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.
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.
He, Y., Gao, X., Goswami, D., Hou, L., Pal, K., Yin, Y., Zhao, G., Ernst, O.P., Griffin, P., Melcher, K., Xu, H.E. (2017)
Molecular assembly of rhodopsin with G protein-coupled receptor kinases. Cell Res. 2017:1–20.
Hénault, C.M., Sun, J., Therien, J.P.D., daCosta, C.J.B., Carswell, C.L., Labriola, J.M., Juranka, P.F., Baenziger,
J.E. (2015) The role of the M4 lipid-sensor in the folding, trafficking, and allosteric modulation of nicotinic
acetylcholine receptors. Neuropharmacology 96:157–168.
Hilf, R.J., Dutzler, R. (2009) Structure of a potentially open state of a proton-activated pentameric ligand-gated ion
channel. Nature 457:115–118.
Hirai, T., Subramaniam, S., Lanyi, J.K. (2009) Structural snapshots of conformational changes in a seven-helix
membrane protein: lessons from bacteriorhodopsin. Curr. Opin. Struct. Biol. 19:433–439.
Hong, H., Tamm, L.K. (2004) Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc. Natl.
Acad. Sci. USA 101:4065–4070.
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.
Huang, K.-S., Bayley, H., Liao, M.-J., London, E., Khorana, H.G. (1981) Refolding of an integral membrane protein.
Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol.
Chem. 256:3802–3809.
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.
Ireland, S.M., Sula, S., Wallace, B.A. (2017) Thermal melt circular dichroism spectroscopic studies for identifying
stabilising amphipathic molecules for the voltage-gated sodium channel NavMs. Biopolymers 2017:e23067.
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.T.,
Overduin, M., Dafforn, T.R. (2011) Surfactant-free purification of membrane proteins with intact native membrane
environment. Biochem. Soc. Trans. 39:813–818.
Jeong, H., Kim, J.-S., Song, S., Shigematsu, H., Yokoyama, T., Hyun, J., Ha, N.-C. (2016) Pseudoatomic structure of the
tripartite multidrug efflux pump AcrAB-TolC reveals the intermeshing cogwheel-like interaction between AcrA and
TolC. Structure 24:272–276.
Jin, P., Bulkley, D., Guo, Y., Zhang, W., Guo, Z., Huynh, W., Wu, S., Meltzer, S., Cheng, T., Jan, L.Y., Jan, Y.-N.,
Cheng, Y. (2017) Electron cryo-microscopy structure of the mechanotransduction channel NOMPC. Nature
547:118–122.
Joshi, M., Dracheva, S., Mukhopadhyay, A.K., Bose, S., Hendler, R.W. (1998) Importance of specific native lipids in
controlling the photocycle of bacteriorhodopsin. Biochemistry 37:14463–14470.
Kevany, B.M., Tsybovsky, Y., Campuzano, I.D.G., Schnier, P.D., Engel, A., Palczewski, K. (2013) Structural and
functional analysis of the native peripherin-ROM1 complex isolated from photoreceptor cells. J. Biol. Chem.
288:36272–36284.
Kievit, O., Brudvig, G.W. (2001) Direct electrochemistry of photosystem I. J. Electroanal. Chem. 497:139–149.
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.
326
5 Formation and Properties of Membrane Protein/Amphipol Complexes
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.
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.
He, Y., Gao, X., Goswami, D., Hou, L., Pal, K., Yin, Y., Zhao, G., Ernst, O.P., Griffin, P., Melcher, K., Xu, H.E. (2017)
Molecular assembly of rhodopsin with G protein-coupled receptor kinases. Cell Res. 2017:1–20.
Hénault, C.M., Sun, J., Therien, J.P.D., daCosta, C.J.B., Carswell, C.L., Labriola, J.M., Juranka, P.F., Baenziger,
J.E. (2015) The role of the M4 lipid-sensor in the folding, trafficking, and allosteric modulation of nicotinic
acetylcholine receptors. Neuropharmacology 96:157–168.
Hilf, R.J., Dutzler, R. (2009) Structure of a potentially open state of a proton-activated pentameric ligand-gated ion
channel. Nature 457:115–118.
Hirai, T., Subramaniam, S., Lanyi, J.K. (2009) Structural snapshots of conformational changes in a seven-helix
membrane protein: lessons from bacteriorhodopsin. Curr. Opin. Struct. Biol. 19:433–439.
Hong, H., Tamm, L.K. (2004) Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc. Natl.
Acad. Sci. USA 101:4065–4070.
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.
Huang, K.-S., Bayley, H., Liao, M.-J., London, E., Khorana, H.G. (1981) Refolding of an integral membrane protein.
Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol.
Chem. 256:3802–3809.
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.
Ireland, S.M., Sula, S., Wallace, B.A. (2017) Thermal melt circular dichroism spectroscopic studies for identifying
stabilising amphipathic molecules for the voltage-gated sodium channel NavMs. Biopolymers 2017:e23067.
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.T.,
Overduin, M., Dafforn, T.R. (2011) Surfactant-free purification of membrane proteins with intact native membrane
environment. Biochem. Soc. Trans. 39:813–818.
Jeong, H., Kim, J.-S., Song, S., Shigematsu, H., Yokoyama, T., Hyun, J., Ha, N.-C. (2016) Pseudoatomic structure of the
tripartite multidrug efflux pump AcrAB-TolC reveals the intermeshing cogwheel-like interaction between AcrA and
TolC. Structure 24:272–276.
Jin, P., Bulkley, D., Guo, Y., Zhang, W., Guo, Z., Huynh, W., Wu, S., Meltzer, S., Cheng, T., Jan, L.Y., Jan, Y.-N.,
Cheng, Y. (2017) Electron cryo-microscopy structure of the mechanotransduction channel NOMPC. Nature
547:118–122.
Joshi, M., Dracheva, S., Mukhopadhyay, A.K., Bose, S., Hendler, R.W. (1998) Importance of specific native lipids in
controlling the photocycle of bacteriorhodopsin. Biochemistry 37:14463–14470.
Kevany, B.M., Tsybovsky, Y., Campuzano, I.D.G., Schnier, P.D., Engel, A., Palczewski, K. (2013) Structural and
functional analysis of the native peripherin-ROM1 complex isolated from photoreceptor cells. J. Biol. Chem.
288:36272–36284.
Kievit, O., Brudvig, G.W. (2001) Direct electrochemistry of photosystem I. J. Electroanal. Chem. 497:139–149.
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.
326
5 Formation and Properties of Membrane Protein/Amphipol Complexes