Roos, C., Zocher, M., Müller, D., Münch, D., Schneider, T., Sahl, H.G., Scholz, F., Wachtveitl, J., Ma, Y., Proverbio, D.,
Henrich, E., Dötsch, V., Bernhard, F. (2012) Characterization of co-translationally formed nanodisc complexes with
small multidrug transporters, proteorhodopsin and with the E. coli MraY translocase. Biochim. Biophys. Acta
1818:3898–3106.
Roy, J., Pondenis, H., Fan, T.M., Das, A. (2015) Direct capture of functional proteins from mammalian plasma
membranes into nanodiscs. Biochemistry 54:6299–6302.
Rues, R.-B., Dötsch, V., Bernhard, F. (2016) Co-translational formation and pharmacological characterization of βadrenergic receptor/nanodisc complexes with different lipid environments. Biochim. Biophys. Acta 1858:1306–1316.
Sanders, C.R. (2008) Development and application of bicelles for use in biological NMR and other biophysical studies,
in: Webb, G.A., ed., Modern Magnetic Resonance. Springer, Dordrecht, pp. 233–239.
Sanders, C.R., Prosser, R.S. (1998) Bicelles: a model membrane system for all seasons? Structure 6:1227–1234.
Sanders, C.R., Schwonek, J.P. (1992) Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR. Biochemistry 31:8898–8905.
Sanders, C.R., Sönnichsen, F. (2006) Solution NMR of membrane proteins: practice and challenges. Magn. Reson.
Chem. 44:S24–S40.
Sanders II, C.R., Hare, B.J., Howard, K.P., Prestegard, J.H. (1994) Magnetically-oriented phospholipid micelles as a tool
for the study of membrane-associated molecules. Prog. NMR Spectrosc. 26:421–444.
Sanders II, C.R., Landis, G.C. (1995) Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for
NMR studies. Biochemistry 34:4030–4040.
Sanders II, C.R., Prestegard, J.H. (1990) Magnetically orientable phospholipid bilayers containing small amounts of a
bile salt analogue, CHAPSO. Biophys. J. 58:447–460.
Sanii, L.S., El-Sayed, M.A. (2005) Partial dehydration of the retinal binding pocket and proof for photochemical
deprotonation of the retinal Schiff base in bicelle bacteriorhodopsin crystals. Photochem. Photobiol. 81:1356–1360.
Sanii, L.S., Schill, A.W., Moran, C.E., El-Sayed, M.A. (2005) The protonation-deprotonation kinetics of the protonated
Schiff base in bicelle bacteriorhodopsin crystals. Biophys. J. 89:444–451.
Santoso, S., Hwang, W., Hartman, H., Zhang, S. (2002) Self-assembly of surfactant-like peptides with variable glycine
tails to form nanotubes and nanovesicles. Nano Lett. 2:687–691.
Schafmeister, C.E., Miercke, L.J.W., Stroud, R.A. (1993) Structure at 2.5 Å of a designed peptide that maintains
solubility of membrane proteins. Science 262:734–738.
Schoch, G.A., Attias, R., Belghazi, M., Dansette, P.M., Werck-Reichhart, D. (2003) Engineering of a water-soluble plant
cytochrome P450, CYP73A1, and NMR-based orientation of natural and alternate substrates in the active site. Plant
Physiol. 133:1198–1208.
Segrest, J.P., Jones, M.K., Klon, A.E., Sheldahl, C.J., Hellinger, M., De Loof, H., Harvey, S.C. (1999) A detailed
molecular belt model for apolipoprotein A-I in discoidal high-density lipoprotein. J. Biol. Chem. 274:31755–31758.
Serebryany, E., Zhu, G.A., Yan, E.C.Y. (2012) Artificial membrane-like environments for in vitro studies of purified
G-protein coupled receptors. Biochim. Biophys. Acta 1818:225–233.
Sevugan Chetty, P., Mayne, L., Kan, Z.Y., Lund-Katz, S., Englander, S.W., Phillips, M.C. (2012) Apolipoprotein A-I
helical structure and stability in discoidal high density lipoprotein (HDL) particles by hydrogen exchange and mass
spectrometry. Proc. Natl. Acad. Sci. USA 109:11687–11692.
