Bond, P.J., Faraldo-Gómez, J.D., Deol, S.S., Sansom, M.S.P. (2006) Membrane protein dynamics and detergent
interactions within a crystal: A simulation study of OmpA. Proc. Natl. Acad. Sci. USA 103:9518–9523.
Bond, P.J., Sansom, M.S.P. (2003) Membrane protein dynamics versus environment: simulations of OmpA in a micelle
and in a bilayer. J. Mol. Biol. 329:1035–1053.
Bowie, J.U. (2001) Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11:397–402.
Breyton, C., Gabel, F., Abla, M., Pierre, Y., Lebaupain, F., Durand, G., Popot, J.-L., Ebel, C., Pucci, B. (2009) Micellar
and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head. Biophys. J.
97:1077–1086.
Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L. (1997) Dimer to monomer conversion of the cytochrome
b 6 f complex: causes and consequences. J. Biol. Chem. 272:21892–21900.
Brotherus, J.R., Jost, P.C., Griffith, O.H., Hokin, L.E. (1979) Detergent inactivation of sodium- and potassium-activated
adenosinetriphosphatase of the electric eel. Biochemistry 18:5043–5050.
Brouillette, C.G., Muccio, D.D., Finney, T.K. (1987) pH dependence of bacteriorhodopsin thermal unfolding. Biochemistry 26:7431–7438.
Carey, M.C., Small, D.M. (1972) Micelle formation by bile salts. Physical-chemical and thermodynamic considerations.
Arch. Intern. Med. 130:506–527.
Chae, P.S., Gotfryd, K., Pacyna, J., Miercke, L.J.W., Rasmussen, S.G.F., Robbins, R.A., Rana, R.R., Loland, C.J.,
Kobilka, B.K., Stroud, R., Byrne, B., Gether, U., Gellman, S.H. (2010a) Tandem facial amphiphiles for membrane
protein stabilization. J. Am. Chem. Soc. 132:16750–16752.
Chae, P.S., Kruse, A.C., Gotfryd, K., Rana, R.R., Cho, K.H., Rasmussen, S.G., Bae, H.E., Chandra, R., Gether, U.,
Guan, L., Kobilka, B.K., Loland, C.J., Byrne, B., Gellman, S.H. (2013a) Novel tripod amphiphiles for membrane
protein analysis. Chemistry – Eur. J. 19:15645–15651.
Chae, P.S., Rana, R.R., Gotfryd, K., Rasmussen, S.G.F., Kruse, A.C., Cho, K.H., Capaldi, S., Carlsson, E., Kobilka, B.
K., Loland, C.J., Gether, U., Banerjee, S., Byrne, B., Lee, J.K., Gellman, S.H. (2013b) Glucose-neopentyl glycol
(GNG) amphiphiles for membrane protein study. Chem. Commun. 49:2287–2289.
Chae, P.S., Rasmussen, S.G.F., Rana, R., Gotfryd, K., Chandra, R., Goren, M.A., Kruse, A.C., Nurva, S., Loland, C.J.,
Pierre, Y., Drew, D., Popot, J.-L., Picot, D., Fox, B.G., Guan, L., Gether, U., Byrne, B., Kobilka, B.K., Gellman,
S.H. (2010b) Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of
membrane proteins. Nat. Methods 7:1003–1008.
Chae, P.S., Rasmussen, S.G.F., Rana, R.R., Gotfryd, K., Kruse, A.C., Nurva, S., Loland, C.J., Guan, L., Gether, U.,
Byrne, B., Kobilka, B.K., Gellman, S.H. (2012) A new class of amphiphiles bearing rigid hydrophobic groups for
solubilization and stabilization of membrane proteins. Chemistry – Eur. J. 18:9485–9490.
Chae, P.S., Wander, M.J., Bowling, A.P., Laible, P.D., Gellman, S.H. (2008) Glycotripod amphiphiles for solubilization
and stabilization of a membrane-protein superassembly: importance of branching in the hydrophilic portion.
ChemBioChem 9:1706–1709.
Champeil, P., Orlowski, S., Babin, S., Lund, S., le Maire, M., Møller, J., Lenoir, G., Montigny, C. (2016) A robust
method to screen detergents for membrane protein stabilization, revisited. Anal. Biochem. 511:31–35.
Chevalier, Y. (2002) New surfactants: new chemical functions and molecular architectures. Curr. Opin. Colloid Interface
Sci. 7:3–11.
Choutko, A., Glättli, A., Fernández, C., Hilty, C., Wüthrich, K., van Gunsteren, W.F. (2011) Membrane protein
dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a
micelle. Eur. Biophys. J. 40:39–58.
Cortes, D.M., Perozo, E. (1997) Structural dynamics of the Streptomyces lividans K
+ channel (SKC1): oligomeric
stoichiometry and stability. Biochemistry 36:10343–10352.
Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., Rosenbusch, J.P. (1992)
Crystal structures explain functional properties of two E. coli porins. Nature 358:727–733.
Cross, T.A., Sharma, M., Yi, M., Zhou, H.-X. (2011) Influence of solubilizing environments on membrane protein
structures. Trends Biochem. Sci. 36:117–125.
Cuthbertson, J.M., Bond, P.J., Sansom, M.S.P. (2006) Transmembrane helix-helix interactions: Comparative simulations
of the glycophorin A dimer. Biochemistry 45:14298–14310.
Dahmane, T. (2007) Protéines membranaires et amphipols : stabilisation, fonction, renaturation, et développement
d'amphipols sulfonatés pour la RMN des solutions. Thèse de Doctorat, Université Paris-7, Paris, 229 p.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
Das, M., Du, Y., Ribeiro, O., Hariharan, P., Mortensen, J.S., Patra, D., Skiniotis, G., Loland, C.J., Guan, L., Kobilka, B.
K., Byrne, B., Chae, P.S. (2017) Conformationally preorganized diastereomeric norbornane-based maltosides for
membrane protein study: Implications of detergent kink for micellar properties. J. Am. Chem. Soc. 139:3072–3081.
de Vitry, C., Diner, B.A., Popot, J.-L. (1991) Photosystem II particles from Chlamydomonas reinhardtii: purification,
molecular weight, small subunit composition, protein phosphorylation. J. Biol. Chem. 266:16614–16621.
References
89
interactions within a crystal: A simulation study of OmpA. Proc. Natl. Acad. Sci. USA 103:9518–9523.
Bond, P.J., Sansom, M.S.P. (2003) Membrane protein dynamics versus environment: simulations of OmpA in a micelle
and in a bilayer. J. Mol. Biol. 329:1035–1053.
Bowie, J.U. (2001) Stabilizing membrane proteins. Curr. Opin. Struct. Biol. 11:397–402.
Breyton, C., Gabel, F., Abla, M., Pierre, Y., Lebaupain, F., Durand, G., Popot, J.-L., Ebel, C., Pucci, B. (2009) Micellar
and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head. Biophys. J.
97:1077–1086.
Breyton, C., Tribet, C., Olive, J., Dubacq, J.-P., Popot, J.-L. (1997) Dimer to monomer conversion of the cytochrome
b 6 f complex: causes and consequences. J. Biol. Chem. 272:21892–21900.
Brotherus, J.R., Jost, P.C., Griffith, O.H., Hokin, L.E. (1979) Detergent inactivation of sodium- and potassium-activated
adenosinetriphosphatase of the electric eel. Biochemistry 18:5043–5050.
Brouillette, C.G., Muccio, D.D., Finney, T.K. (1987) pH dependence of bacteriorhodopsin thermal unfolding. Biochemistry 26:7431–7438.
Carey, M.C., Small, D.M. (1972) Micelle formation by bile salts. Physical-chemical and thermodynamic considerations.
Arch. Intern. Med. 130:506–527.
Chae, P.S., Gotfryd, K., Pacyna, J., Miercke, L.J.W., Rasmussen, S.G.F., Robbins, R.A., Rana, R.R., Loland, C.J.,
Kobilka, B.K., Stroud, R., Byrne, B., Gether, U., Gellman, S.H. (2010a) Tandem facial amphiphiles for membrane
protein stabilization. J. Am. Chem. Soc. 132:16750–16752.
Chae, P.S., Kruse, A.C., Gotfryd, K., Rana, R.R., Cho, K.H., Rasmussen, S.G., Bae, H.E., Chandra, R., Gether, U.,
Guan, L., Kobilka, B.K., Loland, C.J., Byrne, B., Gellman, S.H. (2013a) Novel tripod amphiphiles for membrane
protein analysis. Chemistry – Eur. J. 19:15645–15651.
Chae, P.S., Rana, R.R., Gotfryd, K., Rasmussen, S.G.F., Kruse, A.C., Cho, K.H., Capaldi, S., Carlsson, E., Kobilka, B.
K., Loland, C.J., Gether, U., Banerjee, S., Byrne, B., Lee, J.K., Gellman, S.H. (2013b) Glucose-neopentyl glycol
(GNG) amphiphiles for membrane protein study. Chem. Commun. 49:2287–2289.
Chae, P.S., Rasmussen, S.G.F., Rana, R., Gotfryd, K., Chandra, R., Goren, M.A., Kruse, A.C., Nurva, S., Loland, C.J.,
Pierre, Y., Drew, D., Popot, J.-L., Picot, D., Fox, B.G., Guan, L., Gether, U., Byrne, B., Kobilka, B.K., Gellman,
S.H. (2010b) Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of
membrane proteins. Nat. Methods 7:1003–1008.
Chae, P.S., Rasmussen, S.G.F., Rana, R.R., Gotfryd, K., Kruse, A.C., Nurva, S., Loland, C.J., Guan, L., Gether, U.,
Byrne, B., Kobilka, B.K., Gellman, S.H. (2012) A new class of amphiphiles bearing rigid hydrophobic groups for
solubilization and stabilization of membrane proteins. Chemistry – Eur. J. 18:9485–9490.
Chae, P.S., Wander, M.J., Bowling, A.P., Laible, P.D., Gellman, S.H. (2008) Glycotripod amphiphiles for solubilization
and stabilization of a membrane-protein superassembly: importance of branching in the hydrophilic portion.
ChemBioChem 9:1706–1709.
Champeil, P., Orlowski, S., Babin, S., Lund, S., le Maire, M., Møller, J., Lenoir, G., Montigny, C. (2016) A robust
method to screen detergents for membrane protein stabilization, revisited. Anal. Biochem. 511:31–35.
Chevalier, Y. (2002) New surfactants: new chemical functions and molecular architectures. Curr. Opin. Colloid Interface
Sci. 7:3–11.
Choutko, A., Glättli, A., Fernández, C., Hilty, C., Wüthrich, K., van Gunsteren, W.F. (2011) Membrane protein
dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a
micelle. Eur. Biophys. J. 40:39–58.
Cortes, D.M., Perozo, E. (1997) Structural dynamics of the Streptomyces lividans K
+ channel (SKC1): oligomeric
stoichiometry and stability. Biochemistry 36:10343–10352.
Cowan, S.W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R.A., Jansonius, J.N., Rosenbusch, J.P. (1992)
Crystal structures explain functional properties of two E. coli porins. Nature 358:727–733.
Cross, T.A., Sharma, M., Yi, M., Zhou, H.-X. (2011) Influence of solubilizing environments on membrane protein
structures. Trends Biochem. Sci. 36:117–125.
Cuthbertson, J.M., Bond, P.J., Sansom, M.S.P. (2006) Transmembrane helix-helix interactions: Comparative simulations
of the glycophorin A dimer. Biochemistry 45:14298–14310.
Dahmane, T. (2007) Protéines membranaires et amphipols : stabilisation, fonction, renaturation, et développement
d'amphipols sulfonatés pour la RMN des solutions. Thèse de Doctorat, Université Paris-7, Paris, 229 p.
Dahmane, T., Rappaport, F., Popot, J.-L. (2013) Amphipol-assisted folding of bacteriorhodopsin in the presence and
absence of lipids. Functional consequences. Eur. Biophys. J. 42:85–101.
Das, M., Du, Y., Ribeiro, O., Hariharan, P., Mortensen, J.S., Patra, D., Skiniotis, G., Loland, C.J., Guan, L., Kobilka, B.
K., Byrne, B., Chae, P.S. (2017) Conformationally preorganized diastereomeric norbornane-based maltosides for
membrane protein study: Implications of detergent kink for micellar properties. J. Am. Chem. Soc. 139:3072–3081.
de Vitry, C., Diner, B.A., Popot, J.-L. (1991) Photosystem II particles from Chlamydomonas reinhardtii: purification,
molecular weight, small subunit composition, protein phosphorylation. J. Biol. Chem. 266:16614–16621.
References
89