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.
van Dam, L., Karlsson, G., Edwards, K. (2006) Morphology of magnetically aligning DMPC/DHPC aggregates –
perforated sheets, not disks. Langmuir 22:3280–3285.
Vargas, C., Cuevas Arenas, R., Frotscher, E., Keller, S. (2015) Nanoparticle self-assembly in mixtures of phospholipids
with styrene/maleic acid copolymers or fluorinated surfactants. Nanoscale 7:20685–20696.
Varkey, J., Mizuno, N., Hegde, B.G., Cheng, N., Steven, A.C., Langen, R. (2013) α-Synuclein oligomers with broken
helical conformation form lipoprotein nanoparticles. J. Biol. Chem. 288:17620–17630.
Vauthey, S., Santoso, S., Gong, H., Watson, N., Zhang, S. (2002) Molecular self-assembly of surfactant-like peptides to
form nanotubes and nanovesicles. Proc. Natl. Acad. Sci. USA 99:5355–5360.
Vénien-Bryan, C., Balavoine, F., Toussaint, B., Mioskowski, C., Hewat, E., Helme, B., Vignais, P. (1997) Structural
study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of 2D crystals on a nickelchelating lipid. J. Mol. Biol. 274:687–692.
Vestergaard, M., Kraft, J.F., Vosegaard, T., Thøgersen, L., Schiøtt, B. (2015) Bicelles and other membrane mimics:
Comparison of structure, properties, and dynamics from MD simulations. J. Phys. Chem. B 119:15831–15843.
Viegas, A., Viennet, T., Etzkorn, M. (2016) The power, pitfalls and potential of the nanodisc system for NMR-based
studies. Biol. Chem. 397:1335–1354.
Vinothkumar, K.R. (2011) Structure of rhomboid protease in a lipid environment. J. Mol. Biol. 407:232–247.
Vold, R.R., Prosser, R.S. (1996) Magnetically oriented phospholipid bilayered micelles for structural studies of
polypeptides. Does the ideal bicelle exist? J. Magn. Reson. B113:267–271.
von Maltzahn, G., Vauthey, S., Santoso, S., Zhang, S. (2003) Positively charged surfactant-like peptides self-assemble
into nanostructures. Langmuir 19:4332–4337.
Wadsäter, M., Laursen, T., Singha, A., Hatzakis, N.S., Stamou, D., Barker, R., Mortensen, K., Feidenhans’l, R., Møller,
B.L., Cárdenas, M. (2012) Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome
P450 reductase (POR) in nanodiscs. J. Biol. Chem. 287:34596–34603.
Wald, J.H., Goormaghtigh, E., De Meutter, J., Ruysschaert, J.M., Jonas, A. (1990a) Investigation of the lipid domains
and apolipoprotein orientation in reconstituted high-density lipoproteins by fluorescence and IR methods. J. Biol.
Chem.:20044–20050.
Wald, J.H., Krul, E.S., Jonas, A. (1990b) Structure of apolipoprotein A-I in three homogeneous, reconstituted highdensity lipoprotein particles. J. Biol. Chem. 265:20037–20043.
Wang, G. (2008) NMR of membrane-associated peptides and proteins. Curr. Protein Pept. Sci. 9:50–69.
Wang, X., Mu, Z., Li, Y., Bi, Y., Wang, Y. (2015) Smaller nanodiscs are suitable for studying protein lipid interactions
by solution NMR. Protein J. 34:205–211.
Wang, X.Q., Corin, K., Baaske, P., Wienken, C.J., Jerabek-Willemsen, M., Duhr, S., Braun, D., Zhang, S.G. (2011)
Peptide surfactants for cell-free production of functional G protein-coupled receptors. Proc. Natl. Acad. Sci. USA
108:9049–9054.
Warschawski, D.E., Arnold, A.A., Beaugrand, M., Gravel, A., Chartrand, E., Marcotte, I. (2011) Choosing membrane
mimetics for NMR structural studies of transmembrane proteins. Biochim. Biophys. Acta 1808:1957–1974.
Wilcox, K.C., Marunde, M.R., Das, A., Velasco, P.T., Kuhns, B.D., Marty, M.T., Jiang, H., Luan, C.H., Sligar, S.G.,
Klein, W.L. (2015) Nanoscale synaptic membrane mimetic allows unbiased high-throughput screen that targets
binding sites for Alzheimer’s-associated Ab oligomers. PLoS One 10:e0125263.
