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105:17742–17747.
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von Heijne, G. (1986) The distribution of positively charged residues in bacterial inner membrane proteins correlates
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eukaryotic organisms. Protein Sci. 7:1029–1038.
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Weiss, M.S., Kreusch, A., Schiltz, E., Nestel, U., Welte, W., Weckesser, J., Schulz, G.E. (1991b) The structure of porin
from Rhodobacter capsulatus at 1.8 Å resolution. FEBS Lett. 280:379–382.
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structure of porin from Rhodobacter capsulatus at 0.6 nm resolution. FEBS Lett. 256:143–146.
Wenz, T., Hielscher, R., Hellwig, P., Schägger, H., Richers, S., Hunte, C. (2009) Role of phospholipids in respiratory
cytochrome bc 1 complex catalysis and supercomplex formation. Biochim. Biophys. Acta 1787:609–616.
White, S.H., von Heijne, G., Engelman, D.M. (2018) Cell Boundaries: How Membranes and Their Proteins Work.
Garland, New York, in preparation.
White, S.H., Wimley, W.C. (1999) Membrane protein folding and stability : physical principles. Annu. Rev. Biophys.
Biomol. Struct. 28:319–365.
Wickstrand, C., Dods, R., Royant, A., Neutze, R. (2015) Bacteriorhodopsin: Would the real structural intermediates
please stand up? Biochim. Biophys. Acta 1850:536–553.
Xia, D., Yu, C.-A., Kim, H., Xia, J.-Z., Kachurin, A.M., Zhang, L., Yu, L., Deisenhofer, J. (1997) Crystal structure of the
cytochrome bc 1 complex from bovine heart mitochondria. Science 277:60–66.
Zaccai, G. (2000) Moist and soft, dry and stiff: a review of neutron experiments on hydration-dynamics-activity relations
in the purple membrane of Halobacterium salinarum. Biophys. Chem. 86:249–257.
Zaccai, G. (2004) The effect of water on protein dynamics. Phil. Trans. R. Soc. Lond. B 359:1269–1275.
Zhou, Y., Morais-Cabral, J.H., Kaufman, A., MacKinnon, R. (2001) Chemistry of ion coordination and hydration
revealed by a K
+ channel-F ab complex at 2.0 Å resolution. Nature 414:43–48.
Zorman, S., Botte, M., Jiang, Q., Collinson, I., Schaffitzel, C. (2015) Advances and challenges of membrane-protein
complex production. Curr. Opin. Struct. Biol. 32:123–130.
References
57
Yoshikawa, S. (1996) The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science
272:1136–1144.
Ujwal, R., Cascio, D., Colletier, J.-P., Faham, S., Zhang, J., Toro, L., Ping, P., Abramson, J. (2008) The crystal structure
of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating. Proc. Natl. Acad. Sci. USA
105:17742–17747.
Unwin, N. (2005) Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J. Mol. Biol. 346:967–989.
Unwin, N. (2013) Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from
Torpedo postsynaptic membranes. Quart. Rev. Biophys. 46:283–322.
Unwin, N., Fujiyoshi, Y. (2012) Gating movement of acetylcholine receptor caught by plunge-freezing. J. Mol. Biol.
422:616–634.
Valiyaveetil, F.I., Zhou, Y., MacKinnon, R. (2002) Lipids in the structure, folding, and function of the KcsA K
+ channel.
Biochemistry 41:10771–10777.
Vinothkumar, K.R. (2011) Structure of rhomboid protease in a lipid environment. J. Mol. Biol. 407:232–247.
Vinothkumar, K.R., Henderson, R. (2010) Structures of membrane proteins. Q. Rev. Biophys. 43:65–158.
Vinothkumar, K.R., Zhu, J., Hirst, J. (2014) Architecture of mammalian respiratory complex I. Nature 515:80–84.
von Heijne, G. (1986) The distribution of positively charged residues in bacterial inner membrane proteins correlates
with the trans-membrane topology. EMBO J. 5:3021–3027.
Wallin, E., von Heijne, G. (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archean, and
eukaryotic organisms. Protein Sci. 7:1029–1038.
Weiss, M.S., Abele, U., Weckesser, J., Welte, W., Schiltz, E., Schulz, G.E. (1991a) Molecular architecture and
electrostatic properties of a bacterial porin. Science 254:1627–1630.
Weiss, M.S., Kreusch, A., Schiltz, E., Nestel, U., Welte, W., Weckesser, J., Schulz, G.E. (1991b) The structure of porin
from Rhodobacter capsulatus at 1.8 Å resolution. FEBS Lett. 280:379–382.
Weiss, M.S., Wacker, T., Nestel, U., Woitzik, D., Weckesser, J., Kreutz, W., Welte, W., Schulz, G.E. (1989) The
structure of porin from Rhodobacter capsulatus at 0.6 nm resolution. FEBS Lett. 256:143–146.
Wenz, T., Hielscher, R., Hellwig, P., Schägger, H., Richers, S., Hunte, C. (2009) Role of phospholipids in respiratory
cytochrome bc 1 complex catalysis and supercomplex formation. Biochim. Biophys. Acta 1787:609–616.
White, S.H., von Heijne, G., Engelman, D.M. (2018) Cell Boundaries: How Membranes and Their Proteins Work.
Garland, New York, in preparation.
White, S.H., Wimley, W.C. (1999) Membrane protein folding and stability : physical principles. Annu. Rev. Biophys.
Biomol. Struct. 28:319–365.
Wickstrand, C., Dods, R., Royant, A., Neutze, R. (2015) Bacteriorhodopsin: Would the real structural intermediates
please stand up? Biochim. Biophys. Acta 1850:536–553.
Xia, D., Yu, C.-A., Kim, H., Xia, J.-Z., Kachurin, A.M., Zhang, L., Yu, L., Deisenhofer, J. (1997) Crystal structure of the
cytochrome bc 1 complex from bovine heart mitochondria. Science 277:60–66.
Zaccai, G. (2000) Moist and soft, dry and stiff: a review of neutron experiments on hydration-dynamics-activity relations
in the purple membrane of Halobacterium salinarum. Biophys. Chem. 86:249–257.
Zaccai, G. (2004) The effect of water on protein dynamics. Phil. Trans. R. Soc. Lond. B 359:1269–1275.
Zhou, Y., Morais-Cabral, J.H., Kaufman, A., MacKinnon, R. (2001) Chemistry of ion coordination and hydration
revealed by a K
+ channel-F ab complex at 2.0 Å resolution. Nature 414:43–48.
Zorman, S., Botte, M., Jiang, Q., Collinson, I., Schaffitzel, C. (2015) Advances and challenges of membrane-protein
complex production. Curr. Opin. Struct. Biol. 32:123–130.
References
57