protein-coupled receptor signaling revealed by fluorescence spectroscopy. Proc. Natl. Acad. Sci. USA
109:6733–6738.
Salvay, A.G., Ebel, C. (2006) Analytical ultracentrifuge for the characterization of detergent in solution. Progr. Colloid
Polym. Sci. 131:74–82.
Schägger, H., von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in
enzymatically active form. Anal. Biochem. 1999:223–231.
Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm
equation modeling. Biophys. J. 78:1606–1619.
Sharma, K.S., Durand, G., Gabel, F., Bazzacco, P., Le Bon, C., Billon-Denis, E., Catoire, L.J., Popot, J.-L., Ebel, C.,
Pucci, B. (2012) Non-ionic amphiphilic homopolymers: Synthesis, solution properties, and biochemical validation.
Langmuir 28:4625–4639.
Shen, P.S., Yang, X., DeCaen, P.G., Liu, X., Bulkley, D., Clapham, D.E., Cao, E. (2016) The structure of the Polycystic
Kidney Disease channel PKD2 in lipid nanodiscs. Cell 167:763–773.e711.
Shinzawa-Itoh, K., Shimomura, H., Yanagisawa, S., Shimada, S., Takahashi, R., Oosaki, M., Ogura, T., Tsukihara,
T. (2016) Purification of active respiratory supercomplex from bovine heart mitochondria enables functional studies.
J. Biol. Chem. 291:4178–4184.
Solovyova, A., Schuck, P., Costenaro, L., Ebel, C. (2001) Non-ideality by sedimentation velocity of halophilic malate
dehydrogenase in complex solvents. Biophys. J. 81:1868–1880.
Sousa, J.S., Mills, D.J., Vonck, J., Kühlbrandt, W. (2016) Functional asymmetry and electron flow in the bovine
respirasome. eLIFE 5:e21290.
Stuhrmann, H.B. (1970) Interpretation of small-angle scattering functions of dilute solutions and gases. A representation
of the structures related to a one-particle scattering function. Acta Cryst. Sect. A 26:297–306.
Svergun, D.I. (1999) Restoring low-resolution structure of biological macromolecules from solution scattering using
simulated annealing. Biophys. J. 76:2879–2886.
Svergun, D.I., Koch, M.H.J., Timmins, P.A., May, R.P. (2013) Small Angle X-Ray and Neutron Scattering from
Solutions of Biological Macromolecule. Oxford University Press, Oxford, 368 p.
Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton,
J.W. (2014) Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: A biochemical and
structural case study. J. Membr. Biol. 247:1005–1018.
Tribet, C., Audebert, R., Popot, J.-L. (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous
solutions. Proc. Natl. Acad. Sci. USA 93:15047–15050.
Tribet, C., Audebert, R., Popot, J.-L. (1997) Stabilization of hydrophobic colloidal dispersions in water with amphiphilic
polymers: Application to integral membrane proteins. Langmuir 13:5570–5576.
Tribet, C., Mills, D., Haider, M., Popot, J.-L. (1998) Scanning transmission electron microscopy study of the molecular
mass of amphipol/cytochrome b 6 f complexes. Biochimie 80:475–482.
Tsybovsky, Y., Orban, T., Molday, R.S., Taylor, D., Palczewski, K. (2013) Molecular organization and ATP-induced
conformational changes of ABCA4, the photoreceptor-specific ABC transporter. Structure 21:854–860.
Vázquez-Acevedo, M., Vega-de Luna, F., Sánchez-Vásquez, L., Colina-Tenorio, L., Remacle, C., Cardol, P., MirandaAstudillo, H., González-Halphen, D. (2016) Dissecting the peripheral stalk of the mitochondrial ATP synthase of
chlorophycean algae. Biochim. Biophys. Acta 1857:1183–1190.
Zaccai, N.R., Serdyuk, I.N., Zaccai, G. (2017) Methods in Molecular Biophysics. Structure, dynamics, function, 2nd
ed. Cambridge University Press, Cambridge, 684 p.
Zoonens, M. (2004) Caractérisation des complexes formés entre le domaine transmembranaire de la protéine OmpA et
des polymères amphiphiles, les amphipols. Application à l’étude structurale des protéines membranaires par RMN à
haute résolution. Thèse de Doctorat, Université Paris-6, Paris, 233 p.
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L. (2005) NMR study of a membrane protein in detergent-free aqueous
solution. Proc. Natl. Acad. Sci. USA 102:8893–8898.
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L. (2007) Dynamics of membrane protein/amphipol association studied by
Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins.
Biochemistry 46:10392–10404.
Zoonens, M., Zito, F., Martinez, K.L., Popot, J.-L. (2014) Amphipols: a general introduction and some protocols, in:
Mus-Veteau, I., ed., Membrane Proteins Production for Structural Analysis. Springer, New York, Heidelberg,
Dordrecht, London, pp. 173–203.
452
9 Solution Studies of Membrane Protein/Amphipol Complexes
109:6733–6738.
