Georges, M.K., Veregin, R.P.N., Kazmaier, P.M., Hamer, G.K. (1993) Narrow molecular weight resins by a free-radical
polymerization process. Macromolecules 26:2987–2988.
Gilbert, R.G., Hess, M., Jenkins, A.D., Jones, R.G., Kratochvíl, P., Stepto, R.F.T. (2009) Dispersity in polymer science
(IUPAC Recommendations 2009). Pure Appl. Chem. 81: 351–353.
Giusti, F., Kessler, P., Westh Hansen, R., Della Pia, E.A., Le Bon, C., Mourier, G., Popot, J.-L., Martinez, K.L., Zoonens,
M. (2015) Synthesis of a polyhistidine-bearing amphipol and its use for immobilizing membrane proteins. Biomacromolecules 16:3751–3761.
Giusti, F., Popot, J.-L., Tribet, C. (2012) Well-defined critical association concentration and rapid adsorption at the
air/water interface of a short amphiphilic polymer, amphipol A8-35: A study by Förster resonance energy transfer and
dynamic surface tension measurements. Langmuir 28:10372–10380.
Giusti, F., Rieger, J., Catoire, L., Qian, S., Calabrese, A.N., Watkinson, T.G., Casiraghi, M., Radford, S.E., Ashcroft, A.
E., Popot, J.-L. (2014) Synthesis, characterization and applications of a perdeuterated amphipol. J. Membr. Biol.
247:909–924.
Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Thèse de DEA, Université Paris VI, Paris, 28 p.
Gohon, Y. (2002) Etude structurale et fonctionnelle de deux protéines membranaires, la bactériorhodopsine et le
récepteur nicotinique de l'acétylcholine, maintenues en solution aqueuse non détergente par des polymères
amphiphiles. Thèse de Doctorat, Université Paris-VI, Paris, 467 p.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., Popot, J.-L. (2006) Well-defined
nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35.
Langmuir 22:1281–1290.
Gohon, Y., Pavlov, G., Timmins, P., Tribet, C., Popot, J.-L., Ebel, C. (2004) Partial specific volume and solvent
interactions of amphipol A8-35. Anal. Biochem. 334:318–334.
Gohon, Y., Vindigni, J.-D., Pallier, A., Wien, F., Celia, H., Giuliani, A., Tribet, C., Chardot, T., Briozzo, P. (2011) High
water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed
lipid bodies. Biochim. Biophys. Acta 1808:706–716.
Golas, P.L., Matyjaszewski, K. (2010) Marrying click chemistry with polymerization: expanding the scope of polymeric
materials. Chem. Soc. Rev. 39:1338–1354.
Gorzelle, B.M., Hoffman, A.K., Keyes, M.H., Gray, D.N., Ray, D.G., Sanders II, C.R. (2002) Amphipols can support the
activity of a membrane enzyme. J. Am. Chem. Soc. 124:11594–11595.
Greszta, D., Mardare, D., Matyjaszewski, K. (1994) “Living” radical polymerization. 1. Possibilities and limitations.
Macromolecules 27:638–644.
Grethen, A., Glueck, D., Keller, S. (2018) Role of coulombic repulsion in collisional lipid transfer among SMA(2:1)bounded nanodiscs. J. Membr. Biol., in the press.
Grethen, A., Oluwole, A.O., Danielczak, B., Vargas, C., Keller, S. (2017) Thermodynamics of nanodisc formation
mediated by styrene/maleic acid (2:1) copolymer. Sci. Rep. 7:11517.
Griffith, W.L., Triolo, R., Compere, A.L. (1987) Analytical scattering function of a polydisperse Percus-Yevick fluid
with Schulz- (Γ-) distributed diameters. Phys. Rev. A 35:2200–2206.
Grimaldo, M., Roosen-Runge, F., Hennig, M., Zanini, F., Zhang, F., Jalarvo, N., Zamponi, M., Schreiber, F., Seydel,
T. (2015) Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and
above thermal denaturation. Phys. Chem. Chem. Phys. 17:4645–4655.
Grubbs, R.B. (2011) Nitroxide-mediated radical polymerization: Limitations and versatility. Polym. Rev. 51:104–137.
