메뉴 건너뛰기




Volumn 69, Issue , 2013, Pages 1-22

When detergent meets bilayer: Birth and coming of age of lipid bicelles

Author keywords

Lipid bicelles; Lipid bilayer; Membrane mimetic; Membrane protein; Nuclear magnetic resonance

Indexed keywords

CHEMICAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SPECTROSCOPY;

EID: 84874643050     PISSN: 00796565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pnmrs.2013.01.001     Document Type: Review
Times cited : (115)

References (321)
  • 1
    • 33645524559 scopus 로고    scopus 로고
    • Morphology of magnetically aligning DMPC/DHPC aggregates-perforated sheets, not disks
    • L. van Dam, G. Karlsson, and K. Edwards Morphology of magnetically aligning DMPC/DHPC aggregates-perforated sheets, not disks Langmuir 22 2006 3280 3285
    • (2006) Langmuir , vol.22 , pp. 3280-3285
    • Van Dam, L.1    Karlsson, G.2    Edwards, K.3
  • 2
    • 0027378951 scopus 로고
    • Liposome stability and formation: Experimental parameters and theories on the size distribution
    • M. Winterhalter, and D.D. Lasic Liposome stability and formation: experimental parameters and theories on the size distribution Chem. Phys. Lipids 64 1993 35 43 (Pubitemid 23290864)
    • (1993) Chemistry and Physics of Lipids , vol.64 , Issue.1-3 , pp. 35-43
    • Winterhalter, M.1    Lasic, D.D.2
  • 3
    • 35748949269 scopus 로고    scopus 로고
    • NMR of molecules interacting with lipids in small unilamellar vesicles
    • DOI 10.1007/s00249-007-0186-7
    • G. Da Costa, L. Mouret, S. Chevance, E. Le Rumeur, and A. Bondon NMR of molecules interacting with lipids in small unilamellar vesicles Eur. Biophys. J. 36 2007 933 942 (Pubitemid 350045036)
    • (2007) European Biophysics Journal , vol.36 , Issue.8 , pp. 933-942
    • Da Costa, G.1    Mouret, L.2    Chevance, S.3    Le Rumeur, E.4    Bondon, A.5
  • 4
    • 84934435581 scopus 로고    scopus 로고
    • Artificial membrane models for the study of macromolecular delivery
    • L. Mäler, and A. Gräslund Artificial membrane models for the study of macromolecular delivery Meth. Mol. Biol. 480 2009 129 139
    • (2009) Meth. Mol. Biol. , vol.480 , pp. 129-139
    • Mäler, L.1    Gräslund, A.2
  • 5
    • 33750405141 scopus 로고
    • Sideband intensities in NMR spectra of samples spinning at the magic angle
    • J. Herzfeld, and A.E. Berger Sideband intensities in NMR spectra of samples spinning at the magic angle J. Chem. Phys. 73 1980 6021 6030
    • (1980) J. Chem. Phys. , vol.73 , pp. 6021-6030
    • Herzfeld, J.1    Berger, A.E.2
  • 8
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • S.J. Opella, and F.M. Marassi Structure determination of membrane proteins by NMR spectroscopy Chem. Rev. 104 2004 3587 3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 9
    • 0025101067 scopus 로고
    • Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D
    • F. Moll III, and T.A. Cross Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin D Biophys. J. 57 1990 351 362 (Pubitemid 20058268)
    • (1990) Biophysical Journal , vol.57 , Issue.2 , pp. 351-362
    • Moll III, F.1    Cross, T.A.2
  • 10
    • 0000689027 scopus 로고
    • Saturated solutions for the control of humidity in biological research
    • P.W. Winston, and D.H. Bates Saturated solutions for the control of humidity in biological research Ecology 41 1960 232 237
    • (1960) Ecology , vol.41 , pp. 232-237
    • Winston, P.W.1    Bates, D.H.2
  • 11
    • 0027438626 scopus 로고
    • Fd Coat protein structure in membrane environments
    • DOI 10.1006/jmbi.1993.1523
    • P.A. McDonnel, K. Shon, Y. Kim, and S.J. Opella Fd coat protein structure in membrane environments J. Mol. Biol. 233 1993 447 463 (Pubitemid 23299173)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.3 , pp. 447-463
    • McDonnell, P.A.1    Shon, K.2    Kim, Y.3    Opella, S.J.4
  • 12
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid- state NMR
    • R.R. Ketchem, W. Hu, and T.A. Cross High-resolution conformation of gramicidin A in lipid bilayer by solid-state NMR Science 261 1993 1457 1460 (Pubitemid 23334269)
    • (1993) Science , vol.261 , Issue.5127 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 14
    • 0026447195 scopus 로고
    • Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR
    • A.S. Ulrich, M.P. Heyn, and A. Watts Structure determination of the cyclohexene ring of retinal in bacteriorhodopsin by solid-state deuterium NMR Biochemistry 31 1992 10390 10399
    • (1992) Biochemistry , vol.31 , pp. 10390-10399
    • Ulrich, A.S.1    Heyn, M.P.2    Watts, A.3
  • 15
    • 1542375007 scopus 로고    scopus 로고
    • Solid-State NMR Spectroscopy of Aligned Lipid Bilayers at Low Temperatures
    • DOI 10.1021/ja039077o
    • D.-K. Lee, K.A. Henzler Wildman, and A. Ramamoorthy Solid state NMR spectroscopy of aligned lipid bilayers at low temperatures J. Am. Chem. Soc. 126 2004 2318 2319 (Pubitemid 38295707)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.8 , pp. 2318-2319
    • Lee, D.-K.1    Wildman, K.H.2    Ramamoorthy, A.3
  • 16
    • 0036228299 scopus 로고    scopus 로고
    • An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies
    • K.J. Hallock, K.A. Henzler Wildman, D.-K. Lee, and A. Ramamoorthy An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies Biophys. J. 82 2002 2499 2503 (Pubitemid 34441288)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2499-2503
    • Hallock, K.J.1    Wildman, K.H.2    Lee, D.-K.3    Ramamoorthy, A.4
  • 17
    • 0035997051 scopus 로고    scopus 로고
    • Membrane composition determines Pardaxin's mechanism of lipid bilayer disruption
    • K.J. Hallock, D.-K. Lee, J. Omnaas, H.I. Mosberg, and A. Ramamoorthy Membrane composition determines pardaxin's mechanism of lipid bilayer disruption Biophys. J. 83 2002 1004 1013 (Pubitemid 34803633)
    • (2002) Biophysical Journal , vol.83 , Issue.2 , pp. 1004-1013
    • Hallock, K.J.1    Lee, D.-K.2    Omnaas, J.3    Mosberg, H.I.4    Ramamoorthy, A.5
  • 18
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • K.J. Hallock, D.-K. Lee, and A. Ramamoorthy MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain Biophys. J. 84 2003 3052 3060 (Pubitemid 36531755)
    • (2003) Biophysical Journal , vol.84 , Issue.5 , pp. 3052-3060
    • Hallock, K.J.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 19
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • DOI 10.1021/bi0273563
    • K.A. Henzler Wildman, D.-K. Lee, and A. Ramamoorthy Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37 Biochemistry 42 2003 6545 6558 (Pubitemid 36665830)
    • (2003) Biochemistry , vol.42 , Issue.21 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 20
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • DOI 10.1021/bi036284s
    • K.A. Henzler Wildman, G.V. Martinez, M.F. Brown, and A. Ramamoorthy Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37 Biochemistry 43 2004 8459 8469 (Pubitemid 38902524)
    • (2004) Biochemistry , vol.43 , Issue.26 , pp. 8459-8469
    • Henzler-Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4
  • 21
    • 33846562986 scopus 로고    scopus 로고
    • Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies
    • DOI 10.1021/bi061895g
    • A. Ramamoorthy, S.K. Kandasamy, D.-K. Lee, S. Kidambi, and R.G. Larson Topology and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies Biochemistry 46 2007 965 975 (Pubitemid 46184985)
    • (2007) Biochemistry , vol.46 , Issue.4 , pp. 965-975
    • Ramamoorthy, A.1    Kandasamy, S.K.2    Lee, D.-K.3    Kidambi, S.4    Larson, R.G.5
  • 22
    • 7644228920 scopus 로고    scopus 로고
    • Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy
    • DOI 10.1016/j.chemphyslip.2004.09.004, PII S0009308404001379
    • C.D. Pointer-Keenan, D.-K. Lee, K.J. Hallock, A. Tan, R. Zand, and A. Ramamoorthy Investigation of the interaction of myelin basic protein with phospholipid bilayers using solid-state NMR spectroscopy Chem. Phys. Lipids 132 2004 47 54 (Pubitemid 39458319)
    • (2004) Chemistry and Physics of Lipids , vol.132 , Issue.1 , pp. 47-54
    • Pointer-Keenan, C.D.1    Lee, D.-K.2    Hallok, K.3    Tan, A.4    Zand, R.5    Ramamoorthy, A.6
  • 23
    • 33750097576 scopus 로고
    • The formation of controlled-porosity membranes from anodically oxidized aluminum
    • R.C. Furneaux, W.R. Rigby, and A.P. Davidson The formation of controlled-porosity membranes from anodically oxidized aluminum Nature 337 1989 147 149
    • (1989) Nature , vol.337 , pp. 147-149
    • Furneaux, R.C.1    Rigby, W.R.2    Davidson, A.P.3
  • 24
    • 14844354285 scopus 로고    scopus 로고
    • 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores
    • DOI 10.1016/j.jmr.2004.12.006, PII S1090780704004136
    • 31P solid-state NMR study of transmembrane domain alignment of M2 protein of influenza A virus in hydrated cylindrical lipid bilayers confined to anodic aluminum oxide nanopores J. Magn. Reson. 173 2005 322 327 (Pubitemid 40352456)
    • (2005) Journal of Magnetic Resonance , vol.173 , Issue.2 , pp. 322-327
    • Chekmenev, E.Y.1    Hu, J.2    Gor'Kov, P.L.3    Brey, W.W.4    Cross, T.A.5    Ruuge, A.6    Smirnov, A.I.7
  • 26
    • 4444342324 scopus 로고    scopus 로고
    • Multinuclear NMR studies of single lipid bilayers supported in cylindrical aluminum oxide nanopores
    • H.C. Gaede, K.M. Luckett, I.V. Polozov, and K. Gawrisch Multinuclear NMR studies of single lipid bilayers supported in cylindrical aluminum oxide nanopores Langmuir 20 2004 7711 7719
    • (2004) Langmuir , vol.20 , pp. 7711-7719
    • Gaede, H.C.1    Luckett, K.M.2    Polozov, I.V.3    Gawrisch, K.4
  • 27
    • 34250217114 scopus 로고    scopus 로고
    • Characterization of lipid bilayer formation in aligned nanoporous aluminum oxide nanotube arrays
    • DOI 10.1016/j.jmr.2007.04.004, PII S1090780707001139
    • E.S. Karp, J.P. Newstadt, S. Chu, and G.A. Lorigan Characterization of lipid bilayer formation in aligned nanoporous aluminium oxide nanotube arrays J. Magn. Reson. 187 2007 112 119 (Pubitemid 46898872)
    • (2007) Journal of Magnetic Resonance , vol.187 , Issue.1 , pp. 112-119
    • Karp, E.S.1    Newstadt, J.P.2    Chu, S.3    Lorigan, G.A.4
  • 29
    • 33845929561 scopus 로고    scopus 로고
    • Functional reconstitution of rhodopsin into tubular lipid bilayers supported by nanoporous media
    • DOI 10.1021/bi061416d
    • O. Soubias, I.V. Polozov, W.E. Teague, A.A. Yeliseev, and K. Gawrisch Functional reconstitution of rhodopsin into tubular lipid bilayers supported by nanoporous material Biochemistry 45 2006 15583 15590 (Pubitemid 46032479)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15583-15590
