Polidori, A., Raynal, S., Barret, L.-A., Dahani, M., Barrot-Ivolot, C., Jungas, C., Frotscher, E., Keller, S., Ebel, C.,
Breyton, C., Bonneté, F. (2016) Sparingly fluorinated maltoside-based surfactants for membrane-protein stabilization. New J. Chem. 40:5364–5378.
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. (2010) Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying
membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737–775.
Popot, J.-L., Engelman, D.M. (2000) Helical membrane protein folding, stability and evolution. Annu. Rev. Biochem.
69:881–923.
Popovic, K., Holyoake, J., Pomès, R., Privé, G.G. (2012) Structure of saposin A lipoprotein discs. Proc. Natl. Acad. Sci.
USA 109:2908–2912.
Posokhov, Y.O., Rodnin, M.V., Das, S.K., Pucci, B., Ladokhin, A.S. (2008) FCS study of the thermodynamics of
membrane protein insertion into the lipid bilayer chaperoned by fluorinated surfactants. Biophys. J. 95:L54-L56.
Poulos, S., Morgan, J.L., Zimmer, J., Faham, S. (2015) Bicelles coming of age: an empirical approach to bicelle
crystallization. Meth. Enzymol. 557:393–416.
Privé, G. (2009) Lipopeptide detergents for membrane protein studies. Curr. Opin. Struct. Biol. 19:1–7.
Prosser, R.S., Evanics, F., Kitevski, J.L., Al-Abdul-Wahid, M.S. (2006) Current applications of bicelles in NMR studies
of membrane-associated amphiphiles and proteins. Biochemistry 45:8453–8465.
Prosser, R.S., Hunt, S.A., DiNatale, J.A., Vold, R.R. (1996) Magnetically aligned membrane model systems with
positive order parameters: switching the sign of S zz with paramagnetic ions. J. Am. Chem. Soc. 118:269–270.
Prosser, R.S., Hwang, J.S., Vold, R.R. (1998) Magnetically aligned phospholipid bilayers with positive ordering: a new
model membrane system. Biophys. J. 74:2405–2418.
Proverbio, D., Roos, C., Beyermann, M., Orbán, E., Dötsch, V., Bernhard, F. (2013) Functional properties of cell-free
expressed human endothelin A and endothelin B receptors in artificial membrane environments. Biochim. Biophys.
Acta 1828:2182–2192.
Puthenveetil, R., Nguyen, K., Vinogradova, O. (2017) Nanodiscs and solution NMR: preparation, application and
challenges. Nanotech. Rev. 6:111–126.
Puthenveetil, R., Vinogradova, O. (2013) Optimization of the design and preparation of nanoscale phospholipid bilayers
for its application to solution NMR. Proteins: Struct. Funct. Bioinf. 81:1222–1231.
Qureshi, T., Goto, N.K. (2011) Contemporary methods in structure determination of membrane proteins by solution
NMR. Top. Curr. Chem. 326:123–185.
Ram, P., Prestegard, J.H. (1988) Magnetic field-induced ordering of bile salt/phospholipid micelles: new media for NMR
structural investigations. Biochim. Biophys. Acta 940:289–294.
Ramjeesingh, M., Huan, L.J., Garami, E., Bear, C.E. (1999) Novel method for evaluation of the oligomeric structure of
membrane proteins. Biochem. J. 342.
Ranaghan, M.J., Schwall, C.T., Alder, N.N., Birge, R.R. (2011) Green proteorhodopsin reconstituted into nanoscale
phospholipid bilayers (nanodiscs) as photoactive monomers. J. Am. Chem. Soc. 133:18318–18327.
Raschle, T., Hiller, S., Etzkorn, M., Wagner, G. (2010) Nonmicellar systems for solution NMR spectroscopy of
membrane proteins. Curr. Opin. Struct. Biol. 20:471–479.
Raschle, T., Hiller, S., Yu, T.Y., Rice, A.J., Walz, T., Wagner, G. (2009) Structural and functional characterization of the
integral membrane protein VDAC-1 in lipid bilayer nanodiscs. J. Am. Chem. Soc. 131:17777–17779.
