Sirokmán, G., Fasman, G.D. (1993) Refolding and proton pumping activity of a polyethylene glycol-bacteriorhodopsin
water-soluble conjugate. Protein Sci. 2:1161–1170.
Slovic, A.M., Kono, H., Lear, J.D., Saven, J.G., DeGrado, W.F. (2004) Computational design of water-soluble analogues
of the potassium channel KcsA. Proc. Natl. Acad. Sci. USA 101:1828–1833.
Slovic, A.M., Lear, J.D., DeGrado, W.F. (2005a) De novo design of a pentameric coiled-coil: decoding the motif for
tetramer versus pentamer formation in water-soluble phospholamban. J. Pept. Res. 65:312–321.
Slovic, A.M., Stayrook, S.E., North, B., Degrado, W.F. (2005b) X-ray structure of a water-soluble analog of the
membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled
coils. J. Mol. Biol. 348:777–787.
Snijder, H.J., Timmins, P.A., Kalk, K.H., Dijkstra, B.W. (2003) Detergent organisation in crystals of monomeric outer
membrane phospholipase A. J. Struct. Biol. 141:122–131.
Stroebel, D., Choquet, Y., Popot, J.-L., Picot, D. (2003) An atypical haem in the cytochrome b 6 f complex. Nature
426:413–418.
Stubbs, G.W., Smith, H.G., Jr., Litman, B.J. (1976) Alkyl glucosides as effective solubilizing agents for bovine
rhodopsin. A comparison with several commonly used detergents. Biochim. Biophys. Acta 426:46–56.
Tanford, C. (1972) Micelle Shape and Size. J. Phys. Chem. 76:3020–3024.
Tanford, C. (1980) The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd ed.. Wiley,
New York, 233 p.
Tanford, C., Reynolds, J.A. (1976) Characterization of membrane proteins in detergent solutions. Biochim. Biophys. Acta
457:133–170.
Tate, C.G. (2010) Practical considerations of membrane protein instability for purification and crystallisation, in:
Mus-Veteau, I., ed., Membrane Protein Expression. The Humana Press, Totowa, New Jersey, USA, pp. 187–203.
Tate, C.G. (2012) A crystal-clear solution for determining G-protein-coupled receptor structures. Trends Biochem. Sci.
37:343–352.
Tausk, R.J.M., Karmiggelt, J., Oudshoorn, C., Overbeek, J.T.G. (1974) Physical chemical studies of short-chain lecithin
homologues. I.: Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle
concentration. Biophys. Chem. 1:175–183.
Timmins, P., Pebay-Peyroula, E., Welte, W. (1994) Detergent organisation in solutions and in crystals of membrane
proteins. Biophys. Chem. 53:27–36.
Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic
reticulum at 2.6 Å resolution. Nature 405:647–655.
Triba, M.N., Warschawski, D.E., Devaux, P.F. (2005) Reinvestigation by phosphorus NMR of lipid distribution in
bicelles. Biophys. J. 88:1887–1901.
Vaidehi, N., Grisshammer, R., Tate, C.G. (2016) How can mutations thermostabilize G protein-coupled receptors?
Trends Pharmacol. Sci. 37:37–46.
VanAken, T., Foxall-VanAken, S., Castleman, S., Ferguson-Miller, S. (1986) Alkyl glycoside detergents: synthesis and
applications to the study of membrane proteins. Methods Enzymol. 125:27–35.
Vieler, A., Wilhelm, C., Goss, R., Süss, R., Schiller, J. (2007) The lipid composition of the unicellular green alga
Chlamydomonas reinhardtii and the diatom Cyclotella meneghiniana investigated by MALDI-TOF MS and TLC.
Chem. Phys. Lipids 150:143–155.
Wang, C., Deber, C.M. (2000) Peptide mimics of the M13 coat protein transmembrane segment. Retention of helix-helix
interaction motifs. J. Biol. Chem. 275:16155–16159.