Wlodawer, A., Segrest, J.P., Chung, B.H., Chiovetti, R., Jr., Weinstein, J.N. (1979) High-density lipoprotein
recombinants: evidence for a bicycle tire micelle structure obtained by neutron scattering and electron microscopy.
FEBS Lett. 104:231–235.
Xu, X.P., Zhai, D., Kim, E., Swift, M., Reed, J.C., Volkmann, N., Hanein, D. (2013) Three-dimensional structure of
Bax-mediated pores in membrane bilayers. Cell Death Dis. 4:e683.
Yang, J.P., Cirico, T., Katzen, F., Peterson, T.C., Kudlicki, W. (2011) Cell-free synthesis of a functional G proteincoupled receptor complexed with nanometer scale bilayer discs. BMC Biotechnol. 11:57.
Yang, S.J., Zhang, S.G. (2006) Self-assembling behavior of designer lipid-like peptides. Supramol. Chem. 18:389–396.
Ye, F., Hu, G., Taylor, D., Ratnikov, B., Bobkov, A.A., McLean, M.A., Sligar, S.G., Taylor, K.A., Ginsberg,
M.H. (2010) Recreation of the terminal events in physiological integrin activation. J. Cell Biol. 188:157–173.
Yeh, J.I., Du, S., Tortajada, A., Paulo, J., Zhang, S. (2005) Peptergents: peptide detergents that improve stability and
functionality of a membrane protein, glycerol-3-phosphate dehydrogenase. Biochemistry 44:16912–16919.
Yoon, J.Y., Kim, J., An, D.R., Lee, S.J., Kim, H.S., Im, H.N., Yoon, H.J., Kim, J.Y., Kim, S.J., Han, B.W., Suh,
S.W. (2013) Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter
pylori. Acta Crystallogr. D 69:735–746.
148
3 Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions
of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating. Proc. Natl. Acad. Sci. USA
105:17742–17747.
van Dam, L., Karlsson, G., Edwards, K. (2006) Morphology of magnetically aligning DMPC/DHPC aggregates –
perforated sheets, not disks. Langmuir 22:3280–3285.
Vargas, C., Cuevas Arenas, R., Frotscher, E., Keller, S. (2015) Nanoparticle self-assembly in mixtures of phospholipids
with styrene/maleic acid copolymers or fluorinated surfactants. Nanoscale 7:20685–20696.
Varkey, J., Mizuno, N., Hegde, B.G., Cheng, N., Steven, A.C., Langen, R. (2013) α-Synuclein oligomers with broken
helical conformation form lipoprotein nanoparticles. J. Biol. Chem. 288:17620–17630.
Vauthey, S., Santoso, S., Gong, H., Watson, N., Zhang, S. (2002) Molecular self-assembly of surfactant-like peptides to
form nanotubes and nanovesicles. Proc. Natl. Acad. Sci. USA 99:5355–5360.
Vénien-Bryan, C., Balavoine, F., Toussaint, B., Mioskowski, C., Hewat, E., Helme, B., Vignais, P. (1997) Structural
study of the response regulator HupR from Rhodobacter capsulatus. Electron microscopy of 2D crystals on a nickelchelating lipid. J. Mol. Biol. 274:687–692.
Vestergaard, M., Kraft, J.F., Vosegaard, T., Thøgersen, L., Schiøtt, B. (2015) Bicelles and other membrane mimics:
Comparison of structure, properties, and dynamics from MD simulations. J. Phys. Chem. B 119:15831–15843.
Viegas, A., Viennet, T., Etzkorn, M. (2016) The power, pitfalls and potential of the nanodisc system for NMR-based
studies. Biol. Chem. 397:1335–1354.
Vinothkumar, K.R. (2011) Structure of rhomboid protease in a lipid environment. J. Mol. Biol. 407:232–247.
Vold, R.R., Prosser, R.S. (1996) Magnetically oriented phospholipid bilayered micelles for structural studies of
polypeptides. Does the ideal bicelle exist? J. Magn. Reson. B113:267–271.
von Maltzahn, G., Vauthey, S., Santoso, S., Zhang, S. (2003) Positively charged surfactant-like peptides self-assemble
into nanostructures. Langmuir 19:4332–4337.
