Deber, C.M., Khan, A.R., Li, Z., Joensson, C., Glibowicka, M., Wang, J. (1993) Val ! Ala mutations selectively alter
helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Nat. Acad. Sci. USA
90:11648–11652.
DeGrado, W.F., Gratkowski, H., Lear, J.D. (2003) How do helix-helix interactions help determine the folds of membrane
proteins? Perspectives from the study of homo-oligomeric helical bundles. Protein Sci. 12:647–665.
Dodevski, I., Plückthun, A. (2011) Evolution of three human GPCRs for higher expression and stability. J. Mol. Biol.
408:599–615.
Duquesne, K., Sturgis, J.N. (2010) Membrane protein solubilization. Methods Mol. Biol. 601:205–217.
Ehsan, M., Du, Y., Scull, N.J., Tikhonova, E., Tarrasch, J., Mortensen, J.S., Loland, C.J., Skiniotis, G., Guan, L., Byrne,
B., Kobilka, B.K., Chae, P.S. (2016) Highly branched pentasaccharide-bearing amphiphiles for membrane protein
studies. J. Am. Chem. Soc. 138:3789–3796.
Ehsan, M., Ghani, L., Du, Y., Hariharan, P., Mortensen, J.S., Ribeiro, O., Hu, H.L., Skiniotis, G., Loland, C.J., Guan, L.,
Kobilka, B.K., Byrne, B., Chae, P.S. (2017) New penta-saccharide-bearing tripod amphiphiles for membrane protein
structure studies. Analyst 142:3889–3898
Esmann, M. (1986) Solubilized (Na
+ + K
+ )-ATPase from shark rectal gland and ox kidney – an inactivation study.
Biochim. Biophys. Acta 857:38–47.
Fredriksson, R., Lagerstrom, M.C., Lundin, L.G., Schioth, H.B. (2003) The G protein-coupled receptors in the human
genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol.
63:1256–1272.
Frey, L., Lakomek, N.-A., Riek, R., Bibow, S. (2017) Micelles, bicelles, and nanodiscs: Comparing the impact of
membrane mimetics on membrane protein backbone dynamics. Angew. Chem. Int. Ed. 56:380–383.
Frindi, M., Michels, B., Zana, R. (1992) Ultrasonic absorption studies of surfactant exchange between micelles and bulk
phase in aqueous micellar solutions of nonionic surfactants with a short alkyl chain. 3. Surfactants with a sugar head
group. J. Phys. Chem. 96:8137–8141.
Garavito, R.M., Ferguson-Miller, S. (2001) Detergents as tools in membrane biochemistry. J. Biol. Chem.
276:32403–32406.
Glaeser, R.M., Jubb, J.S., Henderson, R. (1985) Structural comparison of native and deoxycholate-treated purple
membrane. Biophys. J. 48:775–780.
Gohon, Y., Popot, J.-L. (2003) Membrane protein-surfactant complexes. Curr. Opin. Colloid Interface Sci. 8:15–22.
Guan, L., Smirnova, I.N., Verner, G., Nagamori, S., Kaback, H.R. (2006) Manipulating phospholipids for crystallization
of a membrane transport protein. Proc. Natl. Acad. Sci. USA 103:1723–1726.
Haneskog, L., Andersson, L., Brekkan, E., Englund, A.K., Kameyama, K., Liljas, L., Greijer, E., Fischbarg, J., Lundahl,
P. (1996) Monomeric human red cell glucose transporter (Glut1) in non-ionic detergent solution and a semi-elliptical
torus model for detergent binding to membrane proteins. Biochim. Biophys. Acta. 1282:39–47.
Hauser, H. (2000) Short-chain phospholipids as detergents. Biochim. Biophys. Acta. 1508:164–181.
Heidmann, T., Sobel, A., Popot, J.-L., Changeux, J.-P. (1980) Reconstitution of a functional acetylcholine receptor:
conservation of the conformational and allosteric transitions and recovery of the permeability response; role of lipids.
Eur. J. Biochem. 110:35–55.
Helenius, A., McCaslin, D.R., Fries, E., Tanford, C. (1979) Properties of detergents. Meth. Enzymol. 56:734–749.
