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Nagy, J.K., Kuhn Hoffmann, A., Keyes, M.H., Gray, D.N., Oxenoid, K., Sanders, C.R. (2001) Use of amphipathic
polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501:115–120.
Natali, F., Castellano, C., Pozzi, D., Congiu-Castellano, A. (2005) Dynamic properties of an oriented lipid/DNA complex
studied by neutron scattering. Biophys. J. 88:1081–1090.
Natali, F., Relini, A., Gliozzi, A., Rolandi, R., Cavatorta, P., Deriu, A., Fasano, A., Riccio, P. (2004) The influence of the
lipid–protein interaction on the membrane dynamics. Physica B: Condensed Matter 350:E623-E626.
Noda, T., Morishima, Y. (1999) Hydrophobic association of random copolymers of sodium 2-(acrylamido)-2-methylpropanesulfonate and dodecyl methacrylate in water as studied by fluorescence and dynamic light scattering.
Macromolecules 32:4631–4640.
Oluwole, A.O., Danielczak, B., Meister, A., Babalola, J.O., Vargas, C., Keller, S. (2017) Solubilization of membrane
proteins into functional lipid-bilayer nanodiscs using a diisobutylene/maleic acid copolymer. Angew. Chem. Int.
Ed. Engl. 56:1919–1924.
Opačić, M., Durand, G., Bosco, M., Polidori, A., Popot, J.-L. (2014a) Amphipols and photosynthetic light-harvesting
pigment-protein complexes. J. Membr. Biol. 247:1031–1041.
Opačić, M., Giusti, F., Broos, J., Popot, J.-L. (2014b) Isolation of Escherichia coli mannitol permease, EII
mtl , trapped in
amphipol A8-35 and fluorescein-labeled A8-35. J. Membr. Biol. 247:1019–1030.
Orwick, M.C., Judge, P.J., Procek, J., Lindholm, L., Graziadei, A., Engel, A., Grobner, G., Watts, A. (2012) Detergentfree formation and physicochemical characterization of nanosized lipid-polymer complexes. Angew. Chem. Int. Ed.
51:4653–4657.
Orwick-Rydmark, M., Lovett, J.E., Graziadei, A., Lindholm, L., Hicks, M.R., Watts, A. (2012) Detergent-free
incorporation of a seven-transmembrane receptor protein into nanosized bilayer Lipodisq particles for functional
and biophysical studies. Nano Lett. 12:4687–4692.
Parambil, A.M., Puttaiahgowda, Y.M., Shankarappa, P. (2012) Copolymerization of N-vinyl pyrrolidone with methyl
methacrylate by Ti(III)-DMG redox initiator. Turk. J. Chem. 36:397–409.
Paulsen, C.E., Armache, J.-P., Gao, Y., Cheng, Y., Julius, D. (2015) Structure of the TRPA1 ion channel suggests
regulatory mechanisms. Nature 520:511–517.
Perlmutter, J.D., Drasler, W.J., Xie, W., Gao, J., Popot, J.-L., Sachs, J.N. (2011) All-atom and coarse-grained molecular
dynamics simulations of a membrane protein stabilizing polymer. Langmuir 27:10523–10537.
Perlmutter, J.D., Sachs, J.N. (2009a) Experimental verification of lipid bilayer structure through multi-scale modeling.
Biochim. Biophys. Acta 1788:2284–2290.
Perlmutter, J.D., Sachs, J.N. (2009b) Inhibiting lateral domain formation in lipid bilayers: simulations of alternative
steroid headgroup chemistries. J. Am. Chem. Soc. 131:1636–16363.
Perry, T., Souabni, H., Rapisarda, C., Fronzes, R., Giusti, F., Popot, J.-L., Zoonens, M., Gubellini, F. (2018) Visualizing
transmembrane regions of protein complexes by electron microscopy using biotinylated amphipols. Submitted for
publication.
Petit-Agnely, F., Iliopoulos, I. (1999) Aggregation mechanism of amphiphilic associating polymers studied by
19 F and
13 C nuclear magnetic resonance. J. Phys. Chem. B 103:4803–4808.
Petit-Agnely, F., Iliopoulos, I., Zana, R. (2000) Hydrophobically modified sodium polyacrylates in aqueous solutions:
Association mechanism and characterization of the aggregates by fluorescence probing. Langmuir 16:9921–9927.