Rasmussen, S.G., Choi, H.J., Rosenbaum, D.M., Kobilka, T.S., Thian, F.S., Edwards, P.C., Burghammer, M., Ratnala,
V.R., Sanishvili, R., Fischetti, R.F., Schertler, G.F., Weis, W.I., Kobilka, B.K. (2007) Crystal structure of the human
β 2 adrenergic G protein-coupled receptor. Nature 450:383–387.
Raychaudhuri, P., Li, Q., Mason, A., Mikhailova, E., Heron, A.J., Bayley, H. (2011) Fluorinated amphiphiles control the
insertion of α-hemolysin pores into lipid bilayers. Biochemistry 50:1599–1606.
Reichart, T.M., Baksh, M.M., Rhee, J.-K., Fiedler, J.D., Sligar, S.G., Finn, M.G., Zwick, M.B., Dawson, P.E. (2016)
Trimerization of the HIV transmembrane domain in lipid bilayers modulates broadly neutralizing antibody binding.
Angew. Chem. Int. Ed. 55:2688–2692.
Riess, J.G. (2005) Fluorous materials for biomedical uses, in: Gladysz, J.A., Curran, D.P., Horváth, I.T., eds., Handbook
of fluorous chemistry. Wiley-VCH, Weinheim, pp. 521–573.
Ritchie, T.K., Grinkova, Y.V., Bayburt, T.H., Denisov, I.G., Zolnerciks, J.K., Atkins, W.M., Sligar, S.G. (2009)
Reconstitution of membrane proteins in phospholipid bilayer nanodiscs. Meth. Enzymol. 464:211–231.
Ritchie, T.K., Kwon, H., Atkins, W.M. (2011) Conformational analysis of human ATP-binding cassette transporter
ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2. J. Biol. Chem. 286:39489–39496.
Rodnin, M.V., Posokhov, Y.O., Contino-Pépin, C., Brettmann, J., Kyrychenko, A., Palchevskyy, S.S., Pucci, B.,
Ladokhin, A.S. (2008) Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media
for studies of membrane proteins. Biophys. J. 94:4348–4357.
References
145
Breyton, C., Bonneté, F. (2016) Sparingly fluorinated maltoside-based surfactants for membrane-protein stabilization. New J. Chem. 40:5364–5378.
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. (2010) Amphipols, nanodiscs, and fluorinated surfactants: Three non-conventional approaches to studying
membrane proteins in aqueous solutions. Annu. Rev. Biochem. 79:737–775.
Popot, J.-L., Engelman, D.M. (2000) Helical membrane protein folding, stability and evolution. Annu. Rev. Biochem.
69:881–923.
Popovic, K., Holyoake, J., Pomès, R., Privé, G.G. (2012) Structure of saposin A lipoprotein discs. Proc. Natl. Acad. Sci.
USA 109:2908–2912.
Posokhov, Y.O., Rodnin, M.V., Das, S.K., Pucci, B., Ladokhin, A.S. (2008) FCS study of the thermodynamics of
membrane protein insertion into the lipid bilayer chaperoned by fluorinated surfactants. Biophys. J. 95:L54-L56.
Poulos, S., Morgan, J.L., Zimmer, J., Faham, S. (2015) Bicelles coming of age: an empirical approach to bicelle
crystallization. Meth. Enzymol. 557:393–416.
Privé, G. (2009) Lipopeptide detergents for membrane protein studies. Curr. Opin. Struct. Biol. 19:1–7.
Prosser, R.S., Evanics, F., Kitevski, J.L., Al-Abdul-Wahid, M.S. (2006) Current applications of bicelles in NMR studies
of membrane-associated amphiphiles and proteins. Biochemistry 45:8453–8465.
Prosser, R.S., Hunt, S.A., DiNatale, J.A., Vold, R.R. (1996) Magnetically aligned membrane model systems with
positive order parameters: switching the sign of S zz with paramagnetic ions. J. Am. Chem. Soc. 118:269–270.
Prosser, R.S., Hwang, J.S., Vold, R.R. (1998) Magnetically aligned phospholipid bilayers with positive ordering: a new
model membrane system. Biophys. J. 74:2405–2418.
