Sharma, K.S., Durand, G., Gabel, F., Bazzacco, P., Le Bon, C., Billon-Denis, E., Catoire, L.J., Popot, J.-L., Ebel, C.,
Pucci, B. (2012) Non-ionic amphiphilic homopolymers: Synthesis, solution properties, and biochemical validation.
Langmuir 28:4625–4639.
Sharma, K.S., Durand, G., Giusti, F., Olivier, B., Fabiano, A.-S., Bazzacco, P., Dahmane, T., Ebel, C., Popot, J.-L.,
Pucci, B. (2008) Glucose-based amphiphilic telomers designed to keep membrane proteins soluble in aqueous
solutions: synthesis and physico-chemical characterization. Langmuir 24:13581–13590.
Shenkarev, Z.O., Lyukmanova, E.N., Paramonov, A.S., Shingarova, L.N., Chupin, V.V., Kirpichnikov, M.P.,
Blommers, M.J., Arseniev, A.S. (2010) Lipid-protein nanodiscs as reference medium in detergent screening for
high-resolution NMR studies of integral membrane proteins. J. Am. Chem. Soc. 132:5628–5629.
Sim, D.-W., Lu, Z., Won, H.-S., Lee, S.-N., Seo, M.D., Lee, B.-J., Kim, J.-H. (2017) Application of solution NMR to
structural studies on α-helical integral membrane proteins. Molecules 22:1347.
Sólyom, Z., Ma, P., Schwarten, M., Bosco, M.I., Polidori, A., Durand, G., Willbold, D., Brutscher, B. (2015) The
disordered region of the HCV protein NS5A: conformational dynamics, SH3 binding, and phosphorylation. Biophys.
J. 109:1483–1496.
Sprangers, R., Velyvis, A., Kay, L.E. (2007) Solution NMR of supramolecular complexes: providing new insights into
function. Nat. Meth. 4:697–703.
Sugiura, M., Beierbeck, H., Bélanger, P.C., Kotovych, G. (1984) Conformational analysis of leukotriene B 4 in solution
based on high-field nuclear magnetic resonance measurements. J. Am. Chem. Soc. 106:4021–4025.
Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton,
J.W. (2014) Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: A biochemical and
structural case study. J. Membr. Biol. 247:1005–1018.
Tapaneeyakorn, S., Goddard, A.D., Oates, J., Willis, C.L., Watts, A. (2011) Solution- and solid-state NMR studies of
GPCRs and their ligands. Biochim. Biophys. Acta 1808:1462–1475.
Tehei, M., Perlmutter, J.D., Giusti, F., Sachs, J.N., Zaccai, G., Popot, J.-L. (2014) Thermal fluctuations in amphipol
A8-35 particles: A neutron scattering and molecular dynamics study. J. Membr. Biol. 247:897–908.
Tifrea, D.F., Pal, S., Cocco, M.J., Popot, J.-L., de la Maza, L.M. (2014) Increased immunoaccessibility of MOMP
epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal
challenge with C. muridarum. J. Immunol. 192:5201–5213.
Tifrea, D.F., Sun, G., Pal, S., Zardeneta, G., Cocco, M.J., Popot, J.-L., de la Maza, L.M. (2011) Amphipols stabilize the
Chlamydia major outer membrane protein and enhance its protective ability as a vaccine. Vaccine 29:4623–4631.
Torchia, D.A. (2015) NMR studies of dynamic biomolecular conformational ensembles. Prog. Nucl. Magn. Reson.
Spectrosc. 84-85:14–32.
Triba, M.N., Warschawski, D.E., Devaux, P.F. (2005) Reinvestigation by phosphorus NMR of lipid distribution in
bicelles. Biophys. J. 88:1887–1901.
Tribet, C., Audebert, R., Popot, J.-L. (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous
solutions. Proc. Natl. Acad. Sci. USA 93:15047–15050.
Tugarinov, V., Kanelis, V., Kay, L.E. (2006) Isotope labeling strategies for the study of high-molecular-weight proteins
by solution NMR spectroscopy. Nat. Protoc. 1:749–754.
Van Horn, W.D., Kim, H.J., Ellis, C.D., Hadziselimovic, A., Sulistijo, E.S., Karra, M.D., Tian, C., Sönnichsen, F.D.,
Sanders, C.R. (2009) Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase.
Science 324:1726–1729.
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.
Vogt, J., Schulz, G.E. (1999) The structure of the outer membrane protein OmpX from Escherichia coli reveals possible
mechanisms of virulence. Structure 7:1301–1309.
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.
Wang, G. (2008) NMR of membrane-associated peptides and proteins. Curr. Protein Pept. Sci. 9:50–69.
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.
Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids. Wiley, New York, NY, USA, 320 p.
Yu, C., Levy, G.C. (1983) Solvent and intramolecular proton dipolar relaxation of the three phosphates of ATP: a
heteronuclear 2D study. J. Am. Chem. Soc. 105:6994–6996.
Yu, L., Sun, C., Song, D., Shen, J., Xu, N., Gunasekera, A., Hajduk, P.J., Olejniczak, E.T. (2005) Nuclear magnetic
resonance structural studies of a potassium channel-charybdotoxin complex. Biochemistry 44:15834–15841.
Zhou, H.X., Cross, T.A. (2013) Influences of membrane mimetic environments on membrane protein structures. Annu.
Rev. Biophys. 42:361–392.
References
495
Pucci, B. (2012) Non-ionic amphiphilic homopolymers: Synthesis, solution properties, and biochemical validation.
