Nehmé, R., Joubert, O., Bidet, M., Lacombe, B., Polidori, A., Pucci, B., Mus-Veteau, I. (2010) Stability study of the
human G protein-coupled receptor, Smoothened. Biochim. Biophys. Acta 1786:1100–1110.
Nietlispach, D., Gautier, A. (2011) Solution NMR studies of polytopic alpha-helical membrane proteins. Curr. Opin.
Struct. Biol. 21:497–508.
Nikolaev, M., Round, E., Gushchin, I., Polovinkin, V., Balandin, T., Kuzmichev, P., Shevchenko, V., Borshchevskiy,
V., Kuklin, A., Round, A., Bernhard, F., Willbold, D., Büldt, G., Gordeliy, V. (2017) Integral membrane proteins can
be crystallized directly from nanodiscs. Cryst. Growth Des. 17:945–948.
Noinaj, N., Kuszak, A.J., Gumbart, J.C., Lukacik, P., Chang, H., Easley, N.C., Lithgow, T., Buchanan, S.K. (2013)
Structural insight into the biogenesis of β-barrel membrane proteins. Nature 501:385–390.
Nolte, R.T., Atkinson, D. (1992) Conformational analysis of apolipoproteins A-I and E-3 based on primary sequence and
circular dichroism. Biophys. J. 63:1221–1239.
Nusair, N.A., Mayo, D.J., Dorozenski, T.D., Cardon, T.B., Inbaraj, J.J., Karp, E.S., Newstadt, J.P., Grosser, S.M.,
Lorigan, G.A. (2012) Time-resolved EPR immersion depth studies of a transmembrane peptide incorporated into
bicelles. Biochim. Biophys. Acta 1818:821–828.
Opella, S.J., Marassi, F.M. (2004) Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev.
104:3587–3606.
Otzen, D.E. (2015) Proteins in a brave new surfactant world. Curr. Opin. Colloid Interface Sci. 20:161–169.
Palchevskyy, S.S., Posokhov, Y.O., Olivier, B., Popot, J.-L., Pucci, B., Ladokhin, A.S. (2006) Chaperoning of
membrane protein insertion into lipid bilayers by hemifluorinated surfactants: application to diphtheria toxin.
Biochemistry 45:2629–2635.
Park, K.-H., Berrier, C., Lebaupain, F., Pucci, B., Popot, J.-L., Ghazi, A., Zito, F. (2007) Fluorinated and hemifluorinated
surfactants as alternatives to detergents for membrane protein cell-free synthesis. Biochem. J. 403:183–187.
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.
Park, S.H., Berkamp, S., Cook, G.A., Chan, M.K., Viadiu, H., Opella, S.J. (2011a) Nanodiscs versus macrodiscs for
NMR of membrane proteins. Biochemistry 50:8983–8985.
Park, S.H., Casagrande, F., Cho, L., Albrecht, L., Opella, S.J. (2011b) Interactions of interleukin-8 with the human
chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy. J. Mol. Biol. 414:194–203.
Park, S.H., Casagrande, F., Das, B.B., Albrecht, L., Chu, M., Opella, S.J. (2011c) Local and global dynamics of the G
protein-coupled receptor CXCR1. Biochemistry 50:2371–2380.
Park, S.H., Das, B.B., Casagrande, F., Tian, Y., Nothnagel, H.J., Chu, M., Kiefer, H., Maier, K., De Angelis, A.A.,
Marassi, F.M., Opella, S.J. (2012) Structure of the chemokine receptor CXCR1 in phospholipid bilayers. Nature
491:770–783.
Park, S.H., Prytulla, S., De Angelis, A.A., Brown, J.M., Kiefer, H., Opella, S.J. (2006) High-resolution NMR spectroscopy of a GPCR in aligned bicelles. J. Am. Chem. Soc. 128:7402–7403.
Pavia, A.A., Pucci, B., Riess, J.G., Zarif, L. (1991) New fluorinated biocompatible non-ionic telomeric amphiphiles
bearing trishydroxymethyl groups. Bioorg. Med. Chem. Letters 1:103–106.
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.
Peters, B.M., Shirtliff, M.E., Jabra-Rizk, M.A. (2010) Antimicrobial peptides: Primeval molecules or future drugs? PLoS
Pathog. 6:e1001067.
Petkova, V., Benattar, J.J., Zoonens, M., Zito, F., Popot, J.-L., Polidori, A., Jasseron, S., Pucci, B. (2007) Free-standing
films of fluorinated surfactants as 2D matrices for organizing detergent-solubilized membrane proteins. Langmuir
23:4303–4309.
Phillips, J.C., Wriggers, W., Li, Z., Jonas, A., Schulten, K. (1997) Predicting the structure of apolipoprotein A-I in
reconstituted high-density lipoprotein disks. Biophys. J. 73:2337–2346.
Phillips, M.C. (2013) New insights into the determination of HDL structure by apolipoproteins. J. Lipid Res.
54:2034–2048.
Poget, S.F., Cahill, S.M., Girvin, M.E. (2007) Isotropic bicelles stabilize the functional form of a small multidrugresistance pump for NMR structural studies. J. Am. Chem. Soc. 129:2432–2433.
Poget, S.F., Girvin, M.E. (2007) Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but
sometimes bigger is better. Biochim. Biophys. Acta 1768:3098–3106.
Polidori, A., Presset, M., Lebaupain, F., Améduri, B., Popot, J.-L., Breyton, C., Pucci, B. (2006) Fluorinated and
hemifluorinated surfactants derived from maltose: Synthesis and application to handling membrane proteins in
aqueous solution. Bioorg. Med. Chem. Lett. 16:5827–5831.