Shaw, A.W., McLean, M.A., Sligar, S.G. (2004) Phospholipid phase transitions in homogeneous nanometer scale
bilayers discs. FEBS Lett. 556:260–264.
Shaw, A.W., Pureza, V.S., Sligar, S.G., Morrissey, J.H. (2007) The local phospholipid environment modulates the
activation of blood clotting. J. Biol. Chem. 282:6556–6563.
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.
Shenkarev, Z.O., Lyukmanova, E.N., Butenko, I.O., Petrovskaya, L.E., Paramonov, A.S., Shulepko, M.A., Nekrasova,
O.V., Kirpichnikov, M.P., Arseniev, A.S. (2013) Lipid-protein nanodiscs promote in vitro folding of transmembrane
domains of multi-helical and multimeric membrane proteins. Biochim. Biophys. Acta 1828:776–784.
Shenkarev, Z.O., Lyukmanova, E.N., Paramonov, A.S., Shingarova, L.N., Chupin, V.V., Kirpichnikov, M.P.,
Blommers, M.J., Arseniev, A.S. (2010) Lipid-protein nanodiscs as reference medium in detergent screening for
high-resolution NMR studies of integral membrane proteins. J. Am. Chem. Soc. 132:5628–5629.
Shepherd, F.H., Holzenburg, A. (1995) The potential of fluorinated surfactants in membrane biochemistry. Anal.
Biochem. 224:21–27.
Shi, L., Howan, K., Shen, Q.T., Wang, Y.J., Rothman, J.E., Pincet, F. (2013) Preparation and characterization of
SNARE-containing nanodiscs and direct study of cargo release through fusion pores. Nat. Protoc. 8:935–948.
Shi, L., Shen, Q.T., Kiel, A., Wang, J., Wang, H.W., Melia, T.J., Rothman, J.E., Pincet, F. (2012) SNARE proteins: one
to fuse and three to keep the nascent fusion pore open. Science 335:1355–1359.
Shih, A.Y., Denisov, I.G., Phillips, J.C., Sligar, S.G., Schulten, K. (2005) Molecular dynamics simulations of discoidal
bilayers assembled from truncated human lipoproteins. Biophys. J. 88:548–556.
146
3 Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions
Henrich, E., Dötsch, V., Bernhard, F. (2012) Characterization of co-translationally formed nanodisc complexes with
small multidrug transporters, proteorhodopsin and with the E. coli MraY translocase. Biochim. Biophys. Acta
1818:3898–3106.
Roy, J., Pondenis, H., Fan, T.M., Das, A. (2015) Direct capture of functional proteins from mammalian plasma
membranes into nanodiscs. Biochemistry 54:6299–6302.
Rues, R.-B., Dötsch, V., Bernhard, F. (2016) Co-translational formation and pharmacological characterization of βadrenergic receptor/nanodisc complexes with different lipid environments. Biochim. Biophys. Acta 1858:1306–1316.
Sanders, C.R. (2008) Development and application of bicelles for use in biological NMR and other biophysical studies,
in: Webb, G.A., ed., Modern Magnetic Resonance. Springer, Dordrecht, pp. 233–239.
Sanders, C.R., Prosser, R.S. (1998) Bicelles: a model membrane system for all seasons? Structure 6:1227–1234.
Sanders, C.R., Schwonek, J.P. (1992) Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR. Biochemistry 31:8898–8905.
Sanders, C.R., Sönnichsen, F. (2006) Solution NMR of membrane proteins: practice and challenges. Magn. Reson.
Chem. 44:S24–S40.
Sanders II, C.R., Hare, B.J., Howard, K.P., Prestegard, J.H. (1994) Magnetically-oriented phospholipid micelles as a tool
for the study of membrane-associated molecules. Prog. NMR Spectrosc. 26:421–444.
Sanders II, C.R., Landis, G.C. (1995) Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for
NMR studies. Biochemistry 34:4030–4040.
Sanders II, C.R., Prestegard, J.H. (1990) Magnetically orientable phospholipid bilayers containing small amounts of a
bile salt analogue, CHAPSO. Biophys. J. 58:447–460.