Salvay, A.G., Ebel, C. (2006) Analytical ultracentrifuge for the characterization of detergent in solution. Progr. Colloid
Polym. Sci. 131:74–82.
Schägger, H., von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in
enzymatically active form. Anal. Biochem. 1999:223–231.
Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm
equation modeling. Biophys. J. 78:1606–1619.
Sharma, K.S., Durand, G., Gabel, F., Bazzacco, P., Le Bon, C., Billon-Denis, E., Catoire, L.J., Popot, J.-L., Ebel, C.,
Pucci, B. (2012) Non-ionic amphiphilic homopolymers: Synthesis, solution properties, and biochemical validation.
Langmuir 28:4625–4639.
Shen, P.S., Yang, X., DeCaen, P.G., Liu, X., Bulkley, D., Clapham, D.E., Cao, E. (2016) The structure of the Polycystic
Kidney Disease channel PKD2 in lipid nanodiscs. Cell 167:763–773.e711.
Shinzawa-Itoh, K., Shimomura, H., Yanagisawa, S., Shimada, S., Takahashi, R., Oosaki, M., Ogura, T., Tsukihara,
T. (2016) Purification of active respiratory supercomplex from bovine heart mitochondria enables functional studies.
J. Biol. Chem. 291:4178–4184.
Solovyova, A., Schuck, P., Costenaro, L., Ebel, C. (2001) Non-ideality by sedimentation velocity of halophilic malate
dehydrogenase in complex solvents. Biophys. J. 81:1868–1880.
Sousa, J.S., Mills, D.J., Vonck, J., Kühlbrandt, W. (2016) Functional asymmetry and electron flow in the bovine
respirasome. eLIFE 5:e21290.
Stuhrmann, H.B. (1970) Interpretation of small-angle scattering functions of dilute solutions and gases. A representation
of the structures related to a one-particle scattering function. Acta Cryst. Sect. A 26:297–306.
Svergun, D.I. (1999) Restoring low-resolution structure of biological macromolecules from solution scattering using
simulated annealing. Biophys. J. 76:2879–2886.
Svergun, D.I., Koch, M.H.J., Timmins, P.A., May, R.P. (2013) Small Angle X-Ray and Neutron Scattering from
Solutions of Biological Macromolecule. Oxford University Press, Oxford, 368 p.
Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton,
J.W. (2014) Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: A biochemical and
structural case study. J. Membr. Biol. 247:1005–1018.
Tribet, C., Audebert, R., Popot, J.-L. (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous
solutions. Proc. Natl. Acad. Sci. USA 93:15047–15050.
Tribet, C., Audebert, R., Popot, J.-L. (1997) Stabilization of hydrophobic colloidal dispersions in water with amphiphilic
polymers: Application to integral membrane proteins. Langmuir 13:5570–5576.
Tribet, C., Mills, D., Haider, M., Popot, J.-L. (1998) Scanning transmission electron microscopy study of the molecular
mass of amphipol/cytochrome b 6 f complexes. Biochimie 80:475–482.
Tsybovsky, Y., Orban, T., Molday, R.S., Taylor, D., Palczewski, K. (2013) Molecular organization and ATP-induced
conformational changes of ABCA4, the photoreceptor-specific ABC transporter. Structure 21:854–860.
Vázquez-Acevedo, M., Vega-de Luna, F., Sánchez-Vásquez, L., Colina-Tenorio, L., Remacle, C., Cardol, P., MirandaAstudillo, H., González-Halphen, D. (2016) Dissecting the peripheral stalk of the mitochondrial ATP synthase of
chlorophycean algae. Biochim. Biophys. Acta 1857:1183–1190.
Zaccai, N.R., Serdyuk, I.N., Zaccai, G. (2017) Methods in Molecular Biophysics. Structure, dynamics, function, 2nd
ed. Cambridge University Press, Cambridge, 684 p.
Zoonens, M. (2004) Caractérisation des complexes formés entre le domaine transmembranaire de la protéine OmpA et
des polymères amphiphiles, les amphipols. Application à l’étude structurale des protéines membranaires par RMN à
haute résolution. Thèse de Doctorat, Université Paris-6, Paris, 233 p.
Zoonens, M., Catoire, L.J., Giusti, F., Popot, J.-L. (2005) NMR study of a membrane protein in detergent-free aqueous
solution. Proc. Natl. Acad. Sci. USA 102:8893–8898.
Zoonens, M., Giusti, F., Zito, F., Popot, J.-L. (2007) Dynamics of membrane protein/amphipol association studied by
Förster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins.
Biochemistry 46:10392–10404.
Zoonens, M., Zito, F., Martinez, K.L., Popot, J.-L. (2014) Amphipols: a general introduction and some protocols, in:
Mus-Veteau, I., ed., Membrane Proteins Production for Structural Analysis. Springer, New York, Heidelberg,
Dordrecht, London, pp. 173–203.
452
9 Solution Studies of Membrane Protein/Amphipol Complexes