Picard, M., Dahmane, T., Garrigos, M., Gauron, C., Giusti, F., le Maire, M., Popot, J.-L., Champeil, P. (2006) Protective
and inhibitory effects of various types of amphipols on the Ca
2+ -ATPase from sarcoplasmic reticulum: a comparative
study. Biochemistry 45:1861–1869.
Picard, M., Duval-Terrié, C., Dé, E., Champeil, P. (2004) Stabilization of membranes upon interaction of amphipathic
polymers with membrane proteins. Protein Sci. 13:3056–3058.
Pierik, S.C.J., van Herk, A.M. (2003) Catalytic chain transfer copolymerization of methyl methacrylate and butyl
acrylate. Macromol. Chem. Phys. 204:1406–1418.
Pintauer, T., Matyjaszewski, K. (2008) Atom transfer radical addition and polymerization reactions catalyzed by ppm
amounts of copper complexes. Chem. Soc. Rev. 37:1087–1097.
Planchard, N., Point, E., Dahmane, T., Giusti, F., Renault, M., Le Bon, C., Durand, G., Milon, A., Guittet, E., Zoonens,
M., Popot, J.-L., Catoire, L.J. (2014) The use of amphipols for solution NMR studies of membrane proteins:
advantages and limitations as compared to other solubilizing media. J. Membr. Biol. 247:827–842.
Polovinkin, V., Balandin, T., Volkov, O., Round, E., Borshchevskiy, V., Utrobin, P., von Stetten, D., Royant, A.,
Willbold, D., Arzumanyan, A., Popot, J.-L., Gordeliy, V. (2014) Nanoparticle surface-enhanced Raman scattering of
bacteriorhodopsin stabilized by amphipol A8-35. J. Membr. Biol. 247:971–980.
Popot, J.-L. (2010) Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying
membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737–775.
References
233
Nagy, J.K., Kuhn Hoffmann, A., Keyes, M.H., Gray, D.N., Oxenoid, K., Sanders, C.R. (2001) Use of amphipathic
polymers to deliver a membrane protein to lipid bilayers. FEBS Lett. 501:115–120.
Natali, F., Castellano, C., Pozzi, D., Congiu-Castellano, A. (2005) Dynamic properties of an oriented lipid/DNA complex
studied by neutron scattering. Biophys. J. 88:1081–1090.
Natali, F., Relini, A., Gliozzi, A., Rolandi, R., Cavatorta, P., Deriu, A., Fasano, A., Riccio, P. (2004) The influence of the
lipid–protein interaction on the membrane dynamics. Physica B: Condensed Matter 350:E623-E626.
Noda, T., Morishima, Y. (1999) Hydrophobic association of random copolymers of sodium 2-(acrylamido)-2-methylpropanesulfonate and dodecyl methacrylate in water as studied by fluorescence and dynamic light scattering.
Macromolecules 32:4631–4640.
Oluwole, A.O., Danielczak, B., Meister, A., Babalola, J.O., Vargas, C., Keller, S. (2017) Solubilization of membrane
proteins into functional lipid-bilayer nanodiscs using a diisobutylene/maleic acid copolymer. Angew. Chem. Int.
Ed. Engl. 56:1919–1924.
Opačić, M., Durand, G., Bosco, M., Polidori, A., Popot, J.-L. (2014a) Amphipols and photosynthetic light-harvesting
pigment-protein complexes. J. Membr. Biol. 247:1031–1041.
Opačić, M., Giusti, F., Broos, J., Popot, J.-L. (2014b) Isolation of Escherichia coli mannitol permease, EII
mtl , trapped in
amphipol A8-35 and fluorescein-labeled A8-35. J. Membr. Biol. 247:1019–1030.
Orwick, M.C., Judge, P.J., Procek, J., Lindholm, L., Graziadei, A., Engel, A., Grobner, G., Watts, A. (2012) Detergentfree formation and physicochemical characterization of nanosized lipid-polymer complexes. Angew. Chem. Int. Ed.
