Henke, A., Kadłubowski, S., Wolszczak, M., Ulański, P., Boyko, V., Schmidt, T., Arndt, K.-F., Rosiak, J.M. (2011) The
structure and aggregation of hydrogen-bonded interpolymer complexes of poly(acrylic acid) with poly(N-vinylpyrrolidone) in dilute aqueous solution. Macromol. Chem. Phys. 212:2529–2540.
Heredia, K.L., Grover, G.N., Tao, L., Maynard, H.D. (2009) Synthesis of heterotelechelic polymers for conjugation of
two different proteins. Macromolecules 42:2360–2367.
Hernandez, H., Robinson, C.V. (2007) Determining the stoichiometry and interactions of macromolecular assemblies
from mass spectrometry. Nat. Protocols 2:715–726.
Heuts, J.P.A., Muratore, L.M., Davis, T.P. (2000) Preparation and characterization of oligomeric terpolymers of styrene,
methyl methacrylate and 2-hydroxyethyl methacrylate: A comparison of conventional and catalytic chain transfer.
Macromol. Chem. Phys. 201:2780–2788.
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.
Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2014) Application of amphipols for structure-functional analysis
of TRP channels. J. Membr. Biol. 247:843–851.
Jacrot, B., Zaccai, G. (1981) Determination of molecular weight by neutron scattering. Biopolymers 20:2413–2426.
Jamshad, M., Charlton, J., Lin, Y.-P., Routledge, S.J., Bawa, Z., Knowles, T.J., Overduin, M., Dekker, N., Dafforn, T.R.,
Bill, R.M., Poyner, D.R., Wheatley, M. (2015a) G protein-coupled receptor solubilization and purification for
biophysical analysis and functional studies, in the total absence of detergent. Biosc. Rep. 35:e00188.
Jamshad, M., Grimard, V., Idini, I., Knowles, T.J., Dowle, M.R., Schofield, N., Sridhar, P., Lin, Y., Finka, R., Wheatley,
M., Thomas, O.R.T., Palmer, R.E., Overduin, M., Govaerts, C., Ruysschaert, J.-M., Edler, K.J., Dafforn,
T.R. (2015b) Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of
membrane proteins. Nano Res. 8:774–789.
Jamshad, M., Lin, Y.P., Knowles, T.J., Parslow, R.A., Harris, C., Wheatley, M., Poyner, D.R., Bill, R.M., Thomas, O.R.,
Overduin, M., Dafforn, T.R. (2011) Surfactant-free purification of membrane proteins with intact native membrane
environment. Biochem. Soc. Trans. 39:813–818.
Jasnin, M., van Eijck, L., Koza, M.M., J. Peters., Laguri, C., Lortat-Jacob, H., Zaccai, G. (2010) Dynamics of heparan
sulfate explored by neutron scattering. Phys. Chem. Chem. Phys. 12:3360–3362.
Kanellou, A., Spilioti, A., Theodosopoulos, G.V., Choinopoulos, I., Pitsikalis, M. (2015) Statistical copolymers of
benzyl methacrylate and diethylaminoethyl methacrylate: monomer reactivity ratios and thermal properties. J. Org.
Inorg. Chem. 1:1–11.
Kanu, A.B., Dwivedi, P., Tam, M., Matz, L., Hill Jr., H.H. (2008) Ion mobility – mass spectrometry. J. Mass Spectrom.
43:1–22.
Kelen, T., Tüdös, F., Turcsányi, B. (1980) Confidence intervals for copolymerization reactivity ratios determined by the
Kelen-Tüdös method. Polym. Bull. 2:71–76.
Klammt, C., Perrin, M.-H., Maslennikov, I., Renault, L., Krupa, M., Kwiatkowski, W., Stahlberg, H., Vale, W., Choe,
S. (2011) Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without
detergents. Prot. Sci. 20:1030–1041.
Knoop, C.A., Studer, A. (2003) Hydroxy- and silyloxy-substituted TEMPO derivatives for the living free-radical
polymerization of styrene and n-butyl acrylate: Synthesis, kinetics, and mechanistic studies. J. Am. Chem. Soc.
125:16327–16333.
Knowles, T.J., Finka, R., Smith, C., Lin, Y.-P., Dafforn, T., Overduin, M. (2009) Membrane proteins solubilized intact in
lipid containing nanoparticles bounded by styrene-maleic acid copolymer. J. Am. Chem. Soc. 131:7484–7485.
König, S., Sackmann, E. (1996) Molecular and collective dynamics of lipid bilayers. Curr. Opin. Colloid Interface Sci.
1:78–82.
Ladavière, C., Toustou, M., Gulik-Krzywicki, T., Tribet, C. (2001) Slow reorganization of small phosphatidylcholine
vesicles upon adsorption of amphiphilic polymers. J. Colloid Interface Sci. 241:178–187.
Ladavière, C., Tribet, C., Cribier, S. (2002) Lateral organization of lipid membranes induced by amphiphilic polymer
inclusions. Langmuir 18:7320–7327.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L. (2014a) Synthesis of an
oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res. 42:
e83.
Le Bon, C., Popot, J.-L., Giusti, F. (2014b) Labeling and functionalizing amphipols for biological applications.
J. Membr. Biol. 247:797–814.
Lee, S.C., Khalid, S., Pollock, N.L., Knowles, T.J., Edler, K., Rothnie, A.J., Thomas, O.R.T., Dafforn, T.R. (2016)
Encapsulated membrane proteins: A simplified system for molecular simulation. Biochim. Biophys. Acta
1858:2549–2557.
Leney, A.C., McMorran, L.M., Radford, S.E., Ashcroft, A.E. (2012) Amphipathic polymers enable the study of
functional membrane proteins in the gas phase. Anal. Chem. 84:9841–9847.
References
231
structure and aggregation of hydrogen-bonded interpolymer complexes of poly(acrylic acid) with poly(N-vinylpyrrolidone) in dilute aqueous solution. Macromol. Chem. Phys. 212:2529–2540.
Heredia, K.L., Grover, G.N., Tao, L., Maynard, H.D. (2009) Synthesis of heterotelechelic polymers for conjugation of
two different proteins. Macromolecules 42:2360–2367.
Hernandez, H., Robinson, C.V. (2007) Determining the stoichiometry and interactions of macromolecular assemblies
from mass spectrometry. Nat. Protocols 2:715–726.
Heuts, J.P.A., Muratore, L.M., Davis, T.P. (2000) Preparation and characterization of oligomeric terpolymers of styrene,
methyl methacrylate and 2-hydroxyethyl methacrylate: A comparison of conventional and catalytic chain transfer.
Macromol. Chem. Phys. 201:2780–2788.
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.
Huynh, K.W., Cohen, M.R., Moiseenkova-Bell, V.Y. (2014) Application of amphipols for structure-functional analysis
of TRP channels. J. Membr. Biol. 247:843–851.
Jacrot, B., Zaccai, G. (1981) Determination of molecular weight by neutron scattering. Biopolymers 20:2413–2426.
Jamshad, M., Charlton, J., Lin, Y.-P., Routledge, S.J., Bawa, Z., Knowles, T.J., Overduin, M., Dekker, N., Dafforn, T.R.,
Bill, R.M., Poyner, D.R., Wheatley, M. (2015a) G protein-coupled receptor solubilization and purification for
biophysical analysis and functional studies, in the total absence of detergent. Biosc. Rep. 35:e00188.
Jamshad, M., Grimard, V., Idini, I., Knowles, T.J., Dowle, M.R., Schofield, N., Sridhar, P., Lin, Y., Finka, R., Wheatley,
M., Thomas, O.R.T., Palmer, R.E., Overduin, M., Govaerts, C., Ruysschaert, J.-M., Edler, K.J., Dafforn,
T.R. (2015b) Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of
membrane proteins. Nano Res. 8:774–789.
Jamshad, M., Lin, Y.P., Knowles, T.J., Parslow, R.A., Harris, C., Wheatley, M., Poyner, D.R., Bill, R.M., Thomas, O.R.,
Overduin, M., Dafforn, T.R. (2011) Surfactant-free purification of membrane proteins with intact native membrane
environment. Biochem. Soc. Trans. 39:813–818.
Jasnin, M., van Eijck, L., Koza, M.M., J. Peters., Laguri, C., Lortat-Jacob, H., Zaccai, G. (2010) Dynamics of heparan
sulfate explored by neutron scattering. Phys. Chem. Chem. Phys. 12:3360–3362.
Kanellou, A., Spilioti, A., Theodosopoulos, G.V., Choinopoulos, I., Pitsikalis, M. (2015) Statistical copolymers of
benzyl methacrylate and diethylaminoethyl methacrylate: monomer reactivity ratios and thermal properties. J. Org.
Inorg. Chem. 1:1–11.
Kanu, A.B., Dwivedi, P., Tam, M., Matz, L., Hill Jr., H.H. (2008) Ion mobility – mass spectrometry. J. Mass Spectrom.
43:1–22.
Kelen, T., Tüdös, F., Turcsányi, B. (1980) Confidence intervals for copolymerization reactivity ratios determined by the
Kelen-Tüdös method. Polym. Bull. 2:71–76.
Klammt, C., Perrin, M.-H., Maslennikov, I., Renault, L., Krupa, M., Kwiatkowski, W., Stahlberg, H., Vale, W., Choe,
S. (2011) Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without
detergents. Prot. Sci. 20:1030–1041.
Knoop, C.A., Studer, A. (2003) Hydroxy- and silyloxy-substituted TEMPO derivatives for the living free-radical
polymerization of styrene and n-butyl acrylate: Synthesis, kinetics, and mechanistic studies. J. Am. Chem. Soc.
125:16327–16333.
Knowles, T.J., Finka, R., Smith, C., Lin, Y.-P., Dafforn, T., Overduin, M. (2009) Membrane proteins solubilized intact in
lipid containing nanoparticles bounded by styrene-maleic acid copolymer. J. Am. Chem. Soc. 131:7484–7485.
König, S., Sackmann, E. (1996) Molecular and collective dynamics of lipid bilayers. Curr. Opin. Colloid Interface Sci.
1:78–82.
Ladavière, C., Toustou, M., Gulik-Krzywicki, T., Tribet, C. (2001) Slow reorganization of small phosphatidylcholine
vesicles upon adsorption of amphiphilic polymers. J. Colloid Interface Sci. 241:178–187.
Ladavière, C., Tribet, C., Cribier, S. (2002) Lateral organization of lipid membranes induced by amphiphilic polymer
inclusions. Langmuir 18:7320–7327.
Le Bon, C., Della Pia, E.A., Giusti, F., Lloret, N., Zoonens, M., Martinez, K.L., Popot, J.-L. (2014a) Synthesis of an
oligonucleotide-derivatized amphipol and its use to trap and immobilize membrane proteins. Nucleic Acids Res. 42:
e83.
Le Bon, C., Popot, J.-L., Giusti, F. (2014b) Labeling and functionalizing amphipols for biological applications.
J. Membr. Biol. 247:797–814.
Lee, S.C., Khalid, S., Pollock, N.L., Knowles, T.J., Edler, K., Rothnie, A.J., Thomas, O.R.T., Dafforn, T.R. (2016)
Encapsulated membrane proteins: A simplified system for molecular simulation. Biochim. Biophys. Acta
1858:2549–2557.
Leney, A.C., McMorran, L.M., Radford, S.E., Ashcroft, A.E. (2012) Amphipathic polymers enable the study of
functional membrane proteins in the gas phase. Anal. Chem. 84:9841–9847.
References
231