Sanii, L.S., El-Sayed, M.A. (2005) Partial dehydration of the retinal binding pocket and proof for photochemical
deprotonation of the retinal Schiff base in bicelle bacteriorhodopsin crystals. Photochem. Photobiol. 81:1356–1360.
Sanii, L.S., Schill, A.W., Moran, C.E., El-Sayed, M.A. (2005) The protonation-deprotonation kinetics of the protonated
Schiff base in bicelle bacteriorhodopsin crystals. Biophys. J. 89:444–451.
Santoso, S., Hwang, W., Hartman, H., Zhang, S. (2002) Self-assembly of surfactant-like peptides with variable glycine
tails to form nanotubes and nanovesicles. Nano Lett. 2:687–691.
Schafmeister, C.E., Miercke, L.J.W., Stroud, R.A. (1993) Structure at 2.5 Å of a designed peptide that maintains
solubility of membrane proteins. Science 262:734–738.
Schoch, G.A., Attias, R., Belghazi, M., Dansette, P.M., Werck-Reichhart, D. (2003) Engineering of a water-soluble plant
cytochrome P450, CYP73A1, and NMR-based orientation of natural and alternate substrates in the active site. Plant
Physiol. 133:1198–1208.
Segrest, J.P., Jones, M.K., Klon, A.E., Sheldahl, C.J., Hellinger, M., De Loof, H., Harvey, S.C. (1999) A detailed
molecular belt model for apolipoprotein A-I in discoidal high-density lipoprotein. J. Biol. Chem. 274:31755–31758.
Serebryany, E., Zhu, G.A., Yan, E.C.Y. (2012) Artificial membrane-like environments for in vitro studies of purified
G-protein coupled receptors. Biochim. Biophys. Acta 1818:225–233.
Sevugan Chetty, P., Mayne, L., Kan, Z.Y., Lund-Katz, S., Englander, S.W., Phillips, M.C. (2012) Apolipoprotein A-I
helical structure and stability in discoidal high density lipoprotein (HDL) particles by hydrogen exchange and mass
spectrometry. Proc. Natl. Acad. Sci. USA 109:11687–11692.
Shaw, A.W., McLean, M.A., Sligar, S.G. (2004) Phospholipid phase transitions in homogeneous nanometer scale
bilayers discs. FEBS Lett. 556:260–264.
Shaw, A.W., Pureza, V.S., Sligar, S.G., Morrissey, J.H. (2007) The local phospholipid environment modulates the
activation of blood clotting. J. Biol. Chem. 282:6556–6563.
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.
Shenkarev, Z.O., Lyukmanova, E.N., Butenko, I.O., Petrovskaya, L.E., Paramonov, A.S., Shulepko, M.A., Nekrasova,
O.V., Kirpichnikov, M.P., Arseniev, A.S. (2013) Lipid-protein nanodiscs promote in vitro folding of transmembrane
domains of multi-helical and multimeric membrane proteins. Biochim. Biophys. Acta 1828:776–784.
Shenkarev, Z.O., Lyukmanova, E.N., Paramonov, A.S., Shingarova, L.N., Chupin, V.V., Kirpichnikov, M.P.,
Blommers, M.J., Arseniev, A.S. (2010) Lipid-protein nanodiscs as reference medium in detergent screening for
high-resolution NMR studies of integral membrane proteins. J. Am. Chem. Soc. 132:5628–5629.
Shepherd, F.H., Holzenburg, A. (1995) The potential of fluorinated surfactants in membrane biochemistry. Anal.
Biochem. 224:21–27.
Shi, L., Howan, K., Shen, Q.T., Wang, Y.J., Rothman, J.E., Pincet, F. (2013) Preparation and characterization of
SNARE-containing nanodiscs and direct study of cargo release through fusion pores. Nat. Protoc. 8:935–948.
Shi, L., Shen, Q.T., Kiel, A., Wang, J., Wang, H.W., Melia, T.J., Rothman, J.E., Pincet, F. (2012) SNARE proteins: one
to fuse and three to keep the nascent fusion pore open. Science 335:1355–1359.
Shih, A.Y., Denisov, I.G., Phillips, J.C., Sligar, S.G., Schulten, K. (2005) Molecular dynamics simulations of discoidal
bilayers assembled from truncated human lipoproteins. Biophys. J. 88:548–556.
146
3 Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions