Le Roy, A., Wang, K., Schaack, B., Schuck, P., Breyton, C., Ebel, C. (2015) AUC and small-angle scattering for
membrane proteins. Meth. Enzymol. 562:257–286.
Leney, A.C., McMorran, L.M., Radford, S.E., Ashcroft, A.E. (2012) Amphipathic polymers enable the study of
functional membrane proteins in the gas phase. Anal. Chem. 84:9841–9847.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryomicroscopy. Nature 504:107–112.
Lindhoud, S., Carvalho, V., Pronk, J.W., Aubin-Tam, M.E. (2016) SMA-SH: Modified styrene-maleic acid copolymer
for functionalization of lipid nanodiscs. Biomacromolecules 17:1516–1522.
Logez, C., Damian, M., Legros, C., Dupré, C., Guéry, M., Mary, S., Wagner, R., M’Kadmi, C., Nosjean, O., Fould, B.,
Marie, J., Fehrentz, J.A., Martinez, J., Ferry, G., Boutin, J.A., Banères, J.-L. (2016) Detergent-free isolation of
functional G protein-coupled receptors into nanometric lipid particles. Biochemistry 55:38–48.
le Maire, M., Arnou, B., Olesen, C., Georgin, D., Ebel, C., Møller, J.V. (2008) Gel chromatography and analytical
ultracentrifugation to determine the extent of detergent binding and aggregation, and Stokes radius of membrane
proteins using sarcoplasmic reticulum Ca
2+ -ATPase as an example. Nat. Protoc. 3:1782–1795.
Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., Popot, J.-L. (2002) Allosteric
transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical
constraints. FEBS Lett. 528:251–256.
McEwen, C.R. (1967) Tables for estimating sedimentation through linear concentration gradients of sucrose solution.
Anal. Biochem. 20:114–119.
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.
Nowaczyk, M., Oworah-Nkruma, R., Zoonens, M., Rögner, M., Popot, J.-L. (2004) Amphipols: strategies for an
improved PS2 environment in aqueous solution, in: Miyake, J., ed., Biohydrogen III. Elsevier, Dordrecht, The
Netherlands, Kyoto, pp. 151–159.
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-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.
Padrick, S.B., Deka, R.K., Chuang, J.L., Wynn, R.M., Chuang, D.T., Norgard, M.V., Rosen, M.K., Brautigam,
C.A. (2010) Determination of protein complex stoichiometry through multisignal sedimentation velocity
experiments. Anal. Biochem. 407:89–103.
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.
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.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014) High-resolution structure of a membrane protein transferred from amphipol to a
lipidic mesophase. J. Membr. Biol. 247:997–1004.
Popot, J.-L., Berry, E.A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D.M., Flötenmeyer, M., Giusti, F., Gohon,
Y., Hervé, P., Hong, Q., Lakey, J.H., Leonard, K., Shuman, H.A., Timmins, P., Warschawski, D.E., Zito, F.,
Zoonens, M., Pucci, B., Tribet, C. (2003) Amphipols: polymeric surfactants for membrane biology research. Cell.
Mol. Life Sci. 60:1559–1574.
Postis, V., Rawson, S., Mitchell, J.K., Lee, S.C., Parslow, R.A., Dafforn, T.R., Baldwin, S.A., Muench, S.P. (2015) The
use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.
Biochim. Biophys. Acta 1848:496–501.
Prata, C., Giusti, F., Gohon, Y., Pucci, B., Popot, J.-L., Tribet, C. (2001) Non-ionic amphiphilic polymers derived from
tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent.
Biopolymers 56:77–84.
Rahmeh, R., Damian, M., Cottet, M., Orcel, H., Mendre, C., Durroux, T., Sharma, K.S., Durand, G., Pucci, B., Trinquet,
E., Zwier, J.M., Deupi, X., Bron, P., Banères J.-L., Mouillac, B., Granier, S. (2012) Structural insights into biased G
References
451
membrane proteins. Meth. Enzymol. 562:257–286.