    • Soubias, O.1    Polozov, I.V.2    Teague, W.E.3    Yeliseev, A.A.4    Gawrisch, K.5
  • 30
    • 34548494605 scopus 로고    scopus 로고
    • Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    • DOI 10.1016/j.bbamem.2007.07.001, PII S0005273607002477
    • J.R. Brender, U.H.N. Dürr, D. Heyl, M.B. Budarapu, and A. Ramamoorthy Membrane fragmentation by an amyloidogenic fragment of human islet amyloid polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes Biochim. Biophys. Acta 1768 2007 2026 2029 (Pubitemid 47379628)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.9 , pp. 2026-2029
    • Brender, J.R.1    Durr, U.H.N.2    Heyl, D.3    Budarapu, M.B.4    Ramamoorthy, A.5
  • 31
    • 0021765682 scopus 로고
    • Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy
    • C.G. Brouillette, J.L. Jones, T.C. Ng, H. Kercret, B.H. Chung, and J.P. Segrest Structural studies of apolipoprotein A-I/phosphatidylcholine recombinants by high-field proton NMR, nondenaturing gradient gel electrophoresis, and electron microscopy Biochemistry 23 1984 359 367
    • (1984) Biochemistry , vol.23 , pp. 359-367
    • Brouillette, C.G.1    Jones, J.L.2    Ng, T.C.3    Kercret, H.4    Chung, B.H.5    Segrest, J.P.6
  • 32
    • 0142179052 scopus 로고    scopus 로고
    • Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers
    • DOI 10.1110/ps.03267503
    • T.H. Bayburt, and S.G. Sligar Self-assembly of single integral membrane proteins into soluble nanoscale phospholipid bilayers Protein Sci. 12 2003 2476 2481 (Pubitemid 37310788)
    • (2003) Protein Science , vol.12 , Issue.11 , pp. 2476-2481
    • Bayburt, T.H.1    Sligar, S.G.2
  • 36
    • 0028947465 scopus 로고
    • Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies
    • C.R. Sanders, and G.C. Landis Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies Biochemistry 34 1995 4030 4040
    • (1995) Biochemistry , vol.34 , pp. 4030-4040
    • Sanders, C.R.1    Landis, G.C.2
  • 37
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • DOI 10.1016/S1047-8477(03)00043-1
    • M. Caffrey Membrane protein crystallization J. Struct. Biol. 142 2003 108 132 (Pubitemid 36457895)
    • (2003) Journal of Structural Biology , vol.142 , Issue.1 , pp. 108-132
    • Caffrey, M.1
  • 39
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • DOI 10.1006/jmbi.2001.5295
    • S. Faham, and J.U. Bowie Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure J. Mol. Biol. 316 2002 1 6 (Pubitemid 34729261)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.1 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 40
    • 14144250152 scopus 로고    scopus 로고
    • Crystallization of bacteriorhodopsin from bicelle formulations at room temperature
    • DOI 10.1110/ps.041167605
    • S. Faham, G.L. Boulting, E.A. Massey, S. Yohannan, D. Yang, and J.U. Bowie Crystallization of bacteriorhodopsin from bicelle formulations at room temperature Prot. Sci. 14 2005 836 840 (Pubitemid 40283923)
    • (2005) Protein Science , vol.14 , Issue.3 , pp. 836-840
    • Faham, S.1    Boulting, G.L.2    Massey, E.A.3    Yohannan, S.4    Yang, D.5    Bowie, J.U.6
  • 41
    • 29844433028 scopus 로고    scopus 로고
    • Partial dehydration of the retinal binding pocket and proof for photochemical deprotonation of the retinal Schiff base in bicelle bacteriorhodopsin crystals
    • DOI 10.1562/2005-03-09-RA-458
    • L.S. Sanii, and M.A. El-Sayed Partial dehydration of the retinal binding pocket and proof for photochemical deprotonation of the retinal Schiff base in bicelle bacteriorhodopsin Photochem. Photobiol. 81 2005 1356 1360 (Pubitemid 43035844)
    • (2005) Photochemistry and Photobiology , vol.81 , Issue.6 , pp. 1356-1360
    • Sanii, L.S.1    El-Sayed, M.A.2
  • 42
    • 84855835025 scopus 로고    scopus 로고
    • A transporter converted into a sensor, a phototaxis signaling mutant of bacteriorhodopsin at 3.0 Å
    • E.N. Spudich, G. Ozorowski, E.V. Schow, D.J. Tobias, J.L. Spudich, and H. Luecke A transporter converted into a sensor, a phototaxis signaling mutant of bacteriorhodopsin at 3.0 Å J. Mol. Biol. 415 2011 455 463
    • (2011) J. Mol. Biol. , vol.415 , pp. 455-463
    • Spudich, E.N.1    Ozorowski, G.2    Schow, E.V.3    Tobias, D.J.4    Spudich, J.L.5    Luecke, H.6
  • 43
    • 84862790971 scopus 로고    scopus 로고
    • Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context
    • H. Wang, J. Elferich, and E. Gouaux Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context Nat. Struct. Mol. Biol. 19 2012 212 219
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 212-219
    • Wang, H.1    Elferich, J.2    Gouaux, E.3
  • 44
    • 84855991060 scopus 로고    scopus 로고
    • Crystallizing membrane proteins using lipidic bicelles
    • R. Ujwal, and J.U. Bowie Crystallizing membrane proteins using lipidic bicelles Methods 55 2011 337 341
    • (2011) Methods , vol.55 , pp. 337-341
    • Ujwal, R.1    Bowie, J.U.2
  • 45
    • 84856983217 scopus 로고    scopus 로고
    • High-throughput crystallization of membrane proteins using the lipidic bicelle method
    • R. Ujwal, and J. Abramson High-throughput crystallization of membrane proteins using the lipidic bicelle method J. Vis. Exp. 59 2012 e3383
    • (2012) J. Vis. Exp. , vol.59 , pp. 3383
    • Ujwal, R.1    Abramson, J.2
  • 46
    • 0030997803 scopus 로고    scopus 로고
    • Effect of polyethyleneglycol-phospholipids on aggregate structure in preparations of small unilamellar liposomes
    • K. Edwards, M. Johnsson, G. Karlsson, and M. Silvander Effect of polyethyleneglycol-phospholipids on aggregate structure in preparations of small unilamellar liposomes Biophys. J. 73 1997 258 266 (Pubitemid 27274123)
    • (1997) Biophysical Journal , vol.73 , Issue.1 , pp. 258-266
    • Edwards, K.1    Johnsson, M.2    Karlsson, G.3    Silvander, M.4
  • 47
    • 0035137152 scopus 로고    scopus 로고
    • Phase behavior and aggregate structure in mixtures of dioleoylphosphatidylethanolamine and poly(ethylene glycol)-lipids
    • M. Johnsson, and K. Edwards Phase behavior and aggregate structure in mixtures of dioleoylphosphatidylethanolamine and poly(ethylene glycol)-lipids Biophys. J. 80 2001 313 323
    • (2001) Biophys. J. , vol.80 , pp. 313-323
    • Johnsson, M.1    Edwards, K.2
  • 49
    • 0344551055 scopus 로고    scopus 로고
    • Liposomes, Disks, and Spherical Micelles: Aggregate Structure in Mixtures of Gel Phase Phosphatidylcholines and Poly(Ethylene Glycol)-Phospholipids
    • M. Johnsson, and K. Edwards Liposomes, disks, and spherical micelles: aggregate structure in mixtures of gel phase phosphatidylcholines and poly(ethylene glycol)-phospholipids Biophys. J. 85 2003 3839 3847 (Pubitemid 37490293)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3839-3847
    • Johnsson, M.1    Edwards, K.2
  • 50
    • 34247360863 scopus 로고    scopus 로고
    • Structure of mixed micelles formed in PEG-lipid/lipid dispersions
    • DOI 10.1021/la063501s
    • M.C. Sandström, E. Johansson, and K. Edwards Structure of mixed micelles formed in PEG-lipid/lipid dispersions Langmuir 23 2007 4192 4198 (Pubitemid 46643140)
    • (2007) Langmuir , vol.23 , Issue.8 , pp. 4192-4198
    • Sandstrom, M.C.1    Johansson, E.2    Edwards, K.3
  • 53
    • 79959473055 scopus 로고    scopus 로고
    • Distribution of BODIPY-labelled phosphatidylethanolamines in lipid bilayers exhibiting different curvatures
    • R. Šachl, I. Mikhalyov, N. Gretskaya, A. Olzynska, M. Hof, and L.B.-Å. Johansson Distribution of BODIPY-labelled phosphatidylethanolamines in lipid bilayers exhibiting different curvatures Phys. Chem. Chem. Phys. 13 2011 11694 11701
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 11694-11701
    • Šachl, R.1    Mikhalyov, I.2    Gretskaya, N.3    Olzynska, A.4    Hof, M.5    Johansson, L.B.-Å.6
  • 54
    • 79959361250 scopus 로고    scopus 로고
    • Coarse-grained model for PEGylated lipids: Effect of PEGylation on the size and shape of self-assembled structures
    • H. Lee, and R.W. Pastor Coarse-grained model for PEGylated lipids: effect of PEGylation on the size and shape of self-assembled structures J. Phys. Chem. B 115 2011 7830 7837
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7830-7837
    • Lee, H.1    Pastor, R.W.2
  • 56
    • 52049094330 scopus 로고    scopus 로고
    • Melittin-lipid interaction: A comparative study using liposomes, micelles and bilayer disks
    • A. Lundquist, P. Wessman, A.R. Rennie, and K. Edwards Melittin-lipid interaction: a comparative study using liposomes, micelles and bilayer disks Biochim. Biopyhs. Acta 1778 2008 2210 2216
    • (2008) Biochim. Biopyhs. Acta , vol.1778 , pp. 2210-2216
    • Lundquist, A.1    Wessman, P.2    Rennie, A.R.3    Edwards, K.4
  • 57
    • 41849083430 scopus 로고    scopus 로고
    • On the formation of discoidal versus threadlike micelles in dilute aqueous surfactant/lipid systems
    • DOI 10.1021/la702637h
    • E. Johansson, M.C. Sandström, M. Bergström, and K. Edwards On the formation of discoidal versus threadlike micelles in dilute aqueous surfactant/lipid systems Langmuir 24 2008 1731 1739 (Pubitemid 351500925)
    • (2008) Langmuir , vol.24 , Issue.5 , pp. 1731-1739
    • Johansson, E.1    Sandstrom, M.C.2    Bergstrom, M.3    Edwards, K.4
  • 59
    • 77749234231 scopus 로고    scopus 로고
    • Uniting polypeptides with sequence-designed peptides: Synthesis and assembly of poly(γ-benzyl l-glutamate)-β-coiled-coil peptide copolymers
    • H.R. Marsden, J.-W. Handgraaf, F. Nudelman, N.A.J.M. Sommerdijk, and A. Kros Uniting polypeptides with sequence-designed peptides: synthesis and assembly of poly(γ-benzyl l-glutamate)-β-coiled-coil peptide copolymers J. Am. Chem. Soc. 132 2010 2370 2377
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 2370-2377
    • Marsden, H.R.1    Handgraaf, J.-W.2    Nudelman, F.3    Sommerdijk, N.A.J.M.4    Kros, A.5
  • 61
    • 25544469706 scopus 로고
    • New lyotropic liquid crystals composed of finite nonspherical micelles
    • B.J. Forrest, and L.W. Reeves New lyotropic liquid crystals composed of finite nonspherical micelles Chem. Rev. 81 1981 1 14
    • (1981) Chem. Rev. , vol.81 , pp. 1-14
    • Forrest, B.J.1    Reeves, L.W.2
  • 63
  • 64
    • 0021772460 scopus 로고
    • Spontaneous formation of stable unilamellar vesicles
    • N.E. Gabriel, and M.F. Roberts Spontaneous formation of stable unilamellar vesicles Biochemistry 23 1984 4011 4015