Wadsäter, M., Laursen, T., Singha, A., Hatzakis, N.S., Stamou, D., Barker, R., Mortensen, K., Feidenhans’l, R., Møller,
B.L., Cárdenas, M. (2012) Monitoring shifts in the conformation equilibrium of the membrane protein cytochrome
P450 reductase (POR) in nanodiscs. J. Biol. Chem. 287:34596–34603.
Wald, J.H., Goormaghtigh, E., De Meutter, J., Ruysschaert, J.M., Jonas, A. (1990a) Investigation of the lipid domains
and apolipoprotein orientation in reconstituted high-density lipoproteins by fluorescence and IR methods. J. Biol.
Chem.:20044–20050.
Wald, J.H., Krul, E.S., Jonas, A. (1990b) Structure of apolipoprotein A-I in three homogeneous, reconstituted highdensity lipoprotein particles. J. Biol. Chem. 265:20037–20043.
Wang, G. (2008) NMR of membrane-associated peptides and proteins. Curr. Protein Pept. Sci. 9:50–69.
Wang, X., Mu, Z., Li, Y., Bi, Y., Wang, Y. (2015) Smaller nanodiscs are suitable for studying protein lipid interactions
by solution NMR. Protein J. 34:205–211.
Wang, X.Q., Corin, K., Baaske, P., Wienken, C.J., Jerabek-Willemsen, M., Duhr, S., Braun, D., Zhang, S.G. (2011)
Peptide surfactants for cell-free production of functional G protein-coupled receptors. Proc. Natl. Acad. Sci. USA
108:9049–9054.
Warschawski, D.E., Arnold, A.A., Beaugrand, M., Gravel, A., Chartrand, E., Marcotte, I. (2011) Choosing membrane
mimetics for NMR structural studies of transmembrane proteins. Biochim. Biophys. Acta 1808:1957–1974.
Wilcox, K.C., Marunde, M.R., Das, A., Velasco, P.T., Kuhns, B.D., Marty, M.T., Jiang, H., Luan, C.H., Sligar, S.G.,
Klein, W.L. (2015) Nanoscale synaptic membrane mimetic allows unbiased high-throughput screen that targets
binding sites for Alzheimer’s-associated Ab oligomers. PLoS One 10:e0125263.
Wlodawer, A., Segrest, J.P., Chung, B.H., Chiovetti, R., Jr., Weinstein, J.N. (1979) High-density lipoprotein
recombinants: evidence for a bicycle tire micelle structure obtained by neutron scattering and electron microscopy.
FEBS Lett. 104:231–235.
Xu, X.P., Zhai, D., Kim, E., Swift, M., Reed, J.C., Volkmann, N., Hanein, D. (2013) Three-dimensional structure of
Bax-mediated pores in membrane bilayers. Cell Death Dis. 4:e683.
Yang, J.P., Cirico, T., Katzen, F., Peterson, T.C., Kudlicki, W. (2011) Cell-free synthesis of a functional G proteincoupled receptor complexed with nanometer scale bilayer discs. BMC Biotechnol. 11:57.
Yang, S.J., Zhang, S.G. (2006) Self-assembling behavior of designer lipid-like peptides. Supramol. Chem. 18:389–396.
Ye, F., Hu, G., Taylor, D., Ratnikov, B., Bobkov, A.A., McLean, M.A., Sligar, S.G., Taylor, K.A., Ginsberg,
M.H. (2010) Recreation of the terminal events in physiological integrin activation. J. Cell Biol. 188:157–173.
Yeh, J.I., Du, S., Tortajada, A., Paulo, J., Zhang, S. (2005) Peptergents: peptide detergents that improve stability and
functionality of a membrane protein, glycerol-3-phosphate dehydrogenase. Biochemistry 44:16912–16919.
Yoon, J.Y., Kim, J., An, D.R., Lee, S.J., Kim, H.S., Im, H.N., Yoon, H.J., Kim, J.Y., Kim, S.J., Han, B.W., Suh,
S.W. (2013) Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter
pylori. Acta Crystallogr. D 69:735–746.
148
3 Alternatives to Detergents for Handling Membrane Proteins in Aqueous Solutions