Guild, K., Zhang, Y., Stacy, R., Mundt, E., Benbow, S., Green, A., Myler, P.J. (2011) Wheat germ cell-free expression
system as a pathway to improve protein yield and solubility for the SSGCID pipeline. Acta Crystallogr. Sect. F Struct.
Biol. Cryst. Commun. 67:1027–1031.
Guinier, A., Fournet, G. (1955) Small-angle scattering of X-rays. John Wiley & sons, New York, 268 p.
Gulati, S., Jamshad, M., Knowles, T.J., Morrison, K.A., Downing, R., Cant, N., Collins, R., Koenderink, J.B., Ford, R.
C., Overduin, M., Kerr, I.D., Dafforn, T.R., Rothnie, A.J. (2014) Detergent-free purification of ABC (ATP-bindingcassette) transporters. Biochem. J. 461:269–278.
Han, S.G., Baek, S.I., Son, T.J., Lee, H., Kim, N.H., Yu, Y.G. (2017) Preparation of functional human lysophosphatidic
acid receptor 2 using a P9* expression system and an amphipathic polymer and investigation of its in vitro binding
preference to G α proteins. Biochem. Biophys. Res. Commun. 487:103–108.
Han, S.G., Na, J.H., Lee, W.K., Park, D., Oh, J., Yoon, S.H., Lee, C.K., Sung, M.H., Shin, Y.K., Yu, Y.G. (2014) An
amphipathic polypeptide derived from poly-γ-glutamic acid for the stabilization of membrane proteins. Prot. Sci.
23:1800–1807.
Harrington, J.C. (2008) Charge density effects on polyelectrolyte dynamic rheology. J. Appl. Polym. Sci.
107:3310–3317.
230
4 Chemical Structure, Synthesis, and Physical-Chemical Properties of Amphipols
polymerization process. Macromolecules 26:2987–2988.
Gilbert, R.G., Hess, M., Jenkins, A.D., Jones, R.G., Kratochvíl, P., Stepto, R.F.T. (2009) Dispersity in polymer science
(IUPAC Recommendations 2009). Pure Appl. Chem. 81: 351–353.
Giusti, F., Kessler, P., Westh Hansen, R., Della Pia, E.A., Le Bon, C., Mourier, G., Popot, J.-L., Martinez, K.L., Zoonens,
M. (2015) Synthesis of a polyhistidine-bearing amphipol and its use for immobilizing membrane proteins. Biomacromolecules 16:3751–3761.
Giusti, F., Popot, J.-L., Tribet, C. (2012) Well-defined critical association concentration and rapid adsorption at the
air/water interface of a short amphiphilic polymer, amphipol A8-35: A study by Förster resonance energy transfer and
dynamic surface tension measurements. Langmuir 28:10372–10380.
Giusti, F., Rieger, J., Catoire, L., Qian, S., Calabrese, A.N., Watkinson, T.G., Casiraghi, M., Radford, S.E., Ashcroft, A.
E., Popot, J.-L. (2014) Synthesis, characterization and applications of a perdeuterated amphipol. J. Membr. Biol.
247:909–924.
Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Thèse de DEA, Université Paris VI, Paris, 28 p.
Gohon, Y. (2002) Etude structurale et fonctionnelle de deux protéines membranaires, la bactériorhodopsine et le
récepteur nicotinique de l'acétylcholine, maintenues en solution aqueuse non détergente par des polymères
amphiphiles. Thèse de Doctorat, Université Paris-VI, Paris, 467 p.
Gohon, Y., Dahmane, T., Ruigrok, R., Schuck, P., Charvolin, D., Rappaport, F., Timmins, P., Engelman, D.M., Tribet,
C., Popot, J.-L., Ebel, C. (2008) Bacteriorhodopsin/amphipol complexes: structural and functional properties.
Biophys. J. 94:3523–3537.
Gohon, Y., Giusti, F., Prata, C., Charvolin, D., Timmins, P., Ebel, C., Tribet, C., Popot, J.-L. (2006) Well-defined
nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35.
Langmuir 22:1281–1290.