    • (1984) Biochemistry , vol.23 , pp. 4011-4015
    • Gabriel, N.E.1    Roberts, M.F.2
  • 65
    • 0022541995 scopus 로고
    • Interaction of short-chain lecithin with long-chain phospholipids: Characterization of vesicles that form spontaneously
    • N.E. Gabriel, and M.F. Roberts Interaction of short-chain lecithin with long-chain phospholipids: characterization of vesicles that form spontaneously Biochemistry 25 1986 2812 2821 (Pubitemid 16073815)
    • (1986) Biochemistry , vol.25 , Issue.10 , pp. 2812-2821
    • Gabriel, N.E.1    Roberts, M.F.2
  • 66
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time-dependent field gradient
    • E.O. Stejskal, and J. Tanner Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient J. Chem. Phys. 42 1965 288 292
    • (1965) J. Chem. Phys. , vol.42 , pp. 288-292
    • Stejskal, E.O.1    Tanner, J.2
  • 67
    • 1942423104 scopus 로고    scopus 로고
    • Spontaneously Formed Monodisperse Biomimetic Unilamellar Vesicles: The Effect of Charge, Dilution, and Time
    • M.-P. Nieh, T.A. Harroun, V.A. Raghunathan, C.J. Glinka, and J. Katsaras Spontaneously formed monodisperse biomimetic unilamellar vesicles: the effect of charge, dilution, and time Biophys. J. 86 2004 2615 2629 (Pubitemid 38524447)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2615-2629
    • Nieh, M.-P.1    Harroun, T.A.2    Raghunathan, V.A.3    Glinka, C.J.4    Katsaras, J.5
  • 68
    • 23144444013 scopus 로고    scopus 로고
    • Spontaneously formed unilamellar vesicles with path-dependent size distribution
    • DOI 10.1021/la0508994
    • M.-P. Nieh, V.A. Raghunathan, S.R. Kline, T.A. Harroun, C.-Y. Huang, J. Pencer, and J. Katsaras Spontaneously formed unilamellar vesicles with path-dependent size distribution Langmuir 21 2005 6656 6661 (Pubitemid 41084450)
    • (2005) Langmuir , vol.21 , Issue.15 , pp. 6656-6661
    • Nieh, M.-P.1    Raghunathan, V.A.2    Kline, S.R.3    Harroun, T.A.4    Huang, C.-Y.5    Pencer, J.6    Katsaras, J.7
  • 70
    • 0019429941 scopus 로고
    • Structural dimorphism of bile salt/lecithin mixed micelles. A possible regulatory mechanism for cholesterol solubility in bile? X-ray structure analysis
    • DOI 10.1021/bi00505a028
    • K. Müller Structural dimorphism of bile salt/lecithin mixed micelles. A possible regulatory mechanism for cholesterol solubility in bile? X-ray structure analysis Biochemistry 20 1981 404 414 (Pubitemid 11151574)
    • (1981) Biochemistry , vol.20 , Issue.2 , pp. 404-414
    • Muller, K.1
  • 71
    • 0024295725 scopus 로고
    • Magnetic field induced ordering of bile salt/phospholipid micelles: New media for NMR structural investigations
    • P. Ram, and J.H. Prestegard Magnetic field induced ordering of bile salt/phospholipid micelles: new media for NMR structural investigations Biochim. Biophys. Acta 940 1988 289 294
    • (1988) Biochim. Biophys. Acta , vol.940 , pp. 289-294
    • Ram, P.1    Prestegard, J.H.2
  • 72
    • 0025182649 scopus 로고
    • Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO
    • C.R. Sanders, and J.H. Prestegard Magnetically orientable phospholipid bilayers containing small amounts of a bile salt analogue, CHAPSO Biophys. J. 58 1990 447 460 (Pubitemid 20249672)
    • (1990) Biophysical Journal , vol.58 , Issue.2 , pp. 447-460
    • Sanders II, C.R.1    Prestegard, J.H.2
  • 73
    • 0028970550 scopus 로고
    • Small angle X-ray scattering studies of magnetically oriented lipid bilayers
    • B.J. Hare, J.H. Prestegard, and D.M. Engelman Small angle X-ray scattering studies of magnetically oriented lipid bilayers Biophys. J. 69 1995 1891 1896
    • (1995) Biophys. J. , vol.69 , pp. 1891-1896
    • Hare, B.J.1    Prestegard, J.H.2    Engelman, D.M.3
  • 74
    • 0027745264 scopus 로고
    • Structure and dynamics of the sialic acid moiety of G(M3)-ganglioside at the surface of a magnetically oriented membrane
    • DOI 10.1021/bi00212a005
    • M3-ganglioside at the surface of a magnetically oriented membrane Biochemistry 32 1993 13405 13413 (Pubitemid 24020214)
    • (1993) Biochemistry , vol.32 , Issue.49 , pp. 13405-13413
    • Aubin, Y.1    Ito, Y.2    Paulson, J.C.3    Prestegard, J.H.4
  • 75
    • 0028169249 scopus 로고
    • 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface
    • 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface Biochemistry 33 1994 10137 10148
    • (1994) Biochemistry , vol.33 , pp. 10137-10148
    • Hare, B.J.1    Rise, F.2    Aubin, Y.3    Prestegard, J.H.4
  • 76
    • 0029960499 scopus 로고    scopus 로고
    • Conformation of sulfoquinovosyldiacylglycerol bound to a magnetically oriented membrane system
    • K.P. Howard, and J.H. Prestegard Conformation of sulfoquinovosyldiacylglycerol bound to a magnetically oriented membrane system Biophys. J. 71 1996 2573 2582 (Pubitemid 26367720)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2573-2582
    • Howard, K.P.1    Prestegard, J.H.2
  • 77
    • 0026774489 scopus 로고
    • Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR
    • C.R. Sanders, and J.P. Schwonek Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR Biochemistry 31 1992 8898 8905
    • (1992) Biochemistry , vol.31 , pp. 8898-8905
    • Sanders, C.R.1    Schwonek, J.P.2
  • 79
    • 38449121914 scopus 로고    scopus 로고
    • Bicelle samples for solid-state NMR of membrane proteins
    • A.A. de Angelis, and S.J. Opella Bicelle samples for solid-state NMR of membrane proteins Nat. Prot. 2 2007 2332 2338
    • (2007) Nat. Prot. , vol.2 , pp. 2332-2338
    • De Angelis, A.A.1    Opella, S.J.2
  • 81
    • 60849097275 scopus 로고    scopus 로고
    • Water diffusion in bicelles and the mixed bicelle model
    • R. Soong, and P.M. Macdonald Water diffusion in bicelles and the mixed bicelle model Langmuir 25 2009 380 390
    • (2009) Langmuir , vol.25 , pp. 380-390
    • Soong, R.1    Macdonald, P.M.2
  • 83
    • 0041992602 scopus 로고    scopus 로고
    • Magnetically aligned phospholipid bilayers in weak magnetic fields: Optimization, mechanism, and advantages for X-band EPR studies
    • T.B. Cardon, E.K. Tiburu, and G.A. Lorigan Magnetically aligned phospholipid bilayers in weak magnetic fields: optimization, mechanism, and advantages for X-band EPR studies J. Magn. Reson. 161 2003 77 90
    • (2003) J. Magn. Reson. , vol.161 , pp. 77-90
    • Cardon, T.B.1    Tiburu, E.K.2    Lorigan, G.A.3
  • 84
    • 79959386431 scopus 로고    scopus 로고
    • Flow-alignment of bicellar lipid mixtures: Orientations of probe molecules and membrane-associated biomacromolecules in lipid membranes studied with polarized light
    • M. Kogan, T. Beke-Somfai, and B. Nordén Flow-alignment of bicellar lipid mixtures: orientations of probe molecules and membrane-associated biomacromolecules in lipid membranes studied with polarized light Chem. Commun. 47 2011 7356 7358
    • (2011) Chem. Commun. , vol.47 , pp. 7356-7358
    • Kogan, M.1    Beke-Somfai, T.2    Nordén, B.3
  • 85
    • 31944445990 scopus 로고    scopus 로고
    • 3+-doped bicelles as studied by solid-state NMR and FT-IR spectroscopy
    • DOI 10.1016/j.chemphyslip.2005.12.002, PII S0009308405001891
    • 3+-doped bicelles as studied by solid-state NMR and FT-IR spectroscopy Chem. Phys. Lip. 139 2006 137 149 (Pubitemid 43185992)
    • (2006) Chemistry and Physics of Lipids , vol.139 , Issue.2 , pp. 137-149
    • Marcotte, I.1    Belanger, A.2    Auger, M.3
  • 86
    • 79960758560 scopus 로고    scopus 로고
    • Unprecedented observation of days-long remnant orientation of phospholipid bicelles: A small-angle X-ray scattering and theoretical study
    • C. Loudet-Courreges, F. Nallet, E.J. Dufourc, and R. Oda Unprecedented observation of days-long remnant orientation of phospholipid bicelles: a small-angle X-ray scattering and theoretical study Langmuir 27 2011 9122 9130
    • (2011) Langmuir , vol.27 , pp. 9122-9130
    • Loudet-Courreges, C.1    Nallet, F.2    Dufourc, E.J.3    Oda, R.4
  • 88
    • 0031969085 scopus 로고    scopus 로고
    • Magnetically aligned phospholipid bilayers with positive ordering: A new model membrane system
    • R.S. Prosser, J.S. Hwang, and R.R. Vold Magnetically aligned phospholipids with positive ordering: a new model membrane system Biophys. J. 74 1998 2405 2418 (Pubitemid 28225237)
    • (1998) Biophysical Journal , vol.74 , Issue.5 , pp. 2405-2418
    • Prosser, R.S.1    Hwang, J.S.2    Vold, R.R.3
  • 89
    • 0031722552 scopus 로고    scopus 로고
    • Novel chelate-induced magnetic alignment of biological membranes
    • R.S. Prosser, V.B. Volkov, and I.V. Shiyanovskaya Novel chelate-induced magnetic alignment of biological membranes Biophys. J. 75 1998 2163 2189
    • (1998) Biophys. J. , vol.75 , pp. 2163-2189
    • Prosser, R.S.1    Volkov, V.B.2    Shiyanovskaya, I.V.3
  • 90
    • 77952566893 scopus 로고    scopus 로고
    • Use of copper-chelated lipid speeds up NMR measurements from membrane proteins
    • K. Yamamoto, J. Xu, K.E. Kawulka, J.C. Vederas, and A. Ramamoorthy Use of copper-chelated lipid speeds up NMR measurements from membrane proteins J. Am. Chem. Soc. 132 2010 6929 6931
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6929-6931
    • Yamamoto, K.1    Xu, J.2    Kawulka, K.E.3    Vederas, J.C.4    Ramamoorthy, A.5
  • 91
    • 80054974914 scopus 로고    scopus 로고
    • Fast NMR data acquisition from bicelles containing a membrane-associated peptide at natural-abundance
    • K. Yamamoto, S. Vivekanandan, and A. Ramamoorthy Fast NMR data acquisition from bicelles containing a membrane-associated peptide at natural-abundance J. Phys. Chem. B 115 2011 12448 12455
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12448-12455
    • Yamamoto, K.1    Vivekanandan, S.2    Ramamoorthy, A.3
  • 92
    • 34250303513 scopus 로고    scopus 로고
    • Biphenyl bicelle disks align perpendicular to magnetic fields on large temperature scales: A study combining synthesis, solid-state NMR, TEM, and SAXS
    • DOI 10.1529/biophysj.106.097758
    • C. Loudet, S. Manet, S. Gineste, R. Oda, M.-F. Achard, and E.J. Dufourc Biphenyl bicelle disks align perpendicular to magnetic fields on large temperature scales. A study combining synthesis, solid state NMR, TEM and SAXS Biophys. J. 92 2007 3949 3959 (Pubitemid 46910581)
    • (2007) Biophysical Journal , vol.92 , Issue.11 , pp. 3949-3959
    • Loudet, C.1    Manet, S.2    Gineste, S.3    Oda, R.4    Achard, M.-F.5    Dufourc, E.J.6
  • 93
    • 44649202072 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field
