(iii) Cell-free expression (CFE) in vitro, in a lysate generally derived either from E. coli or from
wheat germs. The protein may be either left to precipitate, and later solubilized with a
detergent, or integrated into an accepting amphipathic medium, such as lipid vesicles,
detergent micelles, APols, or nanodiscs.
(iv) For short MPs or MP fragments, one may also resort to chemical synthesis.
Routes (i) and (ii) are discussed in Chap. 6 along with the application of APols to folding
denatured MPs, route (iii) in Chap. 7, along with their use for CFE. APols and other nonconventional
surfactants have not been applied yet to chemical synthesis of MPs, which is therefore beyond the
frame of this book.
References
Alberts, B., Johnson, A., Lewis, J., Morgan, D., Raff, M., Roberts, K., Walter, P. (2015) Molecular Biology of the Cell.
Sixth Edition, Garland Publishing, Inc., New York & London.
Allen, L.C. (1975) A model for the hydrogen bond. Proc. Natl. Acad. Sci. USA 72:4701–4705.
Althoff, T., Hibbs, R.E., Banerjee, S., Gouaux, E. (2014) X-ray structures of GluCl in apo states reveal a gating
mechanism of Cys-loop receptors. Nature 512:333–337.
Althoff, T., Mills, D.J., Popot, J.-L., Kühlbrandt, W. (2011) Assembly of electron transport chain components in bovine
mitochondrial supercomplex I 1 III 2 IV 1 . EMBO J. 30:4652–4664.
Amzel, L.M. (1997) Loss of translational entropy in binding, folding, and catalysis. Proteins 28:144–149.
Andersen, O.S., Koeppe, R.E., 2nd. (2007) Bilayer thickness and membrane protein function: an energetic perspective.
Annu. Rev. Biophys. Biomol. Struct. 36:107–130.
Andersson, M., Malmerberg, E., Westenhoff, S., Katona, G., Cammarata, M., Wöhri, A.B., Johansson, L.C., Ewald, F.,
Eklund, M., Wulff, M., Davidsson, J., Neutze, R. (2009) Structural dynamics of light-driven proton pumps. Structure
17:1265–1275.
Anishkin, A., Loukin, S.H., Teng, J., Kung, C. (2014) Feeling the hidden mechanical forces in lipid bilayer is an original
sense. Proc. Natl. Acad. Sci. USA 111:7898–7905.
Arora, A., Abildgaard, F., Bushweller, J.H., Tamm, L.K. (2001) Structure of outer membrane protein A transmembrane
domain by NMR spectroscopy. Nat. Struct. Biol. 8:334–338.
Auerbach, A. (2015) Agonist activation of a nicotinic acetylcholine receptor. Neuropharmacology 96:150–156.
Baenziger, J.E., Hénault, C.M., Therien, J.P.D., Sun, J. (2015) Nicotinic acetylcholine receptor-lipid interactions:
Mechanistic insight and biological function. Biochim. Biophys. Acta 1848:1806–1817.
Baradaran, R., Berrisford, J.M., Minhas, G.S., Sazanov, L.A. (2013) Crystal structure of the entire respiratory complex
I. Nature 494:443–448.
Barrantes, F.J. (2015) Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channels.
Biochim. Biophys. Acta 1848:1796–1805.
Battle, A.R., Ridone, P., Bavi, N., Nakayama, Y., Nikolaev, Y.A., Martinac, B. (2015) Lipid–protein interactions:
Lessons learned from stress. Biochim. Biophys. Acta 1848:1744–1756.
Blobel, G. (1980) Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77:1496–1500.
Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J.-P., Delarue, M., Corringer, P.-J. (2009) X-ray structure
of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457:111–114.
Brejc, K., van Dijk, W.J., Klaassen, R.V., Schuurmans, M., van Der Oost, J., Smit, A.B., Sixma, T.K. (2001) Crystal
structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411:269–276.
Brisson, A., Unwin, N. (1985) Quaternary structure of the acetylcholine receptor. Nature 315:474–477.
Brown, L.S., Ernst, O.P. (2017) Recent advances in biophysical studies of rhodopsins – Oligomerization, folding, and
structure. Biochim. Biophys. Acta 1865:1512–1521.
Buchanan, S.K., Smith, B.S., Venkatramani, L., Xia, D., Esser, L., Palnitkar, M., Chakraborty, R., van der Helm, D.,
Deisenhofer, J. (1999) Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nature
Struct. Biol. 6:56–63.
Buchanan, S.K., Yamashita, S., Fleming, K.G. (2012) Structure and folding of outer membrane proteins, in: Tamm, L.K.,
ed., Membranes. Elsevier, Oxford:Academic Press, pp. 139–163.
Calimet, N., Simoes, M., Changeux, J.-P., Karplus, M., Talye, A., Cecchini, M. (2013) A gating mechanism of
pentameric ligand-gated ion channels. Proc. Natl. Acad. Sci. USA 110:E3987–3996.
Carafoli, E. (2002) Calcium signaling: a tale for all seasons. Proc. Natl. Acad. Sci. USA 99:1115–1122.
