Pautsch, A., Vogt, J., Model, K., Siebold, C., Schulz, G.E. (1999) Strategy for membrane protein crystallization
exemplified with OmpA and OmpX. Proteins 34:167–172.
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.
Perry, T., Souabni, H., Rapisarda, C., Fronzes, R., Giusti, F., Popot, J.-L., Zoonens, M., Gubellini, F. (2018) Visualizing
transmembrane regions of protein complexes by electron microscopy using biotinylated amphipols, submitted for
publication.
Pervushin, K.V., Riek, R., Wider, G., Wüthrich, K. (1997) Attenuated T 2 relaxation by mutual cancellation of dipoledipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological
macromolecules in solution. Proc. Natl. Acad. Sci. USA 94:12366–12371.
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.
Plesniak, L.A., Mahalakshmi, R., Rypien, C., Yang, Y., Racic, J., Marassi, F.M. (2011) Expression, refolding, and initial
structural characterization of the Y. pestis Ail outer membrane protein in lipids. Biochim. Biophys. Acta
1808:482–489.
Plevin, M.J., Boisbouvier, J. (2012) Isotope-labelling of methyl groups for NMR studies of large proteins, in: Clore, M.,
Potts, J., eds., Recent Developments in Biomolecular NMR, Royal Society of Chemistry, pp. 1–24.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
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.
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., Engelman, D.M. (2016) Membranes do not tell proteins how to fold. Biochemistry 55:5–18.
Postis, V., Rawson, S., Mitchell, J.K., Lee, S.C., Parslowc, 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.
Prestegard, J.H., Al-Hashimi, H.M., Tolman, J.R. (2000) NMR structures of biomolecules using field-oriented media and
residual dipolar couplings. Q. Rev. Biophys. 33:371–424.
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.
Puthenveetil, R., Nguyen, K., Vinogradova, O. (2017) Nanodiscs and solution NMR: preparation, application and
challenges. Nanotech. Rev. 6:111–126.
Qureshi, T., Goto, N.K. (2011) Contemporary methods in structure determination of membrane proteins by solution
NMR. Top. Curr. Chem.
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.
Rinaldi, P.L. (1983) Heteronuclear 2D-NOE spectroscopy. J. Am. Chem. Soc. 105:5167–5168.
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.
Salzmann, M., Wider, G., Pervushin, K., Wüthrich, K. (1999) Improved sensitivity and coherence selection for [
15
N,
1
H]TROSY elements in triple resonance experiments. J. Biomol. NMR 15:181–184.
Sanders, C.R., Oxenoid, K. (2000) Customizing model membranes and samples for NMR spectroscopic studies of
complex membrane proteins. Biochim. Biophys. Acta 1508:129–145.
Sanders, C.R., Prosser, R.S. (1998) Bicelles: a model membrane system for all seasons? Structure 6:1227–1234.
Sanders, C.R., Sönnichsen, F. (2006) Solution NMR of membrane proteins: practice and challenges. Magn. Reson.
Chem. 44:S24-S40.
Schweizer, M., Hindennach, I., Garten, W., Henning, U. (1978) Major proteins of the Escherichia coli outer cell
envelope membrane. Interaction of protein II with lipopolysaccharide. Eur. J. Biochem. 82:211–217.
494
10 Nuclear Magnetic Resonance Studies of Amphipol-Trapped Membrane Proteins
exemplified with OmpA and OmpX. Proteins 34:167–172.
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.
Perry, T., Souabni, H., Rapisarda, C., Fronzes, R., Giusti, F., Popot, J.-L., Zoonens, M., Gubellini, F. (2018) Visualizing
transmembrane regions of protein complexes by electron microscopy using biotinylated amphipols, submitted for
publication.
Pervushin, K.V., Riek, R., Wider, G., Wüthrich, K. (1997) Attenuated T 2 relaxation by mutual cancellation of dipoledipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological
macromolecules in solution. Proc. Natl. Acad. Sci. USA 94:12366–12371.
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.
Plesniak, L.A., Mahalakshmi, R., Rypien, C., Yang, Y., Racic, J., Marassi, F.M. (2011) Expression, refolding, and initial
structural characterization of the Y. pestis Ail outer membrane protein in lipids. Biochim. Biophys. Acta
1808:482–489.
Plevin, M.J., Boisbouvier, J. (2012) Isotope-labelling of methyl groups for NMR studies of large proteins, in: Clore, M.,
Potts, J., eds., Recent Developments in Biomolecular NMR, Royal Society of Chemistry, pp. 1–24.
Pocanschi, C.L., Dahmane, T., Gohon, Y., Rappaport, F., Apell, H.-J., Kleinschmidt, J.H., Popot, J.-L. (2006) Amphipathic polymers: tools to fold integral membrane proteins to their active form. Biochemistry 45:13954–13961.
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.
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., Engelman, D.M. (2016) Membranes do not tell proteins how to fold. Biochemistry 55:5–18.
Postis, V., Rawson, S., Mitchell, J.K., Lee, S.C., Parslowc, 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.
Prestegard, J.H., Al-Hashimi, H.M., Tolman, J.R. (2000) NMR structures of biomolecules using field-oriented media and
residual dipolar couplings. Q. Rev. Biophys. 33:371–424.
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.
Puthenveetil, R., Nguyen, K., Vinogradova, O. (2017) Nanodiscs and solution NMR: preparation, application and
challenges. Nanotech. Rev. 6:111–126.
Qureshi, T., Goto, N.K. (2011) Contemporary methods in structure determination of membrane proteins by solution
NMR. Top. Curr. Chem.
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.
Rinaldi, P.L. (1983) Heteronuclear 2D-NOE spectroscopy. J. Am. Chem. Soc. 105:5167–5168.
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.
Salzmann, M., Wider, G., Pervushin, K., Wüthrich, K. (1999) Improved sensitivity and coherence selection for [
15
N,
1
H]TROSY elements in triple resonance experiments. J. Biomol. NMR 15:181–184.
Sanders, C.R., Oxenoid, K. (2000) Customizing model membranes and samples for NMR spectroscopic studies of
complex membrane proteins. Biochim. Biophys. Acta 1508:129–145.
Sanders, C.R., Prosser, R.S. (1998) Bicelles: a model membrane system for all seasons? Structure 6:1227–1234.
Sanders, C.R., Sönnichsen, F. (2006) Solution NMR of membrane proteins: practice and challenges. Magn. Reson.
Chem. 44:S24-S40.
Schweizer, M., Hindennach, I., Garten, W., Henning, U. (1978) Major proteins of the Escherichia coli outer cell
envelope membrane. Interaction of protein II with lipopolysaccharide. Eur. J. Biochem. 82:211–217.
494
10 Nuclear Magnetic Resonance Studies of Amphipol-Trapped Membrane Proteins