Leney, A.C., McMorran, L.M., Radford, S.E., Ashcroft, A.E. (2012) Amphipathic polymers enable the study of
functional membrane proteins in the gas phase. Anal. Chem. 84:9841–9847.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2013) Structure of the TRPV1 ion channel determined by electron cryomicroscopy. Nature 504:107–112.
Lindhoud, S., Carvalho, V., Pronk, J.W., Aubin-Tam, M.E. (2016) SMA-SH: Modified styrene-maleic acid copolymer
for functionalization of lipid nanodiscs. Biomacromolecules 17:1516–1522.
Logez, C., Damian, M., Legros, C., Dupré, C., Guéry, M., Mary, S., Wagner, R., M’Kadmi, C., Nosjean, O., Fould, B.,
Marie, J., Fehrentz, J.A., Martinez, J., Ferry, G., Boutin, J.A., Banères, J.-L. (2016) Detergent-free isolation of
functional G protein-coupled receptors into nanometric lipid particles. Biochemistry 55:38–48.
le Maire, M., Arnou, B., Olesen, C., Georgin, D., Ebel, C., Møller, J.V. (2008) Gel chromatography and analytical
ultracentrifugation to determine the extent of detergent binding and aggregation, and Stokes radius of membrane
proteins using sarcoplasmic reticulum Ca
2+ -ATPase as an example. Nat. Protoc. 3:1782–1795.
Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., Popot, J.-L. (2002) Allosteric
transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical
constraints. FEBS Lett. 528:251–256.
McEwen, C.R. (1967) Tables for estimating sedimentation through linear concentration gradients of sucrose solution.
Anal. Biochem. 20:114–119.
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.
Nowaczyk, M., Oworah-Nkruma, R., Zoonens, M., Rögner, M., Popot, J.-L. (2004) Amphipols: strategies for an
improved PS2 environment in aqueous solution, in: Miyake, J., ed., Biohydrogen III. Elsevier, Dordrecht, The
Netherlands, Kyoto, pp. 151–159.
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-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.
Padrick, S.B., Deka, R.K., Chuang, J.L., Wynn, R.M., Chuang, D.T., Norgard, M.V., Rosen, M.K., Brautigam,
C.A. (2010) Determination of protein complex stoichiometry through multisignal sedimentation velocity
experiments. Anal. Biochem. 407:89–103.
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.
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.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014) High-resolution structure of a membrane protein transferred from amphipol to a
lipidic mesophase. J. Membr. Biol. 247:997–1004.
Popot, J.-L., Berry, E.A., Charvolin, D., Creuzenet, C., Ebel, C., Engelman, D.M., Flötenmeyer, M., Giusti, F., Gohon,
Y., Hervé, P., Hong, Q., Lakey, J.H., Leonard, K., Shuman, H.A., Timmins, P., Warschawski, D.E., Zito, F.,
Zoonens, M., Pucci, B., Tribet, C. (2003) Amphipols: polymeric surfactants for membrane biology research. Cell.
Mol. Life Sci. 60:1559–1574.
Postis, V., Rawson, S., Mitchell, J.K., Lee, S.C., Parslow, R.A., Dafforn, T.R., Baldwin, S.A., Muench, S.P. (2015) The
use of SMALPs as a novel membrane protein scaffold for structure study by negative stain electron microscopy.
Biochim. Biophys. Acta 1848:496–501.
Prata, C., Giusti, F., Gohon, Y., Pucci, B., Popot, J.-L., Tribet, C. (2001) Non-ionic amphiphilic polymers derived from
tris(hydroxymethyl)-acrylamidomethane keep membrane proteins soluble and native in the absence of detergent.
Biopolymers 56:77–84.
Rahmeh, R., Damian, M., Cottet, M., Orcel, H., Mendre, C., Durroux, T., Sharma, K.S., Durand, G., Pucci, B., Trinquet,
E., Zwier, J.M., Deupi, X., Bron, P., Banères J.-L., Mouillac, B., Granier, S. (2012) Structural insights into biased G
References
451