    • S.H. Park, C. Loudet, F.M. Marassi, E.J. Dufourc, and S.J. Opella Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field J. Magn. Reson. 193 2008 133 138
    • (2008) J. Magn. Reson. , vol.193 , pp. 133-138
    • Park, S.H.1    Loudet, C.2    Marassi, F.M.3    Dufourc, E.J.4    Opella, S.J.5
  • 94
    • 0036841870 scopus 로고    scopus 로고
    • Cation modulation of bicelle size and magnetic alignment as revealed by solid-state NMR and electron microscopy
    • A. Arnold, T. Labrot, R. Oda, and E.J. Dufourc Cation modulation of bicelle size and magnetic alignment as revealed by solid-state NMR and electron microscopy Biophys. J. 83 2002 2667 2680 (Pubitemid 35265759)
    • (2002) Biophysical Journal , vol.83 , Issue.5 , pp. 2667-2680
    • Arnold, A.1    Labrot, T.2    Oda, R.3    Dufourc, E.J.4
  • 95
    • 0032919273 scopus 로고    scopus 로고
    • Improved low pH bicelle system for orienting macromolecules over a wide temperature range
    • DOI 10.1023/A:1008360022444
    • S. Cavagnero, H.J. Dyson, and P.E. Wright Improved low pH bicelle system for orienting macromolecules over a wide temperature range J. Biomol. NMR 13 1999 387 391 (Pubitemid 29210332)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.4 , pp. 387-391
    • Cavagnero, S.1    Dyson, H.J.2    Wright, P.E.3
  • 97
    • 0033026167 scopus 로고    scopus 로고
    • Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values
    • DOI 10.1023/A:1008395916985
    • M. Ottiger, and A. Bax Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values J. Biomol. NMR 13 1999 187 191 (Pubitemid 29089229)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.2 , pp. 187-191
    • Ottiger, M.1    Bax, A.2
  • 98
    • 79952000948 scopus 로고    scopus 로고
    • Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: Altered structural information in studies of antimicrobial peptides
    • K. Bertelsen, B. Vad, E.H. Nielsen, S.K. Hansen, T. Skrydstrup, D.E. Otzen, T. Vosegaard, and N.C. Nielsen Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides J. Phys. Chem. B 115 2011 1767 1774
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1767-1774
    • Bertelsen, K.1    Vad, B.2    Nielsen, E.H.3    Hansen, S.K.4    Skrydstrup, T.5    Otzen, D.E.6    Vosegaard, T.7    Nielsen, N.C.8
  • 99
    • 0033627891 scopus 로고    scopus 로고
    • Pegylation of magnetically oriented lipid bilayers
    • V. King, M. Parker, and K.P. Howard Pegylation of magnetically oriented lipid bilayers J. Magn. Reson. 142 2000 177 182
    • (2000) J. Magn. Reson. , vol.142 , pp. 177-182
    • King, V.1    Parker, M.2    Howard, K.P.3
  • 100
    • 0032177257 scopus 로고    scopus 로고
    • Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules
    • J.A. Losonczi, and J.H. Prestegard Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules J. Biomol. NMR 12 1998 447
    • (1998) J. Biomol. NMR , vol.12 , pp. 447
    • Losonczi, J.A.1    Prestegard, J.H.2
  • 101
    • 33746812736 scopus 로고    scopus 로고
    • Effects of lipid chain length and unsaturation on bicelles stability. A phosphorus NMR study
    • DOI 10.1529/biophysj.106.085118
    • M.N. Triba, P.F. Devaux, and D.E. Warschawski Effects of lipid chain length and unsaturation on bicelles stability. A phosphorus NMR study Biophys. J. 91 2006 1357 1367 (Pubitemid 44174252)
    • (2006) Biophysical Journal , vol.91 , Issue.4 , pp. 1357-1367
    • Triba, M.N.1    Devaux, P.F.2    Warschawski, D.E.3
  • 102
    • 77955820270 scopus 로고    scopus 로고
    • Thermal stabilization of DMPC/DHPC bicelles by addition of cholesterol sulfate
    • R.A. Shapiro, A.J. Brindley, and R.W. Martin Thermal stabilization of DMPC/DHPC bicelles by addition of cholesterol sulfate J. Am. Chem. Soc. 132 2010 11406 11407
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11406-11407
    • Shapiro, R.A.1    Brindley, A.J.2    Martin, R.W.3
  • 103
    • 0036434495 scopus 로고    scopus 로고
    • Methods for studying transmembrane peptides in bicelles: Consequences of hydrophobic mismatch and peptide sequence
    • J.A. Whiles, K.J. Glover, R.R. Vold, and E.A. Komives Methods for studying transmembrane peptides in bicelles: consequences of hydrophobic mismatch and peptide sequence J. Magn. Reson. 158 2002 149 156
    • (2002) J. Magn. Reson. , vol.158 , pp. 149-156
    • Whiles, J.A.1    Glover, K.J.2    Vold, R.R.3    Komives, E.A.4
  • 104
    • 0035815973 scopus 로고    scopus 로고
    • Development of magnetically aligned phospholipid bilayers in mixtures of palmitoylstearoylphosphatidylcholine and dihexanoylphosphatidylcholine by solid-state NMR spectroscopy
    • DOI 10.1016/S0005-2736(01)00320-0, PII S0005273601003200
    • E.K. Tiburu, D.M. Moton, and G.A. Lorigan Development of magnetically aligned phospholipid bilayers in mixtures of palmitoylstearoylphosphatidylcholine and dihexanoylphosphatidylcholine by solid-state NMR spectroscopy Biochim. Biophys. Acta 1512 2001 206 214 (Pubitemid 32530767)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1512 , Issue.2 , pp. 206-214
    • Tiburu, E.K.1    Moton, D.M.2    Lorigan, G.A.3
  • 105
    • 0032480641 scopus 로고    scopus 로고
    • 2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles
    • DOI 10.1021/bi981326b
    • 2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles Biochemistry 37 1998 15523 15527 (Pubitemid 28516015)
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15523-15527
    • Struppe, J.1    Komives, E.A.2    Taylor, S.S.3    Vold, R.R.4
  • 106
    • 0034113864 scopus 로고    scopus 로고
    • Acidic phospholipid bicelles: A versatile model membrane system
    • J. Struppe, J.A. Whiles, and R.R. Vold Acidic phospholipid bicelles: a versatile model membrane system Biophys. J. 78 2000 281 289 (Pubitemid 30207137)
    • (2000) Biophysical Journal , vol.78 , Issue.1 , pp. 281-289
    • Struppe, J.1    Whiles, J.A.2    Void, R.R.3
  • 108
    • 1842783195 scopus 로고    scopus 로고
    • The effects of cholesterol on magnetically aligned phospholipid bilayers: A solid-state NMR and EPR spectroscopy study
    • J.-X. Lu, M.A. Caporini, and G.A. Lorigan The effects of cholesterol on magnetically aligned phospholipid bilayers: a solid-state NMR and EPR spectroscopy study J. Magn. Reson. 168 2004 18 30
    • (2004) J. Magn. Reson. , vol.168 , pp. 18-30
    • Lu, J.-X.1    Caporini, M.A.2    Lorigan, G.A.3
  • 109
    • 0842286078 scopus 로고    scopus 로고
    • 2H NMR studies of the effects of cholesterol on the acyl chain dynamics of magnetically aligned phospholipid bilayers
    • DOI 10.1002/mrc.1324
    • 2H NMR studies of the effects of cholesterol on the acyl chain dynamics of magnetically aligned phospholipid bilayers Magn. Reson. Chem. 42 2004 132 138 (Pubitemid 38178081)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 132-138
    • Tiburu, E.K.1    Dave, P.C.2    Lorigan, G.A.3
  • 110
    • 7644223948 scopus 로고    scopus 로고
    • 2H solid-state NMR spectroscopic investigation of biomimetic bicelles containing cholesterol and polyunsaturated phosphatidylcholine
    • DOI 10.1016/j.chemphyslip.2004.09.005, PII S0009308404001380
    • 2H solid-state NMR spectroscopic investigation of biomimetic bicelles containing cholesterol and polyunsaturated phosphatidylcholine Chem. Phys. Lip. 132 2004 55 64 (Pubitemid 39458320)
    • (2004) Chemistry and Physics of Lipids , vol.132 , Issue.1 , pp. 55-64
    • Minto, R.E.1    Adhikari, P.R.2    Lorigan, G.A.3
  • 115
    • 77956448654 scopus 로고    scopus 로고
    • Triton X-100 as the 'short chain lipid' improves the magnetic alignment and stability of membrane proteins in phosphatidylcholine bilayers for oriented sample (OS) solid-state NMR spectroscopy
    • S.H. Park, and S.J. Opella Triton X-100 as the 'short chain lipid' improves the magnetic alignment and stability of membrane proteins in phosphatidylcholine bilayers for oriented sample (OS) solid-state NMR spectroscopy J. Am. Chem. Soc. 132 2010 12552 12553
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12552-12553
    • Park, S.H.1    Opella, S.J.2
  • 116
    • 84857769505 scopus 로고
    • Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis
    • O.V. Nolandt, T.H. Walther, S.L. Grage, and A.S. Ulrich Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis Biochim. Biophys. Acta 2012 1818 1142 1147
    • (1818) Biochim. Biophys. Acta , vol.2012 , pp. 1142-1147
    • Nolandt, O.V.1    Walther, T.H.2    Grage, S.L.3    Ulrich, A.S.4
  • 117
    • 0033531682 scopus 로고    scopus 로고
    • Magnetically oriented phospholipid bilayers for spin label EPR studies [12]
    • DOI 10.1021/ja984371f
    • S.M. Garber, G.A. Lorigan, and K.P. Howard Magnetically oriented phospholipid bilayers for spin label EPR studies J. Am. Chem. Soc. 121 1999 3240 3241 (Pubitemid 29189781)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.13 , pp. 3240-3241
    • Garber, S.M.1    Lorigan, G.A.2    Howard, K.P.3
  • 118
    • 0034718082 scopus 로고    scopus 로고
    • Spectroscopic characterization of spin-labeled magnetically oriented phospolipid bilayers by EPR spectroscopy
    • DOI 10.1021/ja000195a
    • M.L. Mangels, T.B. Cardon, A.C. Harper, K.P. Howard, and G.A. Lorigan Spectroscopic characterization of spin-labeled magnetically oriented phospholipid bilayers by EPR spectroscopy J. Am. Chem. Soc. 122 2000 7052 7058 (Pubitemid 30639880)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.29 , pp. 7052-7058
    • Mangels, M.L.1    Cardon, T.B.2    Harper, A.C.3    Howard, K.P.4    Lorigan, G.A.5
  • 119
    • 0034806920 scopus 로고    scopus 로고
    • Magnetically aligned phospholipid bilayers at the parallel and perpendicular orientations for X-band spin-label EPR studies
    • DOI 10.1021/ja005574i
    • T.B. Cardon, E.K. Tiburu, A. Padmanabhan, K.P. Howard, and G.A. Lorigan Magnetically aligned phospholipid bilayers at the parallel and perpendicular orientations for X-band spin-label EPR studies J. Am. Chem. Soc. 123 2001 2913 2914 (Pubitemid 32910730)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.12 , pp. 2913-2914
    • Cardon, T.B.1    Tiburu, E.K.2    Padmanabhan, A.3    Howard, K.P.4    Lorigan, G.A.5
  • 120
    • 11844264798 scopus 로고    scopus 로고
    • Investigating the structural and dynamic properties of n-doxylstearic acid in magnetically-aligned phospholipid bilayers by X-band EPR spectroscopy
    • DOI 10.1016/j.chemphyslip.2004.09.019, PII S0009308404001549
    • N.A. Nusair, and G.A. Lorigan Investigating the structural and dynamic properties of n-doxylstearic acid in magnetically-aligned phospholipid bilayers by X-band EPR spectroscopy Chem. Phys. Lip. 133 2005 151 164 (Pubitemid 40092116)