Helenius, A., Simons, K. (1975) Solubilization of membranes by detergents. Biochim. Biophys. Acta 415:29–79.
Henderson, R., Jubb, J.S., Rossmann, M.G. (1982) A contracted form of the trigonal purple membrane of Halobacterium
halobium. J. Mol. Biol. 154:501–514.
Hiruma-Shimizu, K., Shimizu, H., Thompson, G.S., Kalverda, A.P., Patching, S.G. (2015) Deuterated detergents for
structural and functional studies of membrane proteins: Properties, chemical synthesis and applications. Mol. Membr.
Biol. 32:139–155.
Hite, R.K., Gonen, T., Harrison, S.C., Walz, T. (2008) Interactions of lipids with aquaporin-0 and other membrane
proteins. Pflügers Arch. 456:651–661.
Hjelmeland, L.M., Nebert, D.W., Osborne, J.C., Jr. (1983) Sulfobetaine derivatives of bile acids: nondenaturing
surfactants for membrane biochemistry. Anal. Biochem. 130:72–82.
Hong, H., Bowie, J.U. (2011) Dramatic destabilization of transmembrane helix interactions by features of natural
membrane environments. J. Am. Chem. Soc. 133:11389–11398.
Hong, W.-X., Baker, K.A., Ma, X., Stevens, R.C., Yeager, M., Zhang, Q. (2011) Design, synthesis and properties of
branch-chained maltoside detergents for stabilization and crystallization of integral membrane proteins: Human
connexin 26. Langmuir 26:8690–8696.
Hovers, J., Potschies, M., Polidori, A., Pucci, B., Raynal, S., Bonneté, F., Serrano-Vega, M., Tate, C., Picot, D., Pierre,
Y., Popot, J.-L., Nehmé, R., Bidet, M., Mus-Veteau, I., Bußkamp, H., Jung, K.-H., Marx, A., Timmins, P.A., Welte,
W. (2011) A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and
crystallization. Mol. Memb. Biol. 28:171–181.
90
2 Extracting Membrane Proteins from Their Native Environment
helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Nat. Acad. Sci. USA
90:11648–11652.
DeGrado, W.F., Gratkowski, H., Lear, J.D. (2003) How do helix-helix interactions help determine the folds of membrane
proteins? Perspectives from the study of homo-oligomeric helical bundles. Protein Sci. 12:647–665.
Dodevski, I., Plückthun, A. (2011) Evolution of three human GPCRs for higher expression and stability. J. Mol. Biol.
408:599–615.
Duquesne, K., Sturgis, J.N. (2010) Membrane protein solubilization. Methods Mol. Biol. 601:205–217.
Ehsan, M., Du, Y., Scull, N.J., Tikhonova, E., Tarrasch, J., Mortensen, J.S., Loland, C.J., Skiniotis, G., Guan, L., Byrne,
B., Kobilka, B.K., Chae, P.S. (2016) Highly branched pentasaccharide-bearing amphiphiles for membrane protein
studies. J. Am. Chem. Soc. 138:3789–3796.
Ehsan, M., Ghani, L., Du, Y., Hariharan, P., Mortensen, J.S., Ribeiro, O., Hu, H.L., Skiniotis, G., Loland, C.J., Guan, L.,
Kobilka, B.K., Byrne, B., Chae, P.S. (2017) New penta-saccharide-bearing tripod amphiphiles for membrane protein
structure studies. Analyst 142:3889–3898
Esmann, M. (1986) Solubilized (Na
+ + K
+ )-ATPase from shark rectal gland and ox kidney – an inactivation study.
Biochim. Biophys. Acta 857:38–47.
Fredriksson, R., Lagerstrom, M.C., Lundin, L.G., Schioth, H.B. (2003) The G protein-coupled receptors in the human
genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol.
63:1256–1272.
Frey, L., Lakomek, N.-A., Riek, R., Bibow, S. (2017) Micelles, bicelles, and nanodiscs: Comparing the impact of
membrane mimetics on membrane protein backbone dynamics. Angew. Chem. Int. Ed. 56:380–383.
