Fernandez, A., Le Bon, C., Baumlin, N., Giusti, F., Crémel, G., Popot, J.-L., Bagnard, D. (2014) In vivo characterization
of the biodistribution profile of amphipols J. Membr. Biol. 247:1043–1051.
Giusti, F., Popot, J.-L., Tribet, C. (2012) Well-defined critical association concentration and rapid adsorption at the
air/water interface of a short amphiphilic polymer, amphipol A8-35: A study by Förster resonance energy transfer and
dynamic surface tension measurements. Langmuir 28:10372–10380.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Vindigni, J.-D., Pallier, A., Wien, F., Celia, H., Giuliani, A., Tribet, C., Chardot, T., Briozzo, P. (2011) High
water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed
lipid bodies. Biochim. Biophys. Acta 1808:706–716.
Gulati, S., Jamshad, M., Knowles, T.J., Morrison, K.A., Downing, R., Cant, N., Collins, R., Koenderink, J.B., Ford, R.
C., Overduin, M., Kerr, I.D., Dafforn, T.R., Rothnie, A.J. (2014) Detergent-free purification of ABC (ATP-bindingcassette) transporters. Biochem. J. 461:269–278.
Henglein, A., Meisel, D. (1998) Spectrophotometric observations of the adsorption of organosulfur compounds on
colloidal silver nanoparticles. J. Phys. Chem. 102:8364–8366.
Heyn, M.P., Bauer, P.-J., Dencher, N.A. (1975) A natural CD label to probe the structure of the purple membrane from
Halobacterium halobium by means of exciton coupling effects. Biochem. Biophys. Res. Commun. 67:897–903.
Jamshad, M., Charlton, J., Lin, Y.-P., Routledge, S.J., Bawa, Z., Knowles, T.J., Overduin, M., Dekker, N., Dafforn, T.R.,
Bill, R.M., Poyner, D.R., Wheatley, M. (2015a) G protein-coupled receptor solubilization and purification for
biophysical analysis and functional studies, in the total absence of detergent. Biosc. Rep. 35:e00188.
Jamshad, M., Grimard, V., Idini, I., Knowles, T.J., Dowle, M.R., Schofield, N., Sridhar, P., Lin, Y., Finka, R., Wheatley,
M., Thomas, O.R.T., Palmer, R.E., Overduin, M., Govaerts, C., Ruysschaert, J.-M., Edler, K.J., Dafforn,
T.R. (2015b) Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of
membrane proteins. Nano Res. 8:774–789.
Knowles, T.J., Finka, R., Smith, C., Lin, Y.-P., Dafforn, T., Overduin, M. (2009) Membrane proteins solubilized intact in
lipid-containing nanoparticles bounded by styrene maleic acid copolymer. J. Am. Chem. Soc. 131:7484–7485.
Kraft, T.E., Hresko, R.C., Hruz, P.W. (2015) Expression, purification, and functional characterization of the insulinresponsive facilitative glucose transporter GLUT4. Protein Sci. 24:2008–2019.
Kyrychenko, A., Rodnin, M.V., Vargas, M.U., Sharma, S.K., Durand, G., Pucci, B., Popot, J.-L., Ladokhin, A.S. (2012)
Folding of diphtheria toxin T-domain in the presence of amphipols and fluorinated surfactants: Toward thermodynamic measurements of membrane protein folding. Biochim. Biophys. Acta 1818:1006–1012.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L. (2014a) Synthesis of an
oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res. 42:
e83.
Le Bon, C., Popot, J.-L., Giusti, F. (2014b) Labeling and functionalizing amphipols for biological applications.
J. Membr. Biol. 247:797–814.
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.
Liguori, N., Roy, L.M., Opačić, M., Durand, G., Croce, R. (2013) Regulation of light-harvesting in the green alga
Chlamydomonas reinhardtii: the C-terminus of LHCSR is the knob of a dimmer switch. J. Am. Chem. Soc.
135:18339–18342.
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.
Ma, D., Martin, N., Herbet, A., Boquet, D., Tribet, C., Winnik, F.M. (2012) The thermally induced aggregation of
immunoglobulin G in solution is prevented by amphipols. Chem. Lett. 41:1380–1382.
Ma, D., Martin, N., Tribet, C., Winnik, F.M. (2014) Quantitative characterization by asymmetrical flow field-flow
fractionation of IgG thermal aggregation with and without polymer protective agents. Anal. Bioanal. Chem.
406:7539–7547.
Martin, N., Ma, D., Herbet, A., Boquet, D., Winnik, F.M., Tribet, C. (2014) Prevention of thermally induced aggregation
of IgG antibodies by noncovalent interaction with poly(acrylate) derivatives. Biomacromolecules 15:2952–2962.
Martin, N., Ruchmann, J., Tribet, C. (2015) Prevention of aggregation during refolding of carbonic anhydrase via
Coulomb and hydrophobic complexation with octadecyl-modified or azobenzene-modified poly(acrylate)
derivatives. Langmuir 31:338–349.
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.
