Gohon, Y. (1996) Etude des interactions entre un analogue du fragment transmembranaire de la glycophorine A et des
polymères amphiphiles: les amphipols. Rapport de DEA, Université Paris VI, Paris, 28 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.
Hall, Z., Robinson, C.V. (2012) Do charge state signatures guarantee protein conformations? J. Am. Soc. Mass Spectrom.
23:1161–1168.
Hebling, C.M., Morgan, C.R., Stafford, D.W., Jorgenson, J.W., Rand, K.D., Engen, J.R. (2010) Conformational analysis
of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry. Anal. Chem.
82:5415–5419.
Hernandez, H., Robinson, C.V. (2007) Determining the stoichiometry and interactions of macromolecular assemblies
from mass spectrometry. Nat. Protocols 2:715–726.
Hilton, G.R., Benesch, J.L. (2012) Two decades of studying non-covalent biomolecular assemblies by means of
electrospray ionization mass spectrometry. J. R. Soc. Interface 9:801–816.
Hopper, J.T.S., Yu, Y.T.-C., Li, D., Raymond, A., Bostock, M., Liko, I., Mikhailov, V., Laganowsky, A., Benesch, J.L.
P., Caffrey, M., Nietlispach, D., Robinson, C.V. (2013) Detergent-free mass spectrometry of membrane protein
complexes. Nat. Meth. 10:1206–1208.
Juraschek, R., Dülcks, T., Karas, M. (1999) Nanoelectrospray–more than just a minimized-flow electrospray ionization
source J. Am. Soc. Mass Spectrom. 10:300–308.
Kanu, A.B., Dwivedi, P., Tam, M., Matz, L., Hill Jr., H.H. (2008) Ion mobility-mass spectrometry. J. Mass Spectrom.
43:1–22.
Konijnenberg, A., van Dyck, J.F., Kailing, L.L., Sobott, F. (2015) Extending native mass spectrometry approaches to
integral membrane proteins. Biol. Chem. 396:991–1002.
Konijnenberg, A., Yilmaz, D., Ingólfsson, H.I., Dimitrova, A., Marrink, S.J., Li, Z., Vénien-Bryan, C., Sobott, F., Koçer,
A. (2014) Global structural changes of an ion channel during its gating are followed by ion mobility mass
spectrometry. Proc. Natl. Acad. Sci. USA 111:17170–17175.
Laganowsky, A., Reading, E., Allison, T.M., Ulmschneider, M.B., Degiacomi, M.T., Baldwin, A.J., Robinson,
C.V. (2014) Membrane proteins bind lipids selectively to modulate their structure and function. Nature 510:172–175.
Laganowsky, A., Reading, E., Hopper, T.S., Robinson, C.V. (2013) Mass spectrometry of intact membrane protein
complexes. Nat. Protoc. 8:639–651.
le Maire, M., Champeil, P., Møller, J.V. (2000) Interaction of membrane proteins and lipids with solubilizing detergents.
Biochim. Biophys. Acta 1508:86–111.
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.
Liu, L., Bagal, D., Kitova, E.N., Schnier, P.D., Klassen, J.S. (2009) Hydrophobic proteinÀligand interactions preserved
in the gas phase. J. Am. Chem. Soc. 131:15980–15981.
Lu, Y., Zhang, H., Niedzwiedzki, D.M., Jiang, J., Blankenship, R.E., Gross, M.L. (2016) Fast photochemical oxidation
of proteins maps the topology of intrinsic membrane proteins: Light-Harvesting Complex 2 in a nanodisc. Anal.
Chem. 88:8827–8834.
Mann, M., Jensen, O.N. (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21:255–261.
Marklund, E.G., Degiacomi, M.T., Robinson, C.V., Baldwin, A.J., Benesch, J.L. (2015) Collision cross-sections for
structural proteomics. Structure 23:791–799.
Martens, C., Stein, R.A., Masureel, M., Roth, A., Mishra, S., Dawaliby, R., Konijnenberg, A., Sobott, F., Govaerts, C.,
McHaourab, H.S. (2016) Lipids modulate the conformational dynamics of a secondary multidrug transporter. Nat.
Struct. Mol. Biol. 23:744–751.
Marty, M.T., Hoi, K.K., Gault, J., Robinson, C.V. (2016a) Probing the lipid annular belt by gas-phase dissociation of
membrane proteins in nanodiscs. Angew. Chem. Int. Ed. 55:550–554.
Marty, M.T., Hoi, K.K., Robinson, C.V. (2016b) Interfacing membrane mimetics with mass spectrometry. Acc. Chem.
Res. 49:2459–2467.
Mehmood, S., Allison, T.M., Robinson, C.V. (2015) Mass spectrometry of protein complexes: from origins to
applications. Annu. Rev. Phys. Chem. 66:453–474.
Mesleh, M.F., Hunter, J.M., Shvartsburg, A.A., Schatz, G.C., Jarrold, M.F. (1996) Structural information from ion
mobility measurements: Effects of the long-range potential. J. Phys. Chem. 100:16082–16086.
Morgner, N., Kleinschroth, T., Barth, H.D., Ludwig, B., Brutschy, B. (2007) A novel approach to analyze membrane
proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom.
18:1429–1438.
Ning, Z., Hawley, B., Seebun, D., Figeys, D. (2014) APols-aided protein precipitation: a rapid method for concentrating
proteins for proteomic analysis. J. Membr. Biol. 247:941–947.
656
14 The Use of Amphipols in Mass Spectrometry
polymères amphiphiles: les amphipols. Rapport de DEA, Université Paris VI, Paris, 28 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.
Hall, Z., Robinson, C.V. (2012) Do charge state signatures guarantee protein conformations? J. Am. Soc. Mass Spectrom.
23:1161–1168.
Hebling, C.M., Morgan, C.R., Stafford, D.W., Jorgenson, J.W., Rand, K.D., Engen, J.R. (2010) Conformational analysis
of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry. Anal. Chem.
82:5415–5419.
Hernandez, H., Robinson, C.V. (2007) Determining the stoichiometry and interactions of macromolecular assemblies
from mass spectrometry. Nat. Protocols 2:715–726.
Hilton, G.R., Benesch, J.L. (2012) Two decades of studying non-covalent biomolecular assemblies by means of
electrospray ionization mass spectrometry. J. R. Soc. Interface 9:801–816.
Hopper, J.T.S., Yu, Y.T.-C., Li, D., Raymond, A., Bostock, M., Liko, I., Mikhailov, V., Laganowsky, A., Benesch, J.L.
P., Caffrey, M., Nietlispach, D., Robinson, C.V. (2013) Detergent-free mass spectrometry of membrane protein
complexes. Nat. Meth. 10:1206–1208.
Juraschek, R., Dülcks, T., Karas, M. (1999) Nanoelectrospray–more than just a minimized-flow electrospray ionization
source J. Am. Soc. Mass Spectrom. 10:300–308.
Kanu, A.B., Dwivedi, P., Tam, M., Matz, L., Hill Jr., H.H. (2008) Ion mobility-mass spectrometry. J. Mass Spectrom.
43:1–22.
Konijnenberg, A., van Dyck, J.F., Kailing, L.L., Sobott, F. (2015) Extending native mass spectrometry approaches to
integral membrane proteins. Biol. Chem. 396:991–1002.
Konijnenberg, A., Yilmaz, D., Ingólfsson, H.I., Dimitrova, A., Marrink, S.J., Li, Z., Vénien-Bryan, C., Sobott, F., Koçer,
A. (2014) Global structural changes of an ion channel during its gating are followed by ion mobility mass
spectrometry. Proc. Natl. Acad. Sci. USA 111:17170–17175.
Laganowsky, A., Reading, E., Allison, T.M., Ulmschneider, M.B., Degiacomi, M.T., Baldwin, A.J., Robinson,
C.V. (2014) Membrane proteins bind lipids selectively to modulate their structure and function. Nature 510:172–175.
Laganowsky, A., Reading, E., Hopper, T.S., Robinson, C.V. (2013) Mass spectrometry of intact membrane protein
complexes. Nat. Protoc. 8:639–651.
le Maire, M., Champeil, P., Møller, J.V. (2000) Interaction of membrane proteins and lipids with solubilizing detergents.
Biochim. Biophys. Acta 1508:86–111.
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.
Liu, L., Bagal, D., Kitova, E.N., Schnier, P.D., Klassen, J.S. (2009) Hydrophobic proteinÀligand interactions preserved
in the gas phase. J. Am. Chem. Soc. 131:15980–15981.
Lu, Y., Zhang, H., Niedzwiedzki, D.M., Jiang, J., Blankenship, R.E., Gross, M.L. (2016) Fast photochemical oxidation
of proteins maps the topology of intrinsic membrane proteins: Light-Harvesting Complex 2 in a nanodisc. Anal.
Chem. 88:8827–8834.
Mann, M., Jensen, O.N. (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21:255–261.
Marklund, E.G., Degiacomi, M.T., Robinson, C.V., Baldwin, A.J., Benesch, J.L. (2015) Collision cross-sections for
structural proteomics. Structure 23:791–799.
Martens, C., Stein, R.A., Masureel, M., Roth, A., Mishra, S., Dawaliby, R., Konijnenberg, A., Sobott, F., Govaerts, C.,
McHaourab, H.S. (2016) Lipids modulate the conformational dynamics of a secondary multidrug transporter. Nat.
Struct. Mol. Biol. 23:744–751.
Marty, M.T., Hoi, K.K., Gault, J., Robinson, C.V. (2016a) Probing the lipid annular belt by gas-phase dissociation of
membrane proteins in nanodiscs. Angew. Chem. Int. Ed. 55:550–554.
Marty, M.T., Hoi, K.K., Robinson, C.V. (2016b) Interfacing membrane mimetics with mass spectrometry. Acc. Chem.
Res. 49:2459–2467.
Mehmood, S., Allison, T.M., Robinson, C.V. (2015) Mass spectrometry of protein complexes: from origins to
applications. Annu. Rev. Phys. Chem. 66:453–474.
Mesleh, M.F., Hunter, J.M., Shvartsburg, A.A., Schatz, G.C., Jarrold, M.F. (1996) Structural information from ion
mobility measurements: Effects of the long-range potential. J. Phys. Chem. 100:16082–16086.
Morgner, N., Kleinschroth, T., Barth, H.D., Ludwig, B., Brutschy, B. (2007) A novel approach to analyze membrane
proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom.
18:1429–1438.
Ning, Z., Hawley, B., Seebun, D., Figeys, D. (2014) APols-aided protein precipitation: a rapid method for concentrating
proteins for proteomic analysis. J. Membr. Biol. 247:941–947.
656
14 The Use of Amphipols in Mass Spectrometry