Warne, T., Serrano-Vega, M.J., Baker, J.G., Moukhametzianov, R., Edwards, P.C., Henderson, R., Leslie, A.G.W., Tate,
C.G., Schertler, G.F.X. (2008) Structure of a β 1 -adrenergic G protein-coupled receptor. Nature 454:486–491.
Warr, G.G., Drummond, C.J., Grieser, F., Ninham, B.W., Evans, D.F. (1986) Aqueous solution properties of nonionic ndodecyl-β-D-maltoside micelles. J. Phys. Chem. 90:4581–4586.
Wei, J., Fasman, G.D. (1995) A poly(ethylene glycol) water-soluble conjugate of porin: refolding to the native state.
Biochemistry 34:6408–6415.
Wiener, M.C. (2004) A pedestrian guide to membrane protein crystallization. Methods 34:364–372.
Yu, S.M., McQuade, D.T., Quinn, M.A., Hackenberger, C.P., Krebs, M.P., Polans, A.S., Gellman, S.H. (2000) An
improved tripod amphiphile for membrane protein solubilization. Protein Sci. 9:2518–2527.
Zhang, Q., Ma, X., Ward, A., Hong, W.X., Jaakola, V.P., Stevens, R.C., Finn, M.G., Chang, G. (2007) Designing facial
amphiphiles for the stabilization of integral membrane proteins. Angew. Chem. Int. Ed. Engl. 46:7023–7025.
Zhang, Q., Tao, H., Hong, W.-X. (2011) New amphiphiles for membrane protein structural biology. Methods
55:318–323.
Zhao, X., Perez-Aguilar, J.M., Matsunaga, F., Lerner, M., Xi, J., Selling, B., Johnson, A.T., Jr., Saven, J.G., Liu,
R. (2014) Characterization of a computationally designed water-soluble human μ-opioid receptor variant using
available structural information. Anesthesiology 121:866–875.
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2 Extracting Membrane Proteins from Their Native Environment
water-soluble conjugate. Protein Sci. 2:1161–1170.
Slovic, A.M., Kono, H., Lear, J.D., Saven, J.G., DeGrado, W.F. (2004) Computational design of water-soluble analogues
of the potassium channel KcsA. Proc. Natl. Acad. Sci. USA 101:1828–1833.
Slovic, A.M., Lear, J.D., DeGrado, W.F. (2005a) De novo design of a pentameric coiled-coil: decoding the motif for
tetramer versus pentamer formation in water-soluble phospholamban. J. Pept. Res. 65:312–321.
Slovic, A.M., Stayrook, S.E., North, B., Degrado, W.F. (2005b) X-ray structure of a water-soluble analog of the
membrane protein phospholamban: sequence determinants defining the topology of tetrameric and pentameric coiled
coils. J. Mol. Biol. 348:777–787.
Snijder, H.J., Timmins, P.A., Kalk, K.H., Dijkstra, B.W. (2003) Detergent organisation in crystals of monomeric outer
membrane phospholipase A. J. Struct. Biol. 141:122–131.
Stroebel, D., Choquet, Y., Popot, J.-L., Picot, D. (2003) An atypical haem in the cytochrome b 6 f complex. Nature
426:413–418.
Stubbs, G.W., Smith, H.G., Jr., Litman, B.J. (1976) Alkyl glucosides as effective solubilizing agents for bovine
rhodopsin. A comparison with several commonly used detergents. Biochim. Biophys. Acta 426:46–56.
Tanford, C. (1972) Micelle Shape and Size. J. Phys. Chem. 76:3020–3024.
Tanford, C. (1980) The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd ed.. Wiley,
New York, 233 p.
Tanford, C., Reynolds, J.A. (1976) Characterization of membrane proteins in detergent solutions. Biochim. Biophys. Acta
457:133–170.