    • (2005) Chemistry and Physics of Lipids , vol.133 , Issue.2 , pp. 151-164
    • Nusair, N.A.1    Lorigan, G.A.2
  • 121
    • 3142697673 scopus 로고    scopus 로고
    • Electron paramagnetic resonance studies of magnetically aligned phospholipid bilayers utilizing a phospholipid spin label
    • P.C. Dave, J.J. Inbaraj, and G.A. Lorigan Electron paramagnetic resonance studies of magnetically aligned phospholipid bilayers utilizing a phospholipid spin label Langmuir 20 2004 5801 5808
    • (2004) Langmuir , vol.20 , pp. 5801-5808
    • Dave, P.C.1    Inbaraj, J.J.2    Lorigan, G.A.3
  • 122
    • 7544228302 scopus 로고    scopus 로고
    • Investigating magnetically aligned phospholipid bilayers with EPR spectroscopy at Q-band (35 GHz): Optimization and comparison with X-band (9 GHz)
    • J.J. Inbaraj, N.A. Nusair, and G.A. Lorigan Investigating magnetically aligned phospholipid bilayers with EPR spectroscopy at Q-band (35 GHz): Optimization and comparison with X-band (9 GHz) J. Magn. Reson. 171 2004 71 79
    • (2004) J. Magn. Reson. , vol.171 , pp. 71-79
    • Inbaraj, J.J.1    Nusair, N.A.2    Lorigan, G.A.3
  • 123
    • 0035743313 scopus 로고    scopus 로고
    • Investigating magnetically aligned phospholipid bilayers with EPR spectroscopy at 94 GHz
    • M.L. Mangels, A.C. Harper, A.I. Smirnov, K.P. Howard, and G.A. Lorigan Investigating magnetically aligned phospholipid bilayers with EPR spectroscopy at 94 GHz J. Magn. Reson. 151 2001 253 259
    • (2001) J. Magn. Reson. , vol.151 , pp. 253-259
    • Mangels, M.L.1    Harper, A.C.2    Smirnov, A.I.3    Howard, K.P.4    Lorigan, G.A.5
  • 125
    • 23644452497 scopus 로고    scopus 로고
    • Electron paramagnetic resonance studies of magnetically aligned phospholipid bilayers utilizing a phospholipid spin label: The effect of cholesterol
    • DOI 10.1016/j.bbamem.2005.06.009, PII S0005273605001975
    • P.C. Dave, N.A. Nusair, J.J. Inbaraj, and G.A. Lorigan Electron paramagnetic resonance studies of magnetically aligned phospholipid bilayers utilizing a phospholipid spin label: the effect of cholesterol Biochim. Biophys. Acta 1714 2005 141 151 (Pubitemid 41133616)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1714 , Issue.2 , pp. 141-151
    • Dave, P.C.1    Nusair, N.A.2    Inbaraj, J.J.3    Lorigan, G.A.4
  • 126
    • 67649467269 scopus 로고    scopus 로고
    • A comparative study of cholesterol on bicelle model membranes using X-band and Q-band EPR spectroscopy
    • H. Ghimire, J.J. Inbaraj, and G.A. Lorigan A comparative study of cholesterol on bicelle model membranes using X-band and Q-band EPR spectroscopy Chem. Phys. Lip. 160 2009 98 104
    • (2009) Chem. Phys. Lip. , vol.160 , pp. 98-104
    • Ghimire, H.1    Inbaraj, J.J.2    Lorigan, G.A.3
  • 127
    • 79954450578 scopus 로고    scopus 로고
    • Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy
    • T. Gruene, M.-K. Cho, I. Karyagina, H.-Y. Kim, C. Grosse, K. Giller, M. Zweckstetter, and S. Becker Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy J. Biomol. NMR 49 2011 111 119
    • (2011) J. Biomol. NMR , vol.49 , pp. 111-119
    • Gruene, T.1    Cho, M.-K.2    Karyagina, I.3    Kim, H.-Y.4    Grosse, C.5    Giller, K.6    Zweckstetter, M.7    Becker, S.8
  • 128
    • 84855748562 scopus 로고
    • Probing the helical tilt and dynamic properties of membrane-bound phospholamban in magnetically aligned bicelles using electron paramagnetic resonance spectroscopy
    • H. Ghimire, S. Abu-Baker, I.D. Sahu, A. Zhou, D.J. Mayo, R.T. Lee, and G.A. Lorigan Probing the helical tilt and dynamic properties of membrane-bound phospholamban in magnetically aligned bicelles using electron paramagnetic resonance spectroscopy Biochim. Biophys. Acta 2011 1818 645 650
    • (1818) Biochim. Biophys. Acta , vol.2011 , pp. 645-650
    • Ghimire, H.1    Abu-Baker, S.2    Sahu, I.D.3    Zhou, A.4    Mayo, D.J.5    Lee, R.T.6    Lorigan, G.A.7
  • 131
    • 63349105151 scopus 로고    scopus 로고
    • Determining the helical tilt of membrane peptides using electron paramagnetic resonance spectroscopy
    • J.P. Newstadt, D.J. Mayo, J.J. Inbaraj, N. Subbaraman, and G.A. Lorigan Determining the helical tilt of membrane peptides using electron paramagnetic resonance spectroscopy J. Magn. Reson. 198 2009 1 7
    • (2009) J. Magn. Reson. , vol.198 , pp. 1-7
    • Newstadt, J.P.1    Mayo, D.J.2    Inbaraj, J.J.3    Subbaraman, N.4    Lorigan, G.A.5
  • 134
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • E.R. Georgieva, T.F. Ramlall, P.P. Borbat, J.H. Freed, and D. Eliezer Membrane-bound alpha-synuclein forms an extended helix: long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles J. Am. Chem. Soc. 130 2008 12856 12857
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 136
    • 64049090768 scopus 로고    scopus 로고
    • Nanopore formation on unilamellar vesicles of long- and short-chain lipids
    • N.L. Yamada, M. Hishida, and N. Torikai Nanopore formation on unilamellar vesicles of long- and short-chain lipids Phys. Rev. E 79 2009 032902
    • (2009) Phys. Rev. e , vol.79 , pp. 032902
    • Yamada, N.L.1    Hishida, M.2    Torikai, N.3
  • 138
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: Theory and application to lipid membranes
    • J. Seelig Deuterium magnetic resonance: theory and application to lipid membranes Q. Rev. Biophys. 10 1977 353 418 (Pubitemid 8203096)
    • (1977) Quarterly Reviews of Biophysics , vol.10 , Issue.3 , pp. 353-418
    • Seelig, J.1
  • 140
    • 0025980621 scopus 로고
    • Phospholipid phase transitions as revealed by NMR
    • A. Watts, and P.J.R. Spooner Phospholipid phase transitions as revealed by NMR Chem. Phys. Lip. 57 1991 195 211
    • (1991) Chem. Phys. Lip. , vol.57 , pp. 195-211
    • Watts, A.1    Spooner, P.J.R.2
  • 141
    • 0032586679 scopus 로고    scopus 로고
    • 31P NMR first spectral moment study of the partial magnetic orientation of phospholipid membranes
    • 31P NMR first sprectral moment study of the partial magnetic orientation of phospholipid membranes Biophys. J. 77 1999 888 902 (Pubitemid 29362460)
    • (1999) Biophysical Journal , vol.77 , Issue.2 , pp. 888-902
    • Picard, F.1    Paquet, M.-J.2    Levesque, J.3    Belanger, A.4    Auger, M.5
  • 142
    • 0035743686 scopus 로고    scopus 로고
    • Simultaneous determination of orientational and order parameter distributions from NMR spectra of partially oriented model membranes
    • E. Sternin, H. Schäfer, I.V. Polozov, and K. Gawrisch Simultaneous determination of orientational and order parameter distributions from NMR spectra of partially oriented model membranes J. Magn. Reson. 149 2001 110 113
    • (2001) J. Magn. Reson. , vol.149 , pp. 110-113
    • Sternin, E.1    Schäfer, H.2    Polozov, I.V.3    Gawrisch, K.4
  • 143
    • 0035353437 scopus 로고    scopus 로고
    • Temperature dependence of DMPC/DHPC mixing in a bicellar solution and its structural implications
    • E. Sternin, D. Nizza, and K. Gawrisch Temperature dependence of DMPC/DHPC mixing in bicellar solution and its structural implications Langmuir 17 2001 2610 2616 (Pubitemid 35330510)
    • (2001) Langmuir , vol.17 , Issue.9 , pp. 2610-2616
    • Sternin, E.1    Nizza, D.2    Gawrisch, K.3
  • 144
    • 21244486782 scopus 로고    scopus 로고
    • Reinvestigation by phosphorus NMR of lipid distribution in bicelles
    • DOI 10.1529/biophysj.104.055061
    • M.N. Triba, D.E. Warschawski, and P.F. Devaux Reinvestigation by phosphorus NMR of lipid distribution in bicelles Biophys. J. 88 2005 1887 1901 (Pubitemid 40976201)
    • (2005) Biophysical Journal , vol.88 , Issue.3 , pp. 1887-1901
    • Triba, M.N.1    Warschawski, D.E.2    Devaux, P.F.3
  • 145
    • 0032174883 scopus 로고    scopus 로고
    • Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules
    • M. Ottiger, and A. Bax Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules J. Biomol. NMR 12 1998 361 372 (Pubitemid 128511302)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.3 , pp. 361-372
    • Ottiger, M.1    Bax, A.2
  • 147
    • 0035353378 scopus 로고    scopus 로고
    • SANS study of the structural phases of magnetically alignable lanthanide-doped phospholipid mixtures
    • M.-P. Nieh, C.J. Glinka, S. Krueger, R.S. Prosser, and J. Katsaras SANS study of the structural phases of magnetically alignable lanthanide-doped phospholipid mixtures Langmuir 17 2001 2629 2638 (Pubitemid 35330513)
    • (2001) Langmuir , vol.17 , Issue.9 , pp. 2629-2638
    • Nieh, M.-P.1    Glinka, C.J.2    Krueger, S.3    Prosser, R.S.4    Katsaras, J.5
  • 148
    • 20744436366 scopus 로고    scopus 로고
    • Comprehensive examination of mesophases formed by DMPC and DHPC mixtures
    • DOI 10.1021/la050018t
    • T.A. Harroun, M. Koslowsky, M.-P. Nieh, C.-F. de Lannoy, V.A. Raghunathan, and J. Katsaras Comprehensive examination of mesophases formed by DMPC and DHPC mixtures Langmuir 21 2005 5356 5361 (Pubitemid 40850619)
    • (2005) Langmuir , vol.21 , Issue.12 , pp. 5356-5361
    • Harroun, T.A.1    Koslowsky, M.2    Nieh, M.-P.3    De Lannoy, C.-F.4    Raghunathan, V.A.5    Katsaras, J.6
  • 149
    • 27644528605 scopus 로고    scopus 로고
    • "Bicellar" lipid mixtures as used in biochemical and biophysical studies
    • DOI 10.1007/s00114-005-0641-1
    • J. Katsaras, T.A. Harroun, J. Pencer, and M.-P. Nieh "Bicellar" lipid mixtures as used in biochemical and biophysical studies Naturwissenschaften 92 2005 355 366 (Pubitemid 41561579)
    • (2005) Naturwissenschaften , vol.92 , Issue.8 , pp. 355-366
    • Katsaras, J.1    Harroun, T.A.2    Pencer, J.3    Nieh, M.-P.4
  • 150
    • 17444365826 scopus 로고    scopus 로고
    • Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins
    • I. Marcotte, and M. Auger Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins Conc. Magn. Reson. 24A 2005 17 37
    • (2005) Conc. Magn. Reson. , vol.24 A , pp. 17-37
    • Marcotte, I.1    Auger, M.2
  • 151
    • 0032238007 scopus 로고    scopus 로고
    • Dilute Bicellar Solutions for Structural NMR Work
    • J. Struppe, and R.R. Vold Dilute bicellar solutions for structural NMR work J. Magn. Reson. 135 1998 541 546 (Pubitemid 128452147)
    • (1998) Journal of Magnetic Resonance , vol.135 , Issue.2 , pp. 541-546
    • Struppe, J.1    Vold, R.R.2
  • 152
    • 33747570634 scopus 로고    scopus 로고
    • Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides. Does the ideal bicelle exist?