402
8 Optical Spectroscopy of Membrane Protein/Amphipol Complexes
of the biodistribution profile of amphipols J. Membr. Biol. 247:1043–1051.
Giusti, F., Popot, J.-L., Tribet, C. (2012) Well-defined critical association concentration and rapid adsorption at the
air/water interface of a short amphiphilic polymer, amphipol A8-35: A study by Förster resonance energy transfer and
dynamic surface tension measurements. Langmuir 28:10372–10380.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Vindigni, J.-D., Pallier, A., Wien, F., Celia, H., Giuliani, A., Tribet, C., Chardot, T., Briozzo, P. (2011) High
water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed
lipid bodies. Biochim. Biophys. Acta 1808:706–716.
Gulati, S., Jamshad, M., Knowles, T.J., Morrison, K.A., Downing, R., Cant, N., Collins, R., Koenderink, J.B., Ford, R.
C., Overduin, M., Kerr, I.D., Dafforn, T.R., Rothnie, A.J. (2014) Detergent-free purification of ABC (ATP-bindingcassette) transporters. Biochem. J. 461:269–278.
Henglein, A., Meisel, D. (1998) Spectrophotometric observations of the adsorption of organosulfur compounds on
colloidal silver nanoparticles. J. Phys. Chem. 102:8364–8366.
Heyn, M.P., Bauer, P.-J., Dencher, N.A. (1975) A natural CD label to probe the structure of the purple membrane from
Halobacterium halobium by means of exciton coupling effects. Biochem. Biophys. Res. Commun. 67:897–903.
Jamshad, M., Charlton, J., Lin, Y.-P., Routledge, S.J., Bawa, Z., Knowles, T.J., Overduin, M., Dekker, N., Dafforn, T.R.,
Bill, R.M., Poyner, D.R., Wheatley, M. (2015a) G protein-coupled receptor solubilization and purification for
biophysical analysis and functional studies, in the total absence of detergent. Biosc. Rep. 35:e00188.
Jamshad, M., Grimard, V., Idini, I., Knowles, T.J., Dowle, M.R., Schofield, N., Sridhar, P., Lin, Y., Finka, R., Wheatley,
M., Thomas, O.R.T., Palmer, R.E., Overduin, M., Govaerts, C., Ruysschaert, J.-M., Edler, K.J., Dafforn,
T.R. (2015b) Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of
membrane proteins. Nano Res. 8:774–789.
Knowles, T.J., Finka, R., Smith, C., Lin, Y.-P., Dafforn, T., Overduin, M. (2009) Membrane proteins solubilized intact in
lipid-containing nanoparticles bounded by styrene maleic acid copolymer. J. Am. Chem. Soc. 131:7484–7485.
Kraft, T.E., Hresko, R.C., Hruz, P.W. (2015) Expression, purification, and functional characterization of the insulinresponsive facilitative glucose transporter GLUT4. Protein Sci. 24:2008–2019.
Kyrychenko, A., Rodnin, M.V., Vargas, M.U., Sharma, S.K., Durand, G., Pucci, B., Popot, J.-L., Ladokhin, A.S. (2012)
Folding of diphtheria toxin T-domain in the presence of amphipols and fluorinated surfactants: Toward thermodynamic measurements of membrane protein folding. Biochim. Biophys. Acta 1818:1006–1012.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L. (2014a) Synthesis of an
oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res. 42:
e83.
Le Bon, C., Popot, J.-L., Giusti, F. (2014b) Labeling and functionalizing amphipols for biological applications.
J. Membr. Biol. 247:797–814.
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.
Liguori, N., Roy, L.M., Opačić, M., Durand, G., Croce, R. (2013) Regulation of light-harvesting in the green alga
Chlamydomonas reinhardtii: the C-terminus of LHCSR is the knob of a dimmer switch. J. Am. Chem. Soc.
135:18339–18342.
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.
Ma, D., Martin, N., Herbet, A., Boquet, D., Tribet, C., Winnik, F.M. (2012) The thermally induced aggregation of
immunoglobulin G in solution is prevented by amphipols. Chem. Lett. 41:1380–1382.
Ma, D., Martin, N., Tribet, C., Winnik, F.M. (2014) Quantitative characterization by asymmetrical flow field-flow
fractionation of IgG thermal aggregation with and without polymer protective agents. Anal. Bioanal. Chem.
406:7539–7547.
Martin, N., Ma, D., Herbet, A., Boquet, D., Winnik, F.M., Tribet, C. (2014) Prevention of thermally induced aggregation
of IgG antibodies by noncovalent interaction with poly(acrylate) derivatives. Biomacromolecules 15:2952–2962.
Martin, N., Ruchmann, J., Tribet, C. (2015) Prevention of aggregation during refolding of carbonic anhydrase via
Coulomb and hydrophobic complexation with octadecyl-modified or azobenzene-modified poly(acrylate)
derivatives. Langmuir 31:338–349.
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.
402
8 Optical Spectroscopy of Membrane Protein/Amphipol Complexes