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.
Palmgren, M.G., Nissen, P. (2011) P-Type ATPases. Annu. Rev. Biophys. 40:243–266.
Park, K.-H., Billon-Denis, E., Dahmane, T., Lebaupain, F., Pucci, B., Breyton, C., Zito, F. (2011) In the cauldron of cellfree synthesis of membrane proteins: Playing with new surfactants. New Biotech. 28:255–261.
Paulin, S., Jamshad, M., Dafforn, T.R., Garcia-Lara, J., Foster, S.J., Galley, N.F., Roper, D.I., Rosado, H., Taylor,
P.W. (2014) Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a. Nanotechnology 25:285101.
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.
Periasamy, A., Shadiac, N., Amalraj, A., Garajová, S., Nagarajan, Y., Waters, S., Mertens, H.D.T., Hrmova, M. (2013)
Cell-free protein synthesis of membrane (1,3)-β-D-glucan (curdlan) synthase: co-translational insertion in liposomes
and reconstitution in nanodiscs. Biochim. Biophys. Acta 1828:743–757.
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., Popot, J.-L., Sachs, J.N. (2014) Molecular dynamics simulations of a membrane protein/amphipol
complex. J. Membr. Biol. 247:883–895.
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.
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.
Pocanschi, C., Popot, J.-L., Kleinschmidt, J.H. (2013) Folding and stability of outer membrane protein A (OmpA) from
Escherichia coli in an amphipathic polymer, amphipol A8-35. Eur. Biophys. J. 42:103–118.
Pocanschi, C.L., Apell, H.-J., Puntervoll, P., Høgh, B.T., Jensen, H.B., Welte, W., Kleinschmidt, J.H. (2006a) Folding
and membrane insertion of the major outer membrane protein of Fusobacterium nucleatum (FomA). J. Mol. Biol.
355:548–561.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006b)
Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
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. (2014a) Nanoparticle surface-enhanced Raman scattering
of bacteriorhodopsin stabilized by amphipol A8-35. J. Membr. Biol. 247:971–980.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014b) 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. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., Althoff, T., Bagnard, D., Banères, J.-L., Bazzacco, P., Billon-Denis, E., Catoire, L.J., Champeil, P.,
Charvolin, D., Cocco, M.J., Crémel, G., Dahmane, T., de la Maza, L.M., Ebel, C., Gabel, F., Giusti, F., Gohon,
Y., Goormaghtigh, E., Guittet, E., Kleinschmidt, J.H., Kühlbrandt, W., Le Bon, C., Martinez, K.L., Picard, M., Pucci,
B., Rappaport, F., Sachs, J.N., Tribet, C., van Heijenoort, C., Wien, F., Zito, F., Zoonens, M. (2011) Amphipols from
A to Z. Annu. Rev. Biophys. 40:379–408.
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.
Prabudiansyah, I., Kusters, I., Caforio, A., Driessen, A.J.M. (2015) Characterization of the annular lipid shell of the Sec
translocon. Biochim. Biophys. Acta 1848:2050–2056.
References
329
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.
Palmgren, M.G., Nissen, P. (2011) P-Type ATPases. Annu. Rev. Biophys. 40:243–266.
Park, K.-H., Billon-Denis, E., Dahmane, T., Lebaupain, F., Pucci, B., Breyton, C., Zito, F. (2011) In the cauldron of cellfree synthesis of membrane proteins: Playing with new surfactants. New Biotech. 28:255–261.
Paulin, S., Jamshad, M., Dafforn, T.R., Garcia-Lara, J., Foster, S.J., Galley, N.F., Roper, D.I., Rosado, H., Taylor,
P.W. (2014) Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a. Nanotechnology 25:285101.
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.
Periasamy, A., Shadiac, N., Amalraj, A., Garajová, S., Nagarajan, Y., Waters, S., Mertens, H.D.T., Hrmova, M. (2013)
Cell-free protein synthesis of membrane (1,3)-β-D-glucan (curdlan) synthase: co-translational insertion in liposomes
and reconstitution in nanodiscs. Biochim. Biophys. Acta 1828:743–757.
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., Popot, J.-L., Sachs, J.N. (2014) Molecular dynamics simulations of a membrane protein/amphipol
complex. J. Membr. Biol. 247:883–895.
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.
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.
Pocanschi, C., Popot, J.-L., Kleinschmidt, J.H. (2013) Folding and stability of outer membrane protein A (OmpA) from
Escherichia coli in an amphipathic polymer, amphipol A8-35. Eur. Biophys. J. 42:103–118.
Pocanschi, C.L., Apell, H.-J., Puntervoll, P., Høgh, B.T., Jensen, H.B., Welte, W., Kleinschmidt, J.H. (2006a) Folding
and membrane insertion of the major outer membrane protein of Fusobacterium nucleatum (FomA). J. Mol. Biol.
355:548–561.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006b)
Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
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. (2014a) Nanoparticle surface-enhanced Raman scattering
of bacteriorhodopsin stabilized by amphipol A8-35. J. Membr. Biol. 247:971–980.
Polovinkin, V., Gushchin, I., Balandin, T., Chervakov, P., Round, E., Shevchenko, V., Popov, A., Borshchevskiy, V.,
Popot, J.-L., Gordeliy, V. (2014b) 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. (2014) Folding membrane proteins in vitro: A table and some comments. Arch. Biochem. Biophys.
564:314–326.
Popot, J.-L., Althoff, T., Bagnard, D., Banères, J.-L., Bazzacco, P., Billon-Denis, E., Catoire, L.J., Champeil, P.,
Charvolin, D., Cocco, M.J., Crémel, G., Dahmane, T., de la Maza, L.M., Ebel, C., Gabel, F., Giusti, F., Gohon,
Y., Goormaghtigh, E., Guittet, E., Kleinschmidt, J.H., Kühlbrandt, W., Le Bon, C., Martinez, K.L., Picard, M., Pucci,
B., Rappaport, F., Sachs, J.N., Tribet, C., van Heijenoort, C., Wien, F., Zito, F., Zoonens, M. (2011) Amphipols from
A to Z. Annu. Rev. Biophys. 40:379–408.
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.
Prabudiansyah, I., Kusters, I., Caforio, A., Driessen, A.J.M. (2015) Characterization of the annular lipid shell of the Sec
translocon. Biochim. Biophys. Acta 1848:2050–2056.
References
329