    • R.R. Vold, and R.S. Prosser Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides. Does the ideal bicelle exist? J. Magn. Reson. B 113 1996 267 271 (Pubitemid 126758778)
    • (1996) Journal of Magnetic Resonance - Series B , vol.113 , Issue.3 , pp. 267-271
    • Vold, R.R.1    Prosser, R.S.2
  • 153
    • 0031112791 scopus 로고    scopus 로고
    • Isotropic solutions of phospholipid bicelles: A new membrane mimetic for high-resolution NMR studies of polypeptides
    • R.R. Vold, R.S. Prosser, and A.J. Deese Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides J. Biomol. NMR 9 1997 329 335 (Pubitemid 127505395)
    • (1997) Journal of Biomolecular NMR , vol.9 , Issue.3 , pp. 329-335
    • Vold, R.R.1    Prosser, R.S.2    Deese, A.J.3
  • 155
  • 156
    • 0035852133 scopus 로고    scopus 로고
    • Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy
    • DOI 10.1021/ja011967l
    • S. Gaemers, and A. Bax Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy J. Am. Chem. Soc. 123 2001 12343 12352 (Pubitemid 33136071)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.49 , pp. 12343-12352
    • Gaemers, S.1    Bax, A.2
  • 157
    • 0037453570 scopus 로고    scopus 로고
    • Fluorescence probe study of bicelle structure as a function of temperature: Developing a practical bicelle structure model
    • B.A. Rowe, and S.L. Neal Fluorescence probe study of bicelle structure as
    • (2003) Langmuir , vol.19 , pp. 2039-2048
    • Rowe, B.A.1    Neal, S.L.2
  • 158
    • 0041377766 scopus 로고    scopus 로고
    • Anomalous viscosity behavior of a bicelle system with various molar ratios of short- and long-chain phospholipids
    • J.S. Hwang, and G.A. Oweimreen Anomalous viscosity behavior of a bicelle system with various molar ratios of short- and long-chain phospholipids Arab. J. Sci. Eng. 28 2003 43 49 (Pubitemid 37067818)
    • (2003) Arabian Journal for Science and Engineering , vol.28 , Issue.1 A , pp. 43-49
    • Hwang, J.S.1    Oweimreen, G.A.2
  • 159
    • 4644372496 scopus 로고    scopus 로고
    • Magnetically alignable phase of phospholipid "bicelle" mixtures is a chiral nematic made up of wormlike micelles
    • M.-P. Nieh, V.A. Raghunathan, C.J. Glinka, T.A. Harroun, G. Pabst, and J. Katsaras Magnetically alignable phase of phospholipid "bicelle" mixtures is a chiral nematic made up of wormlike micelles Langmuir 20 2004 7893 7897
    • (2004) Langmuir , vol.20 , pp. 7893-7897
    • Nieh, M.-P.1    Raghunathan, V.A.2    Glinka, C.J.3    Harroun, T.A.4    Pabst, G.5    Katsaras, J.6
  • 160
    • 4344582879 scopus 로고    scopus 로고
    • Direct observation and characterization of DMPC/DHPC aggregates under conditions relevant for biological solution NMR
    • DOI 10.1016/j.bbamem.2004.06.005, PII S0005273604001506
    • L. van Dam, G. Karlsson, and K. Edwards Direct observation and characterization of DMPC/DHPC aggregates under conditions relevant for biological solution NMR Biochim. Biophys. Acta 1664 2004 241 256 (Pubitemid 39140998)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1664 , Issue.2 , pp. 241-256
    • Van Dam, L.1    Karlsson, G.2    Edwards, K.3
  • 161
    • 58449136911 scopus 로고    scopus 로고
    • Use of high-pressure freeze fixation and freeze fracture electron microscopy to study the influence of the phospholipid molar ratio in the morphology and alignment of bicelles
    • L. Barbosa-Barros, A. de la Maza, P. Walther, A.M. Linares, M. Feliz, J. Estelrich, and O. López Use of high-pressure freeze fixation and freeze fracture electron microscopy to study the influence of the phospholipid molar ratio in the morphology and alignment of bicelles J. Microsc. 233 2009 35 41
    • (2009) J. Microsc. , vol.233 , pp. 35-41
    • Barbosa-Barros, L.1    De La Maza, A.2    Walther, P.3    Linares, A.M.4    Feliz, M.5    Estelrich, J.6    López, O.7
  • 164
    • 0345098288 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of the Formation, Structure, and Dynamics of Small Phospholipid Vesicles
    • DOI 10.1021/ja0352092
    • S.J. Marrink, and A.E. Mark Molecular dynamics simulation of the formation, structure, and dynamics of small phospholipid vesicles J. Am. Chem. Soc. 125 2003 15233 15242 (Pubitemid 37509686)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.49 , pp. 15233-15242
    • Marrink, S.J.1    Mark, A.E.2
  • 165
    • 77952710577 scopus 로고    scopus 로고
    • Zwitterionic lipid assemblies: Molecular dynamics studies of monolayers, bilayers, and vesicles using a new coarse grain force field
    • W. Shinoda, R. DeVane, and M.L. Klein Zwitterionic lipid assemblies: molecular dynamics studies of monolayers, bilayers, and vesicles using a new coarse grain force field J. Phys. Chem. B 114 2010 6836 6849
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6836-6849
    • Shinoda, W.1    Devane, R.2    Klein, M.L.3
  • 166
    • 79959789789 scopus 로고    scopus 로고
    • Modeling the self-assembly of lipids and nanotubes in solution: Forming vesicles and bicelles with transmembrane nanotube channels
    • M. Dutt, O. Kuksenok, M.J. Nayhouse, S.R. Little, and A.C. Balazs Modeling the self-assembly of lipids and nanotubes in solution: forming vesicles and bicelles with transmembrane nanotube channels ACS Nano 5 2011 4769 4782
    • (2011) ACS Nano , vol.5 , pp. 4769-4782
    • Dutt, M.1    Kuksenok, O.2    Nayhouse, M.J.3    Little, S.R.4    Balazs, A.C.5
  • 167
    • 33847765026 scopus 로고    scopus 로고
    • Simulations of edge behavior in a mixed-lipid bilayer: Fluctuation analysis
    • Y. Jiang, and J.T. Kindt Simulations of edge behavior in a mixed-lipid bilayer: fluctuation analysis J. Chem. Phys. 126 2007 045105
    • (2007) J. Chem. Phys. , vol.126 , pp. 045105
    • Jiang, Y.1    Kindt, J.T.2
  • 169
    • 77953547641 scopus 로고    scopus 로고
    • Atomistic simulations of bicelle mixtures
    • Y. Jiang, H. Wang, and J.T. Kindt Atomistic simulations of bicelle mixtures Biophys. J. 98 2010 2895 2903
    • (2010) Biophys. J. , vol.98 , pp. 2895-2903
    • Jiang, Y.1    Wang, H.2    Kindt, J.T.3
  • 170
    • 36849101148 scopus 로고
    • Use of the stimulated echo in NMR diffusion studies
    • J.E. Tanner Use of the stimulated echo in NMR diffusion studies J. Chem. Phys. 52 1970 2523 2526
    • (1970) J. Chem. Phys. , vol.52 , pp. 2523-2526
    • Tanner, J.E.1
  • 172
    • 33746045690 scopus 로고    scopus 로고
    • Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins
    • DOI 10.1021/bi060615u
    • R.S. Prosser, F. Evanics, J.L. Kitevski, and M.S. Al-Abdul-Wahid Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins Biochemistry 45 2006 8453 8465 (Pubitemid 44078865)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8453-8465
    • Prosser, R.S.1    Evanics, F.2    Kitevski, J.L.3    Al-Abdul-Wahid, M.S.4
  • 173
    • 3042767203 scopus 로고    scopus 로고
    • Characterization of phospholipid mixed micelles by translational diffusion
    • DOI 10.1023/B:JNMR.0000032560.43738.6a
    • J.J. Chou, J.L. Baber, and A. Bax Characterization of phospholipid mixed micelles by translational diffusion J. Biomol. NMR 29 2004 299 308 (Pubitemid 38864828)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.3 , pp. 299-308
    • Chou, J.J.1    Baber, J.L.2    Bax, A.3
  • 174
    • 33645509371 scopus 로고    scopus 로고
    • Magnetic resonance investigations of lipid motion in isotropic bicelles
    • DOI 10.1021/la0513003
    • A. Andersson, and L. Mäler Magnetic resonance investigations of lipid motion in isotropic bicelles Langmuir 21 2005 7702 7709 (Pubitemid 44323794)
    • (2005) Langmuir , vol.21 , Issue.17 , pp. 7702-7709
    • Andersson, A.1    Maler, L.2
  • 175
    • 33645520516 scopus 로고    scopus 로고
    • Size and shape of fast-tumbling bicelles as determined by translational diffusion
    • A. Andersson, and L. Mäler Size and shape of fast-tumbling bicelles as determined by translational diffusion Langmuir 22 2006 2447 2449
    • (2006) Langmuir , vol.22 , pp. 2447-2449
    • Andersson, A.1    Mäler, L.2
  • 176
    • 54049129612 scopus 로고    scopus 로고
    • Lipid dynamics in fast-tumbling bicelles with varying bilayer thickness: Effect of model transmembrane peptides
    • J. Lind, J. Nordin, and L. Mäler Lipid dynamics in fast-tumbling bicelles with varying bilayer thickness: effect of model transmembrane peptides Biochim. Biophys. Acta 1778 2008 2526 2534
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 2526-2534
    • Lind, J.1    Nordin, J.2    Mäler, L.3
  • 177
    • 0030059158 scopus 로고    scopus 로고
    • Conformational constraints on the headgroup and sn-2 chain of bilayer DMPC from NMR dipolar couplings
    • DOI 10.1021/bi953083i
    • M. Hong, K. Schmidt-Rohr, and H. Zimmermann Conformational constraints on the headgroup and sn-2 chain of bilayer DMPC from NMR dipolar couplings Biochemistry 35 1996 8335 8341 (Pubitemid 26234938)
    • (1996) Biochemistry , vol.35 , Issue.25 , pp. 8335-8341
    • Hong, M.1    Schmidt-Rohr, K.2    Zimmermann, H.3
  • 179
    • 84906393014 scopus 로고    scopus 로고
    • Uniaxial motional averaging of the chemical shift anisotropy of membrane proteins in bilayer environments
    • A. Ramamoorthy, CRC Press New York
    • A.A. Nevzorov, A.A. De Angelis, S.H. Park, and S.J. Opella Uniaxial motional averaging of the chemical shift anisotropy of membrane proteins in bilayer environments A. Ramamoorthy, NMR Spectroscopy of Biological Solids 2006 CRC Press New York 177 190
    • (2006) NMR Spectroscopy of Biological Solids , pp. 177-190
    • Nevzorov, A.A.1    De Angelis, A.A.2    Park, S.H.3    Opella, S.J.4
  • 180
    • 33846625059 scopus 로고    scopus 로고
    • Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles
    • DOI 10.1016/j.jmr.2006.10.004, PII S1090780706003387
    • S.V. Dvinskikh, K. Yamamoto, U.H.N. Dürr, and A. Ramamoorthy Sensitivity and resolution enhancement in solid-state NMR spectroscopy of bicelles J. Magn. Reson. 184 2007 228 235 (Pubitemid 46177668)
    • (2007) Journal of Magnetic Resonance , vol.184 , Issue.2 , pp. 228-235
    • Dvinskikh, S.V.1    Yamamoto, K.2    Durr, U.H.N.3    Ramamoorthy, A.4
  • 181
    • 33746317772 scopus 로고    scopus 로고
    • Heteronuclear isotropic mixing separated local field NMR spectroscopy
    • S.V. Dvinskikh, K. Yamamoto, and A. Ramamoorthy Heteronuclear isotropic mixing separated local field NMR spectroscopy J. Chem. Phys. 125 2006 034507
    • (2006) J. Chem. Phys. , vol.125 , pp. 034507
    • Dvinskikh, S.V.1    Yamamoto, K.2    Ramamoorthy, A.3
  • 182
    • 30844466828 scopus 로고    scopus 로고
    • 13C heteronuclear dipolar solid-state NMR spectroscopy
    • DOI 10.1016/j.jmr.2005.09.006, PII S1090780705003083
    • 13C heteronuclear dipolar solid-state NMR spectroscopy J. Magn. Reson. 178 2006 283 287 (Pubitemid 43107934)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.2 , pp. 283-287
    • Lu, J.-X.1    Damodaran, K.2    Lorigan, G.A.3
  • 183
    • 33846609269 scopus 로고    scopus 로고
    • High-resolution 2D NMR spectroscopy of bicelles to measure the membrane interaction of ligands
    • DOI 10.1021/ja065536k
    • S.V. Dvinskikh, U.H.N. Dürr, K. Yamamoto, and A. Ramamoorthy High-resolution 2D NMR spectroscopy of bicelles to measure the membrane interaction of ligands J. Am. Chem. Soc. 129 2007 794 802 (Pubitemid 46183929)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.4 , pp. 794-802