51:4653–4657.
Orwick-Rydmark, M., Lovett, J.E., Graziadei, A., Lindholm, L., Hicks, M.R., Watts, A. (2012) Detergent-free
incorporation of a seven-transmembrane receptor protein into nanosized bilayer Lipodisq particles for functional
and biophysical studies. Nano Lett. 12:4687–4692.
Parambil, A.M., Puttaiahgowda, Y.M., Shankarappa, P. (2012) Copolymerization of N-vinyl pyrrolidone with methyl
methacrylate by Ti(III)-DMG redox initiator. Turk. J. Chem. 36:397–409.
Paulsen, C.E., Armache, J.-P., Gao, Y., Cheng, Y., Julius, D. (2015) Structure of the TRPA1 ion channel suggests
regulatory mechanisms. Nature 520:511–517.
Perlmutter, J.D., Drasler, W.J., Xie, W., Gao, J., Popot, J.-L., Sachs, J.N. (2011) All-atom and coarse-grained molecular
dynamics simulations of a membrane protein stabilizing polymer. Langmuir 27:10523–10537.
Perlmutter, J.D., Sachs, J.N. (2009a) Experimental verification of lipid bilayer structure through multi-scale modeling.
Biochim. Biophys. Acta 1788:2284–2290.
Perlmutter, J.D., Sachs, J.N. (2009b) Inhibiting lateral domain formation in lipid bilayers: simulations of alternative
steroid headgroup chemistries. J. Am. Chem. Soc. 131:1636–16363.
Perry, T., Souabni, H., Rapisarda, C., Fronzes, R., Giusti, F., Popot, J.-L., Zoonens, M., Gubellini, F. (2018) Visualizing
transmembrane regions of protein complexes by electron microscopy using biotinylated amphipols. Submitted for
publication.
Petit-Agnely, F., Iliopoulos, I. (1999) Aggregation mechanism of amphiphilic associating polymers studied by
19 F and
13 C nuclear magnetic resonance. J. Phys. Chem. B 103:4803–4808.
Petit-Agnely, F., Iliopoulos, I., Zana, R. (2000) Hydrophobically modified sodium polyacrylates in aqueous solutions:
Association mechanism and characterization of the aggregates by fluorescence probing. Langmuir 16:9921–9927.
Picard, M., Dahmane, T., Garrigos, M., Gauron, C., Giusti, F., le Maire, M., Popot, J.-L., Champeil, P. (2006) Protective
and inhibitory effects of various types of amphipols on the Ca
2+ -ATPase from sarcoplasmic reticulum: a comparative
study. Biochemistry 45:1861–1869.
Picard, M., Duval-Terrié, C., Dé, E., Champeil, P. (2004) Stabilization of membranes upon interaction of amphipathic
polymers with membrane proteins. Protein Sci. 13:3056–3058.
Pierik, S.C.J., van Herk, A.M. (2003) Catalytic chain transfer copolymerization of methyl methacrylate and butyl
acrylate. Macromol. Chem. Phys. 204:1406–1418.
Pintauer, T., Matyjaszewski, K. (2008) Atom transfer radical addition and polymerization reactions catalyzed by ppm
amounts of copper complexes. Chem. Soc. Rev. 37:1087–1097.
Planchard, N., Point, E., Dahmane, T., Giusti, F., Renault, M., Le Bon, C., Durand, G., Milon, A., Guittet, E., Zoonens,
M., Popot, J.-L., Catoire, L.J. (2014) The use of amphipols for solution NMR studies of membrane proteins:
advantages and limitations as compared to other solubilizing media. J. Membr. Biol. 247:827–842.
Polovinkin, V., Balandin, T., Volkov, O., Round, E., Borshchevskiy, V., Utrobin, P., von Stetten, D., Royant, A.,
Willbold, D., Arzumanyan, A., Popot, J.-L., Gordeliy, V. (2014) Nanoparticle surface-enhanced Raman scattering of
bacteriorhodopsin stabilized by amphipol A8-35. J. Membr. Biol. 247:971–980.
Popot, J.-L. (2010) Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying
membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737–775.
References
233