Proverbio, D., Roos, C., Beyermann, M., Orbán, E., Dötsch, V., Bernhard, F. (2013) Functional properties of cell-free
expressed human endothelin A and endothelin B receptors in artificial membrane environments. Biochim. Biophys.
Acta 1828:2182–2192.
Puthenveetil, R., Nguyen, K., Vinogradova, O. (2017) Nanodiscs and solution NMR: preparation, application and
challenges. Nanotech. Rev. 6:111–126.
Puthenveetil, R., Vinogradova, O. (2013) Optimization of the design and preparation of nanoscale phospholipid bilayers
for its application to solution NMR. Proteins: Struct. Funct. Bioinf. 81:1222–1231.
Qureshi, T., Goto, N.K. (2011) Contemporary methods in structure determination of membrane proteins by solution
NMR. Top. Curr. Chem. 326:123–185.
Ram, P., Prestegard, J.H. (1988) Magnetic field-induced ordering of bile salt/phospholipid micelles: new media for NMR
structural investigations. Biochim. Biophys. Acta 940:289–294.
Ramjeesingh, M., Huan, L.J., Garami, E., Bear, C.E. (1999) Novel method for evaluation of the oligomeric structure of
membrane proteins. Biochem. J. 342.
Ranaghan, M.J., Schwall, C.T., Alder, N.N., Birge, R.R. (2011) Green proteorhodopsin reconstituted into nanoscale
phospholipid bilayers (nanodiscs) as photoactive monomers. J. Am. Chem. Soc. 133:18318–18327.
Raschle, T., Hiller, S., Etzkorn, M., Wagner, G. (2010) Nonmicellar systems for solution NMR spectroscopy of
membrane proteins. Curr. Opin. Struct. Biol. 20:471–479.
Raschle, T., Hiller, S., Yu, T.Y., Rice, A.J., Walz, T., Wagner, G. (2009) Structural and functional characterization of the
integral membrane protein VDAC-1 in lipid bilayer nanodiscs. J. Am. Chem. Soc. 131:17777–17779.
Rasmussen, S.G., Choi, H.J., Rosenbaum, D.M., Kobilka, T.S., Thian, F.S., Edwards, P.C., Burghammer, M., Ratnala,
V.R., Sanishvili, R., Fischetti, R.F., Schertler, G.F., Weis, W.I., Kobilka, B.K. (2007) Crystal structure of the human
β 2 adrenergic G protein-coupled receptor. Nature 450:383–387.
Raychaudhuri, P., Li, Q., Mason, A., Mikhailova, E., Heron, A.J., Bayley, H. (2011) Fluorinated amphiphiles control the
insertion of α-hemolysin pores into lipid bilayers. Biochemistry 50:1599–1606.
Reichart, T.M., Baksh, M.M., Rhee, J.-K., Fiedler, J.D., Sligar, S.G., Finn, M.G., Zwick, M.B., Dawson, P.E. (2016)
Trimerization of the HIV transmembrane domain in lipid bilayers modulates broadly neutralizing antibody binding.
Angew. Chem. Int. Ed. 55:2688–2692.
Riess, J.G. (2005) Fluorous materials for biomedical uses, in: Gladysz, J.A., Curran, D.P., Horváth, I.T., eds., Handbook
of fluorous chemistry. Wiley-VCH, Weinheim, pp. 521–573.
Ritchie, T.K., Grinkova, Y.V., Bayburt, T.H., Denisov, I.G., Zolnerciks, J.K., Atkins, W.M., Sligar, S.G. (2009)
Reconstitution of membrane proteins in phospholipid bilayer nanodiscs. Meth. Enzymol. 464:211–231.
Ritchie, T.K., Kwon, H., Atkins, W.M. (2011) Conformational analysis of human ATP-binding cassette transporter
ABCB1 in lipid nanodiscs and inhibition by the antibodies MRK16 and UIC2. J. Biol. Chem. 286:39489–39496.
Rodnin, M.V., Posokhov, Y.O., Contino-Pépin, C., Brettmann, J., Kyrychenko, A., Palchevskyy, S.S., Pucci, B.,
Ladokhin, A.S. (2008) Interactions of fluorinated surfactants with diphtheria toxin T-domain: testing new media
for studies of membrane proteins. Biophys. J. 94:4348–4357.
References
145