    • Dvinskikh, S.V.1    Durr, U.H.N.2    Yamamoto, K.3    Ramamoorthy, A.4
  • 185
    • 18844438694 scopus 로고    scopus 로고
    • PITANSEMA-MAS, a solid-state NMR method to measure heteronuclear dipolar couplings under MAS
    • DOI 10.1016/j.cplett.2005.04.017, PII S0009261405005348
    • K. Yamamoto, V.L. Ermakov, D.K. Lee, and A. Ramamoorthy PITANSEMA-MAS, a solid-state NMR method to measure heteronuclear dipolar couplings under MAS Chem. Phys. Lett. 408 2005 118 122 (Pubitemid 40684030)
    • (2005) Chemical Physics Letters , vol.408 , Issue.1-3 , pp. 118-122
    • Yamamoto, K.1    Ermakov, V.L.2    Lee, D.K.3    Ramamoorthy, A.4
  • 186
    • 33846595904 scopus 로고
    • High-resolution heteronuclear dipolar solid-state NMR spectroscopy
    • C.H. Wu, A. Ramamoorthy, and S.J. Opella High-resolution heteronuclear dipolar solid-state NMR spectroscopy J. Magn. Reson. A 109 1994 270 272
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 187
    • 0042468159 scopus 로고    scopus 로고
    • A "magic sandwich" pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy
    • A.A. Nevzorov, and S.J. Opella A "magic sandwich" pulse sequence with reduced offset dependence for high-resolution separated local field spectroscopy J. Magn. Reson. 164 2003 182 186
    • (2003) J. Magn. Reson. , vol.164 , pp. 182-186
    • Nevzorov, A.A.1    Opella, S.J.2
  • 188
    • 10944242116 scopus 로고    scopus 로고
    • PISEMA Solid-State NMR Spectroscopy
    • DOI 10.1016/S0066-4103(04)52001-X, PII S006641030452001X
    • A. Ramamoorthy, Y. Wei, and D.-K. Lee PISEMA solid-state NMR spectroscopy Annu. Rep. NMR Spectrosc. 52 2004 1 52 (Pubitemid 39752334)
    • (2004) Annual Reports on NMR Spectroscopy , vol.52 , pp. 1-52
    • Ramamoorthy, A.1    Wei, Y.2    Lee, D.-K.3
  • 189
    • 33646594751 scopus 로고    scopus 로고
    • A high-resolution solid-state NMR approach for the structural studies of bicelles
    • DOI 10.1021/ja061153a
    • S.V. Dvinskikh, U.H.N. Dürr, K. Yamamoto, and A. Ramamoorthy A high-resolution solid-state NMR approach for the structural studies of bicelles J. Am. Chem. Soc. 128 2006 6326 6327 (Pubitemid 43727264)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.19 , pp. 6326-6327
    • Dvinskikh, S.1    Durr, U.2    Yamamoto, K.3    Ramamoorthy, A.4
  • 190
    • 43949161069 scopus 로고
    • Ramped-amplitude cross polarization in magic-angle-spinning NMR
    • G. Metz, X. Wu, and S.O. Smith Ramped-amplitude cross polarization in magic-angle-spinning NMR J. Magn. Reson. Ser. A 110 1994 219 227
    • (1994) J. Magn. Reson. Ser. A , vol.110 , pp. 219-227
    • Metz, G.1    Wu, X.2    Smith, S.O.3
  • 191
    • 0000354437 scopus 로고
    • Improvements in carbon-13 broadband homonuclear cross-polarization for 2D and 3D NMR
    • A. Mohebbi, and A.J. Shaka Improvements in carbon-13 broadband homonuclear cross-polarization for 2D and 3D NMR Chem. Phys. Lett. 178 1991 374 378
    • (1991) Chem. Phys. Lett. , vol.178 , pp. 374-378
    • Mohebbi, A.1    Shaka, A.J.2
  • 192
    • 79955426449 scopus 로고    scopus 로고
    • A proton spin diffusion based solid-state NMR approach for structural studies in aligned samples
    • J. Xu, P.E.S. Smith, R. Soong, and A. Ramamoorthy A proton spin diffusion based solid-state NMR approach for structural studies in aligned samples J. Phys. Chem. B 115 2011 4863 4871
    • (2011) J. Phys. Chem. B , vol.115 , pp. 4863-4871
    • Xu, J.1    Smith, P.E.S.2    Soong, R.3    Ramamoorthy, A.4
  • 193
    • 66749144692 scopus 로고    scopus 로고
    • Comprehensive analysis of lipid dynamics variation with lipid composition and hydration of bicelles using nuclear magnetic resonance (NMR) spectroscopy
    • K. Yamamoto, R. Soong, and A. Ramamoorthy Comprehensive analysis of lipid dynamics variation with lipid composition and hydration of bicelles using nuclear magnetic resonance (NMR) spectroscopy Langmuir 25 2009 7010 7018
    • (2009) Langmuir , vol.25 , pp. 7010-7018
    • Yamamoto, K.1    Soong, R.2    Ramamoorthy, A.3
  • 194
    • 0028929692 scopus 로고
    • Restatement of order parameters in biomembranes: Calculation of C-C bond order parameters from C-D quadrupolar splittings
    • J.-P. Douliez, A. Léonard, and E.J. Dufourc Restatement of order parameters in biomembranes: calculation of C-C bond order parameters from C-D quadrupolar splittings Biophys. J. 68 1995 1727 1739
    • (1995) Biophys. J. , vol.68 , pp. 1727-1739
    • Douliez, J.-P.1    Léonard, A.2    Dufourc, E.J.3
  • 196
    • 0018788297 scopus 로고
    • The molecular structure of lecithin dihydrate
    • R.H. Pearson, and I. Pascher The molecular structure of lecithin dihydrate Nature 281 1979 499 501
    • (1979) Nature , vol.281 , pp. 499-501
    • Pearson, R.H.1    Pascher, I.2
  • 197
    • 34248583208 scopus 로고    scopus 로고
    • All-atom molecular dynamics simulations using orientational constraints from anisotropic NMR samples
    • DOI 10.1007/s10858-007-9142-1
    • U. Sternberg, R. Witter, and A.S. Ulrich All-atom molecular dynamics simulations using orientational constraints from anisotropic NMR samples J. Biomol. NMR 38 2007 23 39 (Pubitemid 46745439)
    • (2007) Journal of Biomolecular NMR , vol.38 , Issue.1 , pp. 23-39
    • Sternberg, U.1    Witter, R.2    Ulrich, A.S.3
  • 198
    • 0032942641 scopus 로고    scopus 로고
    • Surface charge response of the phosphatidylcholine head group in bilayered micelles from phosphorus and deuterium nuclear magnetic resonance
    • DOI 10.1016/S0005-2736(98)00206-5, PII S0005273698002065
    • K.J. Crowell, and P.M. Macdonald Surface charge response of the phosphatidylcholine head group in bilayered micelles from phosphorus and deuterium nuclear magnetic resonance Biochim. Biophys. Acta 1416 1999 21 30 (Pubitemid 29065421)
    • (1999) Biochimica et Biophysica Acta - Biomembranes , vol.1416 , Issue.1-2 , pp. 21-30
    • Crowell, K.J.1    Macdonald, P.M.2
  • 199
  • 200
    • 0842329187 scopus 로고    scopus 로고
    • Conformational response of the phosphatidylcholine headgroup to bilayer surface charge: Torsion angle constraints from dipolar and quadrupolar couplings in bicelles
    • DOI 10.1002/mrc.1333
    • D.J. Semchyschyn, and P.M. Macdonald Conformational response of the phosphatidylcholine headgroup to bilayer surface charge: torsion angle constraints from dipolar and quadrupolar couplings in bicelles Magn. Reson. Chem. 42 2004 89 104 (Pubitemid 38178077)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 89-104
    • Semchyschyn, D.J.1    Macdonald, P.M.2
  • 201
    • 0842286082 scopus 로고    scopus 로고
    • Effects of antidepressants on the conformation of phospholipid headgroups studied by solid-state NMR
    • DOI 10.1002/mrc.1327
    • J.S. Santos, D.-K. Lee, and A. Ramamoorthy Effects of antidepressants on the conformation of phospholipid headgroups studied by solid-state NMR Magn. Reson. Chem. 42 2004 105 114 (Pubitemid 38178078)
    • (2004) Magnetic Resonance in Chemistry , vol.42 , Issue.2 , pp. 105-114
    • Santos, J.S.1    Lee, D.-K.2    Ramamoorthy, A.3
  • 202
    • 75749138064 scopus 로고    scopus 로고
    • Presentation of membrane-anchored glycosphingolipids determined from molecular dynamics simulations and NMR paramagnetic relaxation rate enhancement
    • M.L. DeMarco, R.J. Woods, J.H. Prestegard, and F. Tian Presentation of membrane-anchored glycosphingolipids determined from molecular dynamics simulations and NMR paramagnetic relaxation rate enhancement J. Am. Chem. Soc. 132 2010 1334 1338
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1334-1338
    • Demarco, M.L.1    Woods, R.J.2    Prestegard, J.H.3    Tian, F.4
  • 203
    • 67749122326 scopus 로고    scopus 로고
    • Determining the effects of lipophilic drugs on membrane structure by solid-state NMR spectroscopy: The case of the antioxidant curcumin
    • J. Barry, M. Fritz, J.R. Brender, P.E.S. Smith, D.-K. Lee, and A. Ramamoorthy Determining the effects of lipophilic drugs on membrane structure by solid-state NMR spectroscopy: the case of the antioxidant curcumin J. Am. Chem. Soc. 131 2009 4490 4498
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4490-4498
    • Barry, J.1    Fritz, M.2    Brender, J.R.3    Smith, P.E.S.4    Lee, D.-K.5    Ramamoorthy, A.6
  • 204
    • 0031993272 scopus 로고    scopus 로고
    • Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach toward Biomembrane Studies
    • C. Glaubitz, and A. Watts Magic angle-oriented sample spinning (MAOSS): a new approach toward biomembrane studies J. Magn. Reson. 130 1998 305 316 (Pubitemid 128451243)
    • (1998) Journal of Magnetic Resonance , vol.130 , Issue.2 , pp. 305-316
    • Glaubitz, C.1    Watts, A.2
  • 205
    • 0037138669 scopus 로고    scopus 로고
    • Bilayer sample for fast or slow magic angle oriented sample spinning solid-state NMR spectroscopy
    • DOI 10.1021/ja016571o
    • C. Sizun, and B. Bechinger Bilayer sample for fast or slow magic angle oriented sample spinning solid-state NMR spectroscopy J. Am. Chem. Soc. 124 2002 1146 1147 (Pubitemid 34169103)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.7 , pp. 1146-1147
    • Sizun, C.1    Bechinger, B.2
  • 206
    • 0032739155 scopus 로고    scopus 로고
    • Sign determination of dipolar couplings in field-oriented bicelles by variable angle sample spinning (VASS)
    • F. Tian, J.A. Losonczi, M.W.F. Fischer, and J.H. Prestegard Sign determination of dipolar couplings in field-oriented bicelles by variable angle sample spinning (VASS) J. Biomol. NMR 15 1999 145 150
    • (1999) J. Biomol. NMR , vol.15 , pp. 145-150
    • Tian, F.1    Losonczi, J.A.2    Fischer, M.W.F.3    Prestegard, J.H.4
  • 207
    • 0035819588 scopus 로고    scopus 로고
    • Manipulation of the director in bicellar mesophases by sample spinning: A new tool for NMR spectroscopy
    • DOI 10.1021/ja0019326
    • G. Zandomeneghi, M. Tomaselli, J.D. van Beek, and B.H. Meier Manipulation of the director in bicellar mesophases by sample spinning: a new tool for NMR spectroscopy J. Am. Chem. Soc. 123 2001 910 913 (Pubitemid 32151369)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.5 , pp. 910-913
    • Zandomeneghi, G.1    Tomaselli, M.2    Van Beek, J.D.3    Meier, B.H.4
  • 208
    • 0037328276 scopus 로고    scopus 로고
    • NMR of bicelles: Orientation and mosaic spread of the liquid-crystal director under sample rotation
    • DOI 10.1023/A:1022236217018
    • G. Zandomeneghi, M. Tomaselli, P.T.F. Williamson, and B.H. Meier NMR of bicelles: orientation and mosaic spread of the liquid-crystal director under sample rotation J. Biomol. NMR 25 2003 113 123 (Pubitemid 36267002)
    • (2003) Journal of Biomolecular NMR , vol.25 , Issue.2 , pp. 113-123
    • Zandomeneghi, G.1    Tomaselli, M.2    Williamson, P.T.F.3    Meier, B.H.4
  • 209
    • 0037135936 scopus 로고    scopus 로고
    • 1H-NMR in biological membranes: Magic angle spinning of bicelles
    • DOI 10.1016/S0005-2736(02)00446-7, PII S0005273602004467
    • C. Carlotti, F. Aussenac, and E.J. Dufourc Towards high-resolution H-1-NMR in biological membranes: magic angle spinning of bicelles Biochim. Biophys. Acta 1564 2002 156 164 (Pubitemid 34717881)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1564 , Issue.1 , pp. 156-164