Langmuir 28:4625–4639.
Sharma, K.S., Durand, G., Giusti, F., Olivier, B., Fabiano, A.-S., Bazzacco, P., Dahmane, T., Ebel, C., Popot, J.-L.,
Pucci, B. (2008) Glucose-based amphiphilic telomers designed to keep membrane proteins soluble in aqueous
solutions: synthesis and physico-chemical characterization. Langmuir 24:13581–13590.
Shenkarev, Z.O., Lyukmanova, E.N., Paramonov, A.S., Shingarova, L.N., Chupin, V.V., Kirpichnikov, M.P.,
Blommers, M.J., Arseniev, A.S. (2010) Lipid-protein nanodiscs as reference medium in detergent screening for
high-resolution NMR studies of integral membrane proteins. J. Am. Chem. Soc. 132:5628–5629.
Sim, D.-W., Lu, Z., Won, H.-S., Lee, S.-N., Seo, M.D., Lee, B.-J., Kim, J.-H. (2017) Application of solution NMR to
structural studies on α-helical integral membrane proteins. Molecules 22:1347.
Sólyom, Z., Ma, P., Schwarten, M., Bosco, M.I., Polidori, A., Durand, G., Willbold, D., Brutscher, B. (2015) The
disordered region of the HCV protein NS5A: conformational dynamics, SH3 binding, and phosphorylation. Biophys.
J. 109:1483–1496.
Sprangers, R., Velyvis, A., Kay, L.E. (2007) Solution NMR of supramolecular complexes: providing new insights into
function. Nat. Meth. 4:697–703.
Sugiura, M., Beierbeck, H., Bélanger, P.C., Kotovych, G. (1984) Conformational analysis of leukotriene B 4 in solution
based on high-field nuclear magnetic resonance measurements. J. Am. Chem. Soc. 106:4021–4025.
Sverzhinsky, A., Qian, S., Yang, L., Allaire, M., Moraes, I., Ma, D., Chung, J.W., Zoonens, M., Popot, J.-L., Coulton,
J.W. (2014) Amphipol-trapped ExbB-ExbD membrane protein complex from Escherichia coli: A biochemical and
structural case study. J. Membr. Biol. 247:1005–1018.
Tapaneeyakorn, S., Goddard, A.D., Oates, J., Willis, C.L., Watts, A. (2011) Solution- and solid-state NMR studies of
GPCRs and their ligands. Biochim. Biophys. Acta 1808:1462–1475.
Tehei, M., Perlmutter, J.D., Giusti, F., Sachs, J.N., Zaccai, G., Popot, J.-L. (2014) Thermal fluctuations in amphipol
A8-35 particles: A neutron scattering and molecular dynamics study. J. Membr. Biol. 247:897–908.
Tifrea, D.F., Pal, S., Cocco, M.J., Popot, J.-L., de la Maza, L.M. (2014) Increased immunoaccessibility of MOMP
epitopes in a vaccine formulated with amphipols may account for the very robust protection elicited against a vaginal
challenge with C. muridarum. J. Immunol. 192:5201–5213.
Tifrea, D.F., Sun, G., Pal, S., Zardeneta, G., Cocco, M.J., Popot, J.-L., de la Maza, L.M. (2011) Amphipols stabilize the
Chlamydia major outer membrane protein and enhance its protective ability as a vaccine. Vaccine 29:4623–4631.
Torchia, D.A. (2015) NMR studies of dynamic biomolecular conformational ensembles. Prog. Nucl. Magn. Reson.
Spectrosc. 84-85:14–32.
Triba, M.N., Warschawski, D.E., Devaux, P.F. (2005) Reinvestigation by phosphorus NMR of lipid distribution in
bicelles. Biophys. J. 88:1887–1901.
Tribet, C., Audebert, R., Popot, J.-L. (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous
solutions. Proc. Natl. Acad. Sci. USA 93:15047–15050.
Tugarinov, V., Kanelis, V., Kay, L.E. (2006) Isotope labeling strategies for the study of high-molecular-weight proteins
by solution NMR spectroscopy. Nat. Protoc. 1:749–754.
Van Horn, W.D., Kim, H.J., Ellis, C.D., Hadziselimovic, A., Sulistijo, E.S., Karra, M.D., Tian, C., Sönnichsen, F.D.,
Sanders, C.R. (2009) Solution nuclear magnetic resonance structure of membrane-integral diacylglycerol kinase.
Science 324:1726–1729.
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.
Vogt, J., Schulz, G.E. (1999) The structure of the outer membrane protein OmpX from Escherichia coli reveals possible
mechanisms of virulence. Structure 7:1301–1309.
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.
Wang, G. (2008) NMR of membrane-associated peptides and proteins. Curr. Protein Pept. Sci. 9:50–69.
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.
Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids. Wiley, New York, NY, USA, 320 p.
Yu, C., Levy, G.C. (1983) Solvent and intramolecular proton dipolar relaxation of the three phosphates of ATP: a
heteronuclear 2D study. J. Am. Chem. Soc. 105:6994–6996.
Yu, L., Sun, C., Song, D., Shen, J., Xu, N., Gunasekera, A., Hajduk, P.J., Olejniczak, E.T. (2005) Nuclear magnetic
resonance structural studies of a potassium channel-charybdotoxin complex. Biochemistry 44:15834–15841.
Zhou, H.X., Cross, T.A. (2013) Influences of membrane mimetic environments on membrane protein structures. Annu.
Rev. Biophys. 42:361–392.
References
495