Gohon, Y., Pavlov, G., Timmins, P., Tribet, C., Popot, J.-L., Ebel, C. (2004) Partial specific volume and solvent
interactions of amphipol A8-35. Anal. Biochem. 334:318–334.
Gohon, Y., Vindigni, J.-D., Pallier, A., Wien, F., Celia, H., Giuliani, A., Tribet, C., Chardot, T., Briozzo, P. (2011) High
water solubility and fold in amphipols of proteins with large hydrophobic regions: Oleosins and caleosin from seed
lipid bodies. Biochim. Biophys. Acta 1808:706–716.
Golas, P.L., Matyjaszewski, K. (2010) Marrying click chemistry with polymerization: expanding the scope of polymeric
materials. Chem. Soc. Rev. 39:1338–1354.
Gorzelle, B.M., Hoffman, A.K., Keyes, M.H., Gray, D.N., Ray, D.G., Sanders II, C.R. (2002) Amphipols can support the
activity of a membrane enzyme. J. Am. Chem. Soc. 124:11594–11595.
Greszta, D., Mardare, D., Matyjaszewski, K. (1994) “Living” radical polymerization. 1. Possibilities and limitations.
Macromolecules 27:638–644.
Grethen, A., Glueck, D., Keller, S. (2018) Role of coulombic repulsion in collisional lipid transfer among SMA(2:1)bounded nanodiscs. J. Membr. Biol., in the press.
Grethen, A., Oluwole, A.O., Danielczak, B., Vargas, C., Keller, S. (2017) Thermodynamics of nanodisc formation
mediated by styrene/maleic acid (2:1) copolymer. Sci. Rep. 7:11517.
Griffith, W.L., Triolo, R., Compere, A.L. (1987) Analytical scattering function of a polydisperse Percus-Yevick fluid
with Schulz- (Γ-) distributed diameters. Phys. Rev. A 35:2200–2206.
Grimaldo, M., Roosen-Runge, F., Hennig, M., Zanini, F., Zhang, F., Jalarvo, N., Zamponi, M., Schreiber, F., Seydel,
T. (2015) Hierarchical molecular dynamics of bovine serum albumin in concentrated aqueous solution below and
above thermal denaturation. Phys. Chem. Chem. Phys. 17:4645–4655.
Grubbs, R.B. (2011) Nitroxide-mediated radical polymerization: Limitations and versatility. Polym. Rev. 51:104–137.
Guild, K., Zhang, Y., Stacy, R., Mundt, E., Benbow, S., Green, A., Myler, P.J. (2011) Wheat germ cell-free expression
system as a pathway to improve protein yield and solubility for the SSGCID pipeline. Acta Crystallogr. Sect. F Struct.
Biol. Cryst. Commun. 67:1027–1031.
Guinier, A., Fournet, G. (1955) Small-angle scattering of X-rays. John Wiley & sons, New York, 268 p.
Gulati, S., Jamshad, M., Knowles, T.J., Morrison, K.A., Downing, R., Cant, N., Collins, R., Koenderink, J.B., Ford, R.
C., Overduin, M., Kerr, I.D., Dafforn, T.R., Rothnie, A.J. (2014) Detergent-free purification of ABC (ATP-bindingcassette) transporters. Biochem. J. 461:269–278.
Han, S.G., Baek, S.I., Son, T.J., Lee, H., Kim, N.H., Yu, Y.G. (2017) Preparation of functional human lysophosphatidic
acid receptor 2 using a P9* expression system and an amphipathic polymer and investigation of its in vitro binding
preference to G α proteins. Biochem. Biophys. Res. Commun. 487:103–108.
Han, S.G., Na, J.H., Lee, W.K., Park, D., Oh, J., Yoon, S.H., Lee, C.K., Sung, M.H., Shin, Y.K., Yu, Y.G. (2014) An
amphipathic polypeptide derived from poly-γ-glutamic acid for the stabilization of membrane proteins. Prot. Sci.
23:1800–1807.
Harrington, J.C. (2008) Charge density effects on polyelectrolyte dynamic rheology. J. Appl. Polym. Sci.
107:3310–3317.
230
4 Chemical Structure, Synthesis, and Physical-Chemical Properties of Amphipols