with a functional monomeric GHS-R1a
receptor reconstituted in lipid discs. J. Biol. Chem. 287:3630–3641.
Davidson, A.L., Nikaido, H. (1991) Purification and characterization of the membrane-associated components of the
maltose transport system from Escherichia coli. J. Biol. Chem. 266:8946–8951.
de Foresta, B., le Maire, M., Orlowski, S., Champeil, P., Lund, S., Møller, J.V., Michelangeli, F., Lee, A.G. (1989)
Membrane solubilization by detergent: use of brominated phospholipids to evaluate the detergent-induced changes in
Ca
2+ -ATPase/lipid interaction. Biochemistry 28:2558–2567.
de Vitry, C., Diner, B.A., Popot, J.-L. (1991) Photosystem II particles from Chlamydomonas reinhardtii: purification,
molecular weight, small subunit composition, protein phosphorylation. J. Biol. Chem. 266:16614–16621.
Della Pia, E.A., Holm, J., Lloret, N., Le Bon, C., Popot, J.-L., Zoonens, M., Nygård, J., Martinez, K.L. (2014) A step
closer to membrane protein multiplexed nano-arrays using biotin-doped polypyrrole. ACS Nano 8:1844–1853.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
Dominguez Pardo, J.J., Dörr, J.M., Iyer, A., Cox, R.C., Scheidelaar, S., Koorengevel, M.C., Subramaniam, V., Killian,
J.A. (2017) Solubilization of lipids and lipid phases by the styrene-maleic acid copolymer. Eur. Biophys. J.
46:91–101.
Dörr, J.M., Koorengevel, M.C., Schäfer, M., Prokofyev, A.V., Scheidelaar, S., van der Cruijsenb, E.A.W., Dafforn, T.R.,
Baldus, M., Killian, J.A. (2014) Detergent-free isolation, characterization, and functional reconstitution of a tetrameric K
+ channel: The power of native nanodiscs. Proc. Natl. Acad. Sci. USA 111:18607–18612.
Dörr, J.M., Scheidelaar, S., Koorengevel, M.C., Dominguez, J.J., Schäfer, M., van Walree, C.A., Killian, J.A. (2016) The
styrene-maleic acid copolymer: a versatile tool in membrane research. Eur. Biophys. J. 45:3–21.
Duarte, A.M.S., Wolfs, C.J.A.M., Koehorsta, R.B.M., Popot, J.-L., Hemminga, M.A. (2008) Solubilization of V-ATPase
transmembrane peptides by amphipol A8-35. J. Peptide Chem. 14:389–393.
Elter, S., Raschle, T., Arens, S., Viegas, A., Gelev, V., Etzkorn, M., Wagner, G. (2014) The use of amphipols for NMR
structural characterization of 7-TM proteins. J. Membr. Biol. 247:957–964.
Etzkorn, M., Raschle, T., Hagn, F., Gelev, V., Rice, A.J., Walz, T., Wagner, G. (2013) Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure
21:394–401.
Etzkorn, M., Zoonens, M., Catoire, L.J., Popot, J.-L., Hiller, S. (2014) How amphipols embed membrane proteins:
Global solvent accessibility and interaction with a flexible protein terminus. J. Membr. Biol. 247:965–970.
324
5 Formation and Properties of Membrane Protein/Amphipol Complexes
Ravichandran, K.S., Bayliss, D.A. (2017) A quantized mechanism for activation of pannexin channels. Nat.
Commun. 8:14324.
Choutko, A., Glättli, A., Fernández, C., Hilty, C., Wüthrich, K., van Gunsteren, W.F. (2011) Membrane protein
dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a
micelle. Eur. Biophys. J. 40:39–58.
Constantine, M., Liew, C.K., Lo, V., Macmillan, A., Cranfield, C.G., Sunde, M., Whan, R., Graham, R.M., Martinac,
B. (2016) Heterologously-expressed and liposome-reconstituted human transient receptor potential melastatin 4 channel (TRPM4) is a functional tetramer. Sci. Rep. 6:19352.
Corcelli, A., Colella, M., Mascolo, G., Fanizzi, F.P., Kates, M. (2000) A novel glycolipid and phospholipid in the purple
membrane. Biochemistry 39:3318–3326.
Corringer, P.-J., Baaden, M., Bocquet, N., Delarue, M., Dufresne, V., Nury, H., Prevost, M., Van Renterghem, C. (2010)
Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues.
J. Physiol. 588:565–572.
Cuevas Arenas, R., Danielczak, B., Martel, A., Porcar, L., Breyton, C., Ebel, C., Keller, S. (2017) Fast collisional lipid
transfer among polymer-bounded nanodiscs. Sci. Rep. 7:45875.