Tate, C.G. (2010) Practical considerations of membrane protein instability for purification and crystallisation, in:
Mus-Veteau, I., ed., Membrane Protein Expression. The Humana Press, Totowa, New Jersey, USA, pp. 187–203.
Tate, C.G. (2012) A crystal-clear solution for determining G-protein-coupled receptor structures. Trends Biochem. Sci.
37:343–352.
Tausk, R.J.M., Karmiggelt, J., Oudshoorn, C., Overbeek, J.T.G. (1974) Physical chemical studies of short-chain lecithin
homologues. I.: Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle
concentration. Biophys. Chem. 1:175–183.
Timmins, P., Pebay-Peyroula, E., Welte, W. (1994) Detergent organisation in solutions and in crystals of membrane
proteins. Biophys. Chem. 53:27–36.
Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic
reticulum at 2.6 Å resolution. Nature 405:647–655.
Triba, M.N., Warschawski, D.E., Devaux, P.F. (2005) Reinvestigation by phosphorus NMR of lipid distribution in
bicelles. Biophys. J. 88:1887–1901.
Vaidehi, N., Grisshammer, R., Tate, C.G. (2016) How can mutations thermostabilize G protein-coupled receptors?
Trends Pharmacol. Sci. 37:37–46.
VanAken, T., Foxall-VanAken, S., Castleman, S., Ferguson-Miller, S. (1986) Alkyl glycoside detergents: synthesis and
applications to the study of membrane proteins. Methods Enzymol. 125:27–35.
Vieler, A., Wilhelm, C., Goss, R., Süss, R., Schiller, J. (2007) The lipid composition of the unicellular green alga
Chlamydomonas reinhardtii and the diatom Cyclotella meneghiniana investigated by MALDI-TOF MS and TLC.
Chem. Phys. Lipids 150:143–155.
Wang, C., Deber, C.M. (2000) Peptide mimics of the M13 coat protein transmembrane segment. Retention of helix-helix
interaction motifs. J. Biol. Chem. 275:16155–16159.
Warne, T., Serrano-Vega, M.J., Baker, J.G., Moukhametzianov, R., Edwards, P.C., Henderson, R., Leslie, A.G.W., Tate,
C.G., Schertler, G.F.X. (2008) Structure of a β 1 -adrenergic G protein-coupled receptor. Nature 454:486–491.
Warr, G.G., Drummond, C.J., Grieser, F., Ninham, B.W., Evans, D.F. (1986) Aqueous solution properties of nonionic ndodecyl-β-D-maltoside micelles. J. Phys. Chem. 90:4581–4586.
Wei, J., Fasman, G.D. (1995) A poly(ethylene glycol) water-soluble conjugate of porin: refolding to the native state.
Biochemistry 34:6408–6415.
Wiener, M.C. (2004) A pedestrian guide to membrane protein crystallization. Methods 34:364–372.
Yu, S.M., McQuade, D.T., Quinn, M.A., Hackenberger, C.P., Krebs, M.P., Polans, A.S., Gellman, S.H. (2000) An
improved tripod amphiphile for membrane protein solubilization. Protein Sci. 9:2518–2527.
Zhang, Q., Ma, X., Ward, A., Hong, W.X., Jaakola, V.P., Stevens, R.C., Finn, M.G., Chang, G. (2007) Designing facial
amphiphiles for the stabilization of integral membrane proteins. Angew. Chem. Int. Ed. Engl. 46:7023–7025.
Zhang, Q., Tao, H., Hong, W.-X. (2011) New amphiphiles for membrane protein structural biology. Methods
55:318–323.
Zhao, X., Perez-Aguilar, J.M., Matsunaga, F., Lerner, M., Xi, J., Selling, B., Johnson, A.T., Jr., Saven, J.G., Liu,
R. (2014) Characterization of a computationally designed water-soluble human μ-opioid receptor variant using
available structural information. Anesthesiology 121:866–875.
94
2 Extracting Membrane Proteins from Their Native Environment