References
51
wheat germs. The protein may be either left to precipitate, and later solubilized with a
detergent, or integrated into an accepting amphipathic medium, such as lipid vesicles,
detergent micelles, APols, or nanodiscs.
(iv) For short MPs or MP fragments, one may also resort to chemical synthesis.
Routes (i) and (ii) are discussed in Chap. 6 along with the application of APols to folding
denatured MPs, route (iii) in Chap. 7, along with their use for CFE. APols and other nonconventional
surfactants have not been applied yet to chemical synthesis of MPs, which is therefore beyond the
frame of this book.
References
Alberts, B., Johnson, A., Lewis, J., Morgan, D., Raff, M., Roberts, K., Walter, P. (2015) Molecular Biology of the Cell.
Sixth Edition, Garland Publishing, Inc., New York & London.
Allen, L.C. (1975) A model for the hydrogen bond. Proc. Natl. Acad. Sci. USA 72:4701–4705.
Althoff, T., Hibbs, R.E., Banerjee, S., Gouaux, E. (2014) X-ray structures of GluCl in apo states reveal a gating
mechanism of Cys-loop receptors. Nature 512:333–337.
Althoff, T., Mills, D.J., Popot, J.-L., Kühlbrandt, W. (2011) Assembly of electron transport chain components in bovine
mitochondrial supercomplex I 1 III 2 IV 1 . EMBO J. 30:4652–4664.
Amzel, L.M. (1997) Loss of translational entropy in binding, folding, and catalysis. Proteins 28:144–149.
Andersen, O.S., Koeppe, R.E., 2nd. (2007) Bilayer thickness and membrane protein function: an energetic perspective.
Annu. Rev. Biophys. Biomol. Struct. 36:107–130.
Andersson, M., Malmerberg, E., Westenhoff, S., Katona, G., Cammarata, M., Wöhri, A.B., Johansson, L.C., Ewald, F.,
Eklund, M., Wulff, M., Davidsson, J., Neutze, R. (2009) Structural dynamics of light-driven proton pumps. Structure
17:1265–1275.
Anishkin, A., Loukin, S.H., Teng, J., Kung, C. (2014) Feeling the hidden mechanical forces in lipid bilayer is an original
sense. Proc. Natl. Acad. Sci. USA 111:7898–7905.
Arora, A., Abildgaard, F., Bushweller, J.H., Tamm, L.K. (2001) Structure of outer membrane protein A transmembrane
domain by NMR spectroscopy. Nat. Struct. Biol. 8:334–338.
Auerbach, A. (2015) Agonist activation of a nicotinic acetylcholine receptor. Neuropharmacology 96:150–156.
Baenziger, J.E., Hénault, C.M., Therien, J.P.D., Sun, J. (2015) Nicotinic acetylcholine receptor-lipid interactions:
Mechanistic insight and biological function. Biochim. Biophys. Acta 1848:1806–1817.
Baradaran, R., Berrisford, J.M., Minhas, G.S., Sazanov, L.A. (2013) Crystal structure of the entire respiratory complex
I. Nature 494:443–448.
Barrantes, F.J. (2015) Phylogenetic conservation of protein-lipid motifs in pentameric ligand-gated ion channels.
Biochim. Biophys. Acta 1848:1796–1805.
Battle, A.R., Ridone, P., Bavi, N., Nakayama, Y., Nikolaev, Y.A., Martinac, B. (2015) Lipid–protein interactions:
Lessons learned from stress. Biochim. Biophys. Acta 1848:1744–1756.
Blobel, G. (1980) Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77:1496–1500.
Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J.-P., Delarue, M., Corringer, P.-J. (2009) X-ray structure
of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457:111–114.
Brejc, K., van Dijk, W.J., Klaassen, R.V., Schuurmans, M., van Der Oost, J., Smit, A.B., Sixma, T.K. (2001) Crystal
structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411:269–276.
Brisson, A., Unwin, N. (1985) Quaternary structure of the acetylcholine receptor. Nature 315:474–477.
Brown, L.S., Ernst, O.P. (2017) Recent advances in biophysical studies of rhodopsins – Oligomerization, folding, and
structure. Biochim. Biophys. Acta 1865:1512–1521.
Buchanan, S.K., Smith, B.S., Venkatramani, L., Xia, D., Esser, L., Palnitkar, M., Chakraborty, R., van der Helm, D.,
Deisenhofer, J. (1999) Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nature
Struct. Biol. 6:56–63.
Buchanan, S.K., Yamashita, S., Fleming, K.G. (2012) Structure and folding of outer membrane proteins, in: Tamm, L.K.,
ed., Membranes. Elsevier, Oxford:Academic Press, pp. 139–163.
Calimet, N., Simoes, M., Changeux, J.-P., Karplus, M., Talye, A., Cecchini, M. (2013) A gating mechanism of
pentameric ligand-gated ion channels. Proc. Natl. Acad. Sci. USA 110:E3987–3996.
Carafoli, E. (2002) Calcium signaling: a tale for all seasons. Proc. Natl. Acad. Sci. USA 99:1115–1122.
References
51