Cvetkov, T.L., Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2011) Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy. J. Biol. Chem. 286:38168–38176.
daCosta, C.J.B., Baenziger, J.E. (2009) A lipid-dependent uncoupled conformation of the acetylcholine receptor. J. Biol.
Chem. 284:17819–17825.
Dahmane, T. (2007) Protéines membranaires et amphipols : stabilisation, fonction, renaturation, et développement
d'amphipols sulfonatés pour la RMN des solutions. Thèse de Docorat, Université Paris-7, Paris, 229 p.
Dahmane, T., Damian, M., Mary, S., Popot, J.-L., Banères, J.-L. (2009) Amphipol-assisted in vitro folding of G proteincoupled receptors. Biochemistry 48:6516–6521.
Dahmane, T., Giusti, F., Catoire, L.J., Popot, J.-L. (2011) Sulfonated amphipols: Synthesis, properties and applications.
Biopolymers 95:811–823.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
Damian, M., Marie, J., Leyris, J.-P., Fehrentz, J.-A., Verdié, P., Martinez, J., Banères, J.-L., Mary, S. (2012) High
constitutive activity is an intrinsic feature of ghrelin receptor protein: a study with a functional monomeric GHS-R1a
receptor reconstituted in lipid discs. J. Biol. Chem. 287:3630–3641.
Davidson, A.L., Nikaido, H. (1991) Purification and characterization of the membrane-associated components of the
maltose transport system from Escherichia coli. J. Biol. Chem. 266:8946–8951.
de Foresta, B., le Maire, M., Orlowski, S., Champeil, P., Lund, S., Møller, J.V., Michelangeli, F., Lee, A.G. (1989)
Membrane solubilization by detergent: use of brominated phospholipids to evaluate the detergent-induced changes in
Ca
2+ -ATPase/lipid interaction. Biochemistry 28:2558–2567.
de Vitry, C., Diner, B.A., Popot, J.-L. (1991) Photosystem II particles from Chlamydomonas reinhardtii: purification,
molecular weight, small subunit composition, protein phosphorylation. J. Biol. Chem. 266:16614–16621.
Della Pia, E.A., Holm, J., Lloret, N., Le Bon, C., Popot, J.-L., Zoonens, M., Nygård, J., Martinez, K.L. (2014) A step
closer to membrane protein multiplexed nano-arrays using biotin-doped polypyrrole. ACS Nano 8:1844–1853.
Diab, C., Tribet, C., Gohon, Y., Popot, J.-L., Winnik, F.M. (2007) Complexation of integral membrane proteins by
phosphorylcholine-based amphipols. Biochim. Biophys. Acta 1768:2737–2747.
Dominguez Pardo, J.J., Dörr, J.M., Iyer, A., Cox, R.C., Scheidelaar, S., Koorengevel, M.C., Subramaniam, V., Killian,
J.A. (2017) Solubilization of lipids and lipid phases by the styrene-maleic acid copolymer. Eur. Biophys. J.
46:91–101.
Dörr, J.M., Koorengevel, M.C., Schäfer, M., Prokofyev, A.V., Scheidelaar, S., van der Cruijsenb, E.A.W., Dafforn, T.R.,
Baldus, M., Killian, J.A. (2014) Detergent-free isolation, characterization, and functional reconstitution of a tetrameric K
+ channel: The power of native nanodiscs. Proc. Natl. Acad. Sci. USA 111:18607–18612.
Dörr, J.M., Scheidelaar, S., Koorengevel, M.C., Dominguez, J.J., Schäfer, M., van Walree, C.A., Killian, J.A. (2016) The
styrene-maleic acid copolymer: a versatile tool in membrane research. Eur. Biophys. J. 45:3–21.
Duarte, A.M.S., Wolfs, C.J.A.M., Koehorsta, R.B.M., Popot, J.-L., Hemminga, M.A. (2008) Solubilization of V-ATPase
transmembrane peptides by amphipol A8-35. J. Peptide Chem. 14:389–393.
Elter, S., Raschle, T., Arens, S., Viegas, A., Gelev, V., Etzkorn, M., Wagner, G. (2014) The use of amphipols for NMR
structural characterization of 7-TM proteins. J. Membr. Biol. 247:957–964.
Etzkorn, M., Raschle, T., Hagn, F., Gelev, V., Rice, A.J., Walz, T., Wagner, G. (2013) Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure
21:394–401.
Etzkorn, M., Zoonens, M., Catoire, L.J., Popot, J.-L., Hiller, S. (2014) How amphipols embed membrane proteins:
Global solvent accessibility and interaction with a flexible protein terminus. J. Membr. Biol. 247:965–970.
324
5 Formation and Properties of Membrane Protein/Amphipol Complexes