144
3 Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions
human G protein-coupled receptor, Smoothened. Biochim. Biophys. Acta 1786:1100–1110.
Nietlispach, D., Gautier, A. (2011) Solution NMR studies of polytopic alpha-helical membrane proteins. Curr. Opin.
Struct. Biol. 21:497–508.
Nikolaev, M., Round, E., Gushchin, I., Polovinkin, V., Balandin, T., Kuzmichev, P., Shevchenko, V., Borshchevskiy,
V., Kuklin, A., Round, A., Bernhard, F., Willbold, D., Büldt, G., Gordeliy, V. (2017) Integral membrane proteins can
be crystallized directly from nanodiscs. Cryst. Growth Des. 17:945–948.
Noinaj, N., Kuszak, A.J., Gumbart, J.C., Lukacik, P., Chang, H., Easley, N.C., Lithgow, T., Buchanan, S.K. (2013)
Structural insight into the biogenesis of β-barrel membrane proteins. Nature 501:385–390.
Nolte, R.T., Atkinson, D. (1992) Conformational analysis of apolipoproteins A-I and E-3 based on primary sequence and
circular dichroism. Biophys. J. 63:1221–1239.
Nusair, N.A., Mayo, D.J., Dorozenski, T.D., Cardon, T.B., Inbaraj, J.J., Karp, E.S., Newstadt, J.P., Grosser, S.M.,
Lorigan, G.A. (2012) Time-resolved EPR immersion depth studies of a transmembrane peptide incorporated into
bicelles. Biochim. Biophys. Acta 1818:821–828.
Opella, S.J., Marassi, F.M. (2004) Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev.
104:3587–3606.
Otzen, D.E. (2015) Proteins in a brave new surfactant world. Curr. Opin. Colloid Interface Sci. 20:161–169.
Palchevskyy, S.S., Posokhov, Y.O., Olivier, B., Popot, J.-L., Pucci, B., Ladokhin, A.S. (2006) Chaperoning of
membrane protein insertion into lipid bilayers by hemifluorinated surfactants: application to diphtheria toxin.
Biochemistry 45:2629–2635.
Park, K.-H., Berrier, C., Lebaupain, F., Pucci, B., Popot, J.-L., Ghazi, A., Zito, F. (2007) Fluorinated and hemifluorinated
surfactants as alternatives to detergents for membrane protein cell-free synthesis. Biochem. J. 403:183–187.
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.
Park, S.H., Berkamp, S., Cook, G.A., Chan, M.K., Viadiu, H., Opella, S.J. (2011a) Nanodiscs versus macrodiscs for
NMR of membrane proteins. Biochemistry 50:8983–8985.
Park, S.H., Casagrande, F., Cho, L., Albrecht, L., Opella, S.J. (2011b) Interactions of interleukin-8 with the human
chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy. J. Mol. Biol. 414:194–203.
Park, S.H., Casagrande, F., Das, B.B., Albrecht, L., Chu, M., Opella, S.J. (2011c) Local and global dynamics of the G
protein-coupled receptor CXCR1. Biochemistry 50:2371–2380.
Park, S.H., Das, B.B., Casagrande, F., Tian, Y., Nothnagel, H.J., Chu, M., Kiefer, H., Maier, K., De Angelis, A.A.,
Marassi, F.M., Opella, S.J. (2012) Structure of the chemokine receptor CXCR1 in phospholipid bilayers. Nature
491:770–783.
Park, S.H., Prytulla, S., De Angelis, A.A., Brown, J.M., Kiefer, H., Opella, S.J. (2006) High-resolution NMR spectroscopy of a GPCR in aligned bicelles. J. Am. Chem. Soc. 128:7402–7403.
Pavia, A.A., Pucci, B., Riess, J.G., Zarif, L. (1991) New fluorinated biocompatible non-ionic telomeric amphiphiles
bearing trishydroxymethyl groups. Bioorg. Med. Chem. Letters 1:103–106.
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.
Peters, B.M., Shirtliff, M.E., Jabra-Rizk, M.A. (2010) Antimicrobial peptides: Primeval molecules or future drugs? PLoS
Pathog. 6:e1001067.
Petkova, V., Benattar, J.J., Zoonens, M., Zito, F., Popot, J.-L., Polidori, A., Jasseron, S., Pucci, B. (2007) Free-standing
films of fluorinated surfactants as 2D matrices for organizing detergent-solubilized membrane proteins. Langmuir
23:4303–4309.
Phillips, J.C., Wriggers, W., Li, Z., Jonas, A., Schulten, K. (1997) Predicting the structure of apolipoprotein A-I in
reconstituted high-density lipoprotein disks. Biophys. J. 73:2337–2346.
Phillips, M.C. (2013) New insights into the determination of HDL structure by apolipoproteins. J. Lipid Res.
54:2034–2048.
Poget, S.F., Cahill, S.M., Girvin, M.E. (2007) Isotropic bicelles stabilize the functional form of a small multidrugresistance pump for NMR structural studies. J. Am. Chem. Soc. 129:2432–2433.
Poget, S.F., Girvin, M.E. (2007) Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but
sometimes bigger is better. Biochim. Biophys. Acta 1768:3098–3106.
Polidori, A., Presset, M., Lebaupain, F., Améduri, B., Popot, J.-L., Breyton, C., Pucci, B. (2006) Fluorinated and
hemifluorinated surfactants derived from maltose: Synthesis and application to handling membrane proteins in
aqueous solution. Bioorg. Med. Chem. Lett. 16:5827–5831.
144
3 Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions