Howell, S.C., Mesleh, M.F., Opella, S.J. (2005) NMR structure determination of a membrane protein with two
transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry
44:5196–5206.
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.
Kang, C.B., Li, Q. (2011) Solution NMR study of integral membrane proteins. Curr. Opin. Struct. Biol. 15:560–569.
Kaplan, M., Pinto, C., Houben, K., Baldus, M. (2016) Nuclear magnetic resonance (NMR) applied to membrane-protein
complexes. Quart. Rev. Biophys. 49:1–25.
Kay, L.E. (2001) Nuclear magnetic resonance methods for high molecular weight proteins: a study involving a complex
of maltose binding protein and betacyclodextrin. Meth. Enzymol. 339B:174–203.
Kay, L.E., Ikura, M., Tschudin, R., Bax, A. (1990) Three-dimensional triple resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89:496–514.
Kim, H.M., Howell, S.C., Van Horn, W.D., Jeon, Y.H., Sanders, C.R. (2009) Recent advances in the application of
solution NMR spectroscopy to multi-span integral membrane proteins. Progr. Nucl. Magn. Reson. Spectrosc.
55:335–360.
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.
Kraft, T.E., Hresko, R.C., Hruz, P.W. (2015) Expression, purification, and functional characterization of the insulinresponsive facilitative glucose transporter GLUT4. Protein Sci. 24:2008–2019.
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, D., Hilty, C., Wider, G., Wüthrich, K. (2006) Effective rotational correlation times of proteins from NMR relaxation
interference. J. Magn. Reson. 178:72–76.
Lee, D., Walter, K.F., Brückner, A.K., Hilty, C., Becker, S., Griesinger, C. (2008) Bilayer in small bicelles revealed by
lipid-protein interactions using NMR spectroscopy. J. Am. Chem. Soc. 130:13822–13823.
Li, D., Li, J., Zhuang, Y., Zhang, L., Xiong, Y., Shi, P., Tian, C. (2015) Nano-size uni-lamellar lipodisq-improved in situ
auto-phosphorylation analysis of E. coli tyrosine kinase using
19
F nuclear magnetic resonance. Protein Cell
6:229–233.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2014) Single particle electron cryo-microscopy of a mammalian ion channel.
Curr. Opin. Struct. Biol. 27:1–7.
MacKenzie, K.R., Prestegard, J.H., Engelman, D.M. (1997) A transmembrane helix dimer: structure and implications.
Science 276:131–133.
Marcotte, I., Auger, M. (2005) Bicelles as model membranes for solid- and solution-state NMR studies of membrane
peptides and proteins. Concepts Magn. Reson. 24A:17–37.
Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., Popot, J.-L. (2002) Allosteric
transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical
constraints. FEBS Lett. 528:251–256.
Milić, D., Veprintsev, D.B. (2015) Large-scale production and protein engineering of G protein-coupled receptors for
structural studies. Frontiers Pharmacol. 6:66.
Mineev, K.S., Nadezhdin, K.D. (2017) Membrane mimetics for solution NMR studies of membrane proteins. Nanotech.
Rev. 6:15–32.
Nietlispach, D., Gautier, A. (2011) Solution NMR studies of polytopic alpha-helical membrane proteins. Curr. Opin.
Struct. Biol. 21:497–508.
Opella, S.J., Marassi, F.M. (2004) Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev.
104:3587–3606.
Opella, S.J., Marassi, F.M. (2017) Applications of NMR to membrane proteins. Arch. Biochem. Biophys. 628:92–101.
Page, R.C., Moore, J.D., Nguyen, H.B., Sharma, M., Chase, R., Gao, F.P., Mobley, C.K., Sanders, C.R., Ma, L.,
Sönnichsen, F.D., Lee, S., Howell, S.C., Opella, S.J., Cross, T.A. (2006) Comprehensive evaluation of solution
nuclear magnetic resonance spectroscopy sample preparation for helical integral membrane proteins. J. Struct. Func.
Genom. 7:51–64.
Patching, S.G. (2011) NMR structures of polytopic integral membrane proteins. Mol. Membr. Biol. 28:370–397.
Patching, S.G. (2015) Solid-state NMR structures of integral membrane proteins. Mol. Membr. Biol. 32:156–178.
Pautsch, A., Schulz, G.E. (1998) Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol.
5:1013–1017.
Pautsch, A., Schulz, G.E. (2000) High-resolution structure of the OmpA membrane domain. J. Mol. Biol. 298:273–282.
References
493
transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry
44:5196–5206.
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.
Kang, C.B., Li, Q. (2011) Solution NMR study of integral membrane proteins. Curr. Opin. Struct. Biol. 15:560–569.
Kaplan, M., Pinto, C., Houben, K., Baldus, M. (2016) Nuclear magnetic resonance (NMR) applied to membrane-protein
complexes. Quart. Rev. Biophys. 49:1–25.
Kay, L.E. (2001) Nuclear magnetic resonance methods for high molecular weight proteins: a study involving a complex
of maltose binding protein and betacyclodextrin. Meth. Enzymol. 339B:174–203.
Kay, L.E., Ikura, M., Tschudin, R., Bax, A. (1990) Three-dimensional triple resonance NMR spectroscopy of isotopically enriched proteins. J. Magn. Reson. 89:496–514.
Kim, H.M., Howell, S.C., Van Horn, W.D., Jeon, Y.H., Sanders, C.R. (2009) Recent advances in the application of
solution NMR spectroscopy to multi-span integral membrane proteins. Progr. Nucl. Magn. Reson. Spectrosc.
55:335–360.
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.
Kraft, T.E., Hresko, R.C., Hruz, P.W. (2015) Expression, purification, and functional characterization of the insulinresponsive facilitative glucose transporter GLUT4. Protein Sci. 24:2008–2019.
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, D., Hilty, C., Wider, G., Wüthrich, K. (2006) Effective rotational correlation times of proteins from NMR relaxation
interference. J. Magn. Reson. 178:72–76.
Lee, D., Walter, K.F., Brückner, A.K., Hilty, C., Becker, S., Griesinger, C. (2008) Bilayer in small bicelles revealed by
lipid-protein interactions using NMR spectroscopy. J. Am. Chem. Soc. 130:13822–13823.
Li, D., Li, J., Zhuang, Y., Zhang, L., Xiong, Y., Shi, P., Tian, C. (2015) Nano-size uni-lamellar lipodisq-improved in situ
auto-phosphorylation analysis of E. coli tyrosine kinase using
19
F nuclear magnetic resonance. Protein Cell
6:229–233.
Liao, M., Cao, E., Julius, D., Cheng, Y. (2014) Single particle electron cryo-microscopy of a mammalian ion channel.
Curr. Opin. Struct. Biol. 27:1–7.
MacKenzie, K.R., Prestegard, J.H., Engelman, D.M. (1997) A transmembrane helix dimer: structure and implications.
Science 276:131–133.
Marcotte, I., Auger, M. (2005) Bicelles as model membranes for solid- and solution-state NMR studies of membrane
peptides and proteins. Concepts Magn. Reson. 24A:17–37.
Martinez, K.L., Gohon, Y., Corringer, P.-J., Tribet, C., Mérola, F., Changeux, J.-P., Popot, J.-L. (2002) Allosteric
transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical
constraints. FEBS Lett. 528:251–256.
Milić, D., Veprintsev, D.B. (2015) Large-scale production and protein engineering of G protein-coupled receptors for
structural studies. Frontiers Pharmacol. 6:66.
Mineev, K.S., Nadezhdin, K.D. (2017) Membrane mimetics for solution NMR studies of membrane proteins. Nanotech.
Rev. 6:15–32.
Nietlispach, D., Gautier, A. (2011) Solution NMR studies of polytopic alpha-helical membrane proteins. Curr. Opin.
Struct. Biol. 21:497–508.
Opella, S.J., Marassi, F.M. (2004) Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev.
104:3587–3606.
Opella, S.J., Marassi, F.M. (2017) Applications of NMR to membrane proteins. Arch. Biochem. Biophys. 628:92–101.
Page, R.C., Moore, J.D., Nguyen, H.B., Sharma, M., Chase, R., Gao, F.P., Mobley, C.K., Sanders, C.R., Ma, L.,
Sönnichsen, F.D., Lee, S., Howell, S.C., Opella, S.J., Cross, T.A. (2006) Comprehensive evaluation of solution
nuclear magnetic resonance spectroscopy sample preparation for helical integral membrane proteins. J. Struct. Func.
Genom. 7:51–64.
Patching, S.G. (2011) NMR structures of polytopic integral membrane proteins. Mol. Membr. Biol. 28:370–397.
Patching, S.G. (2015) Solid-state NMR structures of integral membrane proteins. Mol. Membr. Biol. 32:156–178.
Pautsch, A., Schulz, G.E. (1998) Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol.
5:1013–1017.
Pautsch, A., Schulz, G.E. (2000) High-resolution structure of the OmpA membrane domain. J. Mol. Biol. 298:273–282.
References
493