Frindi, M., Michels, B., Zana, R. (1992) Ultrasonic absorption studies of surfactant exchange between micelles and bulk
phase in aqueous micellar solutions of nonionic surfactants with a short alkyl chain. 3. Surfactants with a sugar head
group. J. Phys. Chem. 96:8137–8141.
Garavito, R.M., Ferguson-Miller, S. (2001) Detergents as tools in membrane biochemistry. J. Biol. Chem.
276:32403–32406.
Glaeser, R.M., Jubb, J.S., Henderson, R. (1985) Structural comparison of native and deoxycholate-treated purple
membrane. Biophys. J. 48:775–780.
Gohon, Y., Popot, J.-L. (2003) Membrane protein-surfactant complexes. Curr. Opin. Colloid Interface Sci. 8:15–22.
Guan, L., Smirnova, I.N., Verner, G., Nagamori, S., Kaback, H.R. (2006) Manipulating phospholipids for crystallization
of a membrane transport protein. Proc. Natl. Acad. Sci. USA 103:1723–1726.
Haneskog, L., Andersson, L., Brekkan, E., Englund, A.K., Kameyama, K., Liljas, L., Greijer, E., Fischbarg, J., Lundahl,
P. (1996) Monomeric human red cell glucose transporter (Glut1) in non-ionic detergent solution and a semi-elliptical
torus model for detergent binding to membrane proteins. Biochim. Biophys. Acta. 1282:39–47.
Hauser, H. (2000) Short-chain phospholipids as detergents. Biochim. Biophys. Acta. 1508:164–181.
Heidmann, T., Sobel, A., Popot, J.-L., Changeux, J.-P. (1980) Reconstitution of a functional acetylcholine receptor:
conservation of the conformational and allosteric transitions and recovery of the permeability response; role of lipids.
Eur. J. Biochem. 110:35–55.
Helenius, A., McCaslin, D.R., Fries, E., Tanford, C. (1979) Properties of detergents. Meth. Enzymol. 56:734–749.
Helenius, A., Simons, K. (1975) Solubilization of membranes by detergents. Biochim. Biophys. Acta 415:29–79.
Henderson, R., Jubb, J.S., Rossmann, M.G. (1982) A contracted form of the trigonal purple membrane of Halobacterium
halobium. J. Mol. Biol. 154:501–514.
Hiruma-Shimizu, K., Shimizu, H., Thompson, G.S., Kalverda, A.P., Patching, S.G. (2015) Deuterated detergents for
structural and functional studies of membrane proteins: Properties, chemical synthesis and applications. Mol. Membr.
Biol. 32:139–155.
Hite, R.K., Gonen, T., Harrison, S.C., Walz, T. (2008) Interactions of lipids with aquaporin-0 and other membrane
proteins. Pflügers Arch. 456:651–661.
Hjelmeland, L.M., Nebert, D.W., Osborne, J.C., Jr. (1983) Sulfobetaine derivatives of bile acids: nondenaturing
surfactants for membrane biochemistry. Anal. Biochem. 130:72–82.
Hong, H., Bowie, J.U. (2011) Dramatic destabilization of transmembrane helix interactions by features of natural
membrane environments. J. Am. Chem. Soc. 133:11389–11398.
Hong, W.-X., Baker, K.A., Ma, X., Stevens, R.C., Yeager, M., Zhang, Q. (2011) Design, synthesis and properties of
branch-chained maltoside detergents for stabilization and crystallization of integral membrane proteins: Human
connexin 26. Langmuir 26:8690–8696.
Hovers, J., Potschies, M., Polidori, A., Pucci, B., Raynal, S., Bonneté, F., Serrano-Vega, M., Tate, C., Picot, D., Pierre,
Y., Popot, J.-L., Nehmé, R., Bidet, M., Mus-Veteau, I., Bußkamp, H., Jung, K.-H., Marx, A., Timmins, P.A., Welte,
W. (2011) A class of mild surfactants that keep integral membrane proteins water-soluble for functional studies and
crystallization. Mol. Memb. Biol. 28:171–181.
90
2 Extracting Membrane Proteins from Their Native Environment