    • Carlotti, C.1    Aussenac, F.2    Dufourc, E.J.3
  • 210
    • 0042494538 scopus 로고    scopus 로고
    • 15N chemical shift anisotropy in a protein dissolved in a dilute liquid crystalline medium with the application of magic angle sample spinning
    • 15N chemical shift anisotropy in a protein dissolved in a dilute liquid crystalline medium with the application of magic angle sample spinning J. Magn. Reson. 163 2003 163 173
    • (2003) J. Magn. Reson. , vol.163 , pp. 163-173
    • Kurita, J.1    Shimahara, H.2    Utsunomiya-Tate, N.3    Tate, S.4
  • 211
    • 29744447234 scopus 로고    scopus 로고
    • Structural and dynamic studies of the γ-M4 trans-membrane domain of the nicotinic acetylcholine receptor
    • DOI 10.1080/09687860500370653
    • P.T.F. Williamson, G. Zandomeneghi, F.J. Barrantes, A. Watts, and B.H. Meier Structural and dynamic studies of the γ-M4 trans-membrane domain of the nicotinic acetylcholine receptor Mol. Membr. Biol. 22 2005 485 496 (Pubitemid 43030904)
    • (2005) Molecular Membrane Biology , vol.22 , Issue.6 , pp. 485-496
    • Williamson, P.T.F.1    Zandomeneghi, G.2    Barrantes, F.J.3    Watts, A.4    Meier, B.H.5
  • 213
    • 37349050604 scopus 로고    scopus 로고
    • Dynamic behavior of tea catechins interacting with lipid membranes as determined by NMR spectroscopy
    • DOI 10.1021/jf0712402
    • Y. Uekusa, M. Kamihira, and T. Nakayama Dynamic behavior of tea catechins interacting with lipid membranes as determined by NMR spectroscopy J. Agric. Food Chem. 55 2007 9986 9992 (Pubitemid 350305186)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.24 , pp. 9986-9992
    • Uekusa, Y.1    Kamihira, M.2    Nakayama, T.3
  • 214
    • 33745143943 scopus 로고    scopus 로고
    • Detailed description of the conformation and location of membrane-bound erythromycin A using isotropic bicelles
    • DOI 10.1021/jm051210v
    • N. Matsumori, A. Morooka, and M. Murata Detailed description of the conformation and location of membrane-bound erythromycin A using isotropic bicelles J. Med. Chem. 49 2006 3501 3508 (Pubitemid 43902457)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.12 , pp. 3501-3508
    • Matsumori, N.1    Morooka, A.2    Murata, M.3
  • 215
    • 36849015957 scopus 로고    scopus 로고
    • Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles
    • DOI 10.1021/ja075024l
    • N. Matsumori, A. Morooka, and M. Murata Conformation and location of membrane-bound salinomycin-sodium complex deduced from NMR in isotropic bicelles J. Am. Chem. Soc. 129 2007 14989 14995 (Pubitemid 350230721)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.48 , pp. 14989-14995
    • Matsumori, N.1    Morooka, A.2    Murata, M.3
  • 216
    • 55449119778 scopus 로고    scopus 로고
    • Structure of membrane-bound amphidinol 3 in isotropic small bicelles
    • T. Houdai, N. Matsumori, and M. Murata Structure of membrane-bound amphidinol 3 in isotropic small bicelles Org. Lett. 10 2008 4191 4194
    • (2008) Org. Lett. , vol.10 , pp. 4191-4194
    • Houdai, T.1    Matsumori, N.2    Murata, M.3
  • 217
    • 77957144293 scopus 로고    scopus 로고
    • 3D structures of membrane-associated small molecules as determined in isotropic bicelles
    • N. Matsumori, and M. Murata 3D structures of membrane-associated small molecules as determined in isotropic bicelles Nat. Prod. Rep. 27 2010 1480 1492
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 1480-1492
    • Matsumori, N.1    Murata, M.2
  • 218
    • 80052272963 scopus 로고
    • Structural characterization of the interaction of the polyene antibiotic amphotericin B with DODAB bicelles and vesicles
    • T.R. Oliveira, C.R. Benatti, and M.T. Lamy Structural characterization of the interaction of the polyene antibiotic amphotericin B with DODAB bicelles and vesicles Biochim. Biophys. Acta 2011 1808 2629 2637
    • (1808) Biochim. Biophys. Acta , vol.2011 , pp. 2629-2637
    • Oliveira, T.R.1    Benatti, C.R.2    Lamy, M.T.3
  • 219
    • 18144388309 scopus 로고    scopus 로고
    • Lipid-ethanol interaction studied by NMR on bicelles
    • DOI 10.1021/jp044980b
    • B.W. Koenig, and K. Gawrisch Lipid-ethanol interaction studied by NMR on bicelles J. Phys. Chem. B 109 2005 7540 7547 (Pubitemid 40609890)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.15 , pp. 7540-7547
    • Koenig, B.W.1    Gawrisch, K.2
  • 221
    • 2342557924 scopus 로고    scopus 로고
    • Investigating fatty acids inserted into magnetically aligned phospholipid bilayers using EPR and solid-state NMR spectroscopy
    • N.A. Nusair, E.K. Tiburu, P.C. Dave, and G.A. Lorigan Investigating fatty acids inserted into magnetically aligned phospholipid bilayers using EPR and solid-state NMR spectroscopy J. Magn. Reson. 168 2004 228 237
    • (2004) J. Magn. Reson. , vol.168 , pp. 228-237
    • Nusair, N.A.1    Tiburu, E.K.2    Dave, P.C.3    Lorigan, G.A.4
  • 222
    • 56249123302 scopus 로고    scopus 로고
    • Magnetically aligned bicelles to study the orientation of lipophilic ligands in membrane bilayers
    • J. Guo, D.-P. Yang, R. Chari, X. Tian, S. Pavlopoulos, D. Lu, and A. Makriyannis Magnetically aligned bicelles to study the orientation of lipophilic ligands in membrane bilayers J. Med. Chem. 51 2008 6793 6799
    • (2008) J. Med. Chem. , vol.51 , pp. 6793-6799
    • Guo, J.1    Yang, D.-P.2    Chari, R.3    Tian, X.4    Pavlopoulos, S.5    Lu, D.6    Makriyannis, A.7
  • 225
    • 6444238696 scopus 로고    scopus 로고
    • Glycosidic torsional motions in a bicelle-associated disaccharide from residual dipolar couplings
    • DOI 10.1021/ja045697t
    • X. Yi, A. Venot, J. Glushka, and J.H. Prestegard Glycosidic torsional motions in a bicelle-associated disaccharide from residual dipolar couplings J. Am. Chem. Soc. 126 2004 13636 13638 (Pubitemid 39407241)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.42 , pp. 13636-13638
    • Yi, X.1    Venot, A.2    Glushka, J.3    Prestegard, J.H.4
  • 226
    • 39149084199 scopus 로고    scopus 로고
    • Solid-state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers
    • K. Kajiya, S. Kumazawa, A. Naito, and T. Nakayama Solid-state NMR analysis of the orientation and dynamics of epigallocatechin gallate, a green tea polyphenol, incorporated into lipid bilayers Magn. Reson. Chem. 46 2008 174 177
    • (2008) Magn. Reson. Chem. , vol.46 , pp. 174-177
    • Kajiya, K.1    Kumazawa, S.2    Naito, A.3    Nakayama, T.4
  • 227
    • 80053990322 scopus 로고    scopus 로고
    • Monomeric fullerenes in lipid membranes: Effect of molecular shape and polarity
    • M. Bortolus, G. Parisio, A.L. Maniero, and A. Ferrarini Monomeric fullerenes in lipid membranes: effect of molecular shape and polarity Langmuir 27 2011 12560 12568
    • (2011) Langmuir , vol.27 , pp. 12560-12568
    • Bortolus, M.1    Parisio, G.2    Maniero, A.L.3    Ferrarini, A.4
  • 228
    • 41549150245 scopus 로고    scopus 로고
    • Profiling drug membrane permeability and activity via biopartitioning chromatography
    • DOI 10.2174/138920008783571800
    • J. Sun, X. Wu, J. Liu, Y. Wang, and Z. He Profiling drug membrane permeability and activity via biopartitioning chromatography Curr. Drug Metab. 9 2008 152 166 (Pubitemid 351461004)
    • (2008) Current Drug Metabolism , vol.9 , Issue.2 , pp. 152-166
    • Sun, J.1    Wu, X.2    Lu, R.3    Liu, J.4    Wang, Y.5    He, Z.6
  • 229
    • 11144334238 scopus 로고    scopus 로고
    • Development and initial evaluation of PEG-stabilized bilayer disks as novel model membranes
    • DOI 10.1016/j.bpc.2004.09.006, PII S0301462204002455
    • E. Johannson, C. Engvall, M. Arfvidsson, P. Lundahl, and K. Edwards Development and initial evaluation of PEG-stabilized bilayer disks as novel model membranes Biophys. Chem. 113 2005 183 192 (Pubitemid 40029734)
    • (2005) Biophysical Chemistry , vol.113 , Issue.2 , pp. 183-192
    • Johansson, E.1    Engvall, C.2    Arfvidsson, M.3    Lundahl, P.4    Edwards, K.5
  • 230
    • 34249070809 scopus 로고    scopus 로고
    • Nanosized bilayer disks: Attractive model membranes for drug partition studies
    • DOI 10.1016/j.bbamem.2007.03.006, PII S000527360700079X
    • E. Johansson, A. Lundquist, S. Zuo, and K. Edwards Nanosized bilayer disks: attractive model membranes for drug partition studies Biochim. Biophys. Acta 1768 2007 1518 1525 (Pubitemid 46782710)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.6 , pp. 1518-1525
    • Johansson, E.1    Lundquist, A.2    Zuo, S.3    Edwards, K.4
  • 231
    • 34147161604 scopus 로고    scopus 로고
    • Evaluation of bilayer disks as plant cell membrane models in partition studies
    • DOI 10.1016/j.ab.2007.02.012, PII S0003269707000991
    • E. Boija, A. Lundquist, K. Edwards, and G. Johansson Evaluation of bilayer disks as plant cell membrane models in partition studies Anal. Biochem. 364 2007 145 152 (Pubitemid 46559918)
    • (2007) Analytical Biochemistry , vol.364 , Issue.2 , pp. 145-152
    • Boija, E.1    Lundquist, A.2    Edwards, K.3    Johansson, G.4
  • 232
    • 50949114480 scopus 로고    scopus 로고
    • Bilayer disk capillary electrophoresis: A novel method to study drug partitioning into membranes
    • E. Boija, A. Lundquist, M. Nilsson, K. Edwards, R. Isaksson, and G. Johansson Bilayer disk capillary electrophoresis: a novel method to study drug partitioning into membranes Electrophoresis 29 2008 3377 3383
    • (2008) Electrophoresis , vol.29 , pp. 3377-3383
    • Boija, E.1    Lundquist, A.2    Nilsson, M.3    Edwards, K.4    Isaksson, R.5    Johansson, G.6
  • 233
    • 79955691446 scopus 로고    scopus 로고
    • Polyethylene glycol-stabilized lipid disks as model membranes in interaction studies based on electrokinetic capillary chromatography and quartz crystal microbalance
    • K. Vainikka, K. Reijmar, G. Yohannes, J. Samuelsson, K. Edwards, M. Jussila, and M.-L. Riekkola Polyethylene glycol-stabilized lipid disks as model membranes in interaction studies based on electrokinetic capillary chromatography and quartz crystal microbalance Anal. Biochem. 414 2011 117 124
    • (2011) Anal. Biochem. , vol.414 , pp. 117-124
    • Vainikka, K.1    Reijmar, K.2    Yohannes, G.3    Samuelsson, J.4    Edwards, K.5    Jussila, M.6    Riekkola, M.-L.7
  • 235
    • 1542285304 scopus 로고    scopus 로고
    • 1H NMR Investigation of the Conformation of Methionine-Enkephalin in Fast-Tumbling Bicelles
    • 1H NMR investigation of methionine-enkephalin in fast-tumbling bicelles Biophys. J. 86 2004 1587 1600 (Pubitemid 38295592)
    • (2004) Biophysical Journal , vol.86 , Issue.3 , pp. 1587-1600
    • Marcotte, I.1    Separovic, F.2    Auger, M.3    Gagne, S.M.4
  • 236
    • 84869166856 scopus 로고    scopus 로고
    • The magic of bicelles lights up membrane protein structure
    • U.H.N. Dürr, M. Gildenberg, and A. Ramamoorthy The magic of bicelles lights up membrane protein structure Chem. Rev. 112 2012 6054 6074
    • (2012) Chem. Rev. , vol.112 , pp. 6054-6074
    • Dürr, U.H.N.1    Gildenberg, M.2    Ramamoorthy, A.3
  • 237
    • 84855649990 scopus 로고    scopus 로고
    • Q-Titration' of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
    • W.S. Son, S.H. Park, H.J. Nothnagel, G.J. Lu, Y. Wang, H. Zhang, G.A. Cook, S.C. Howell, and S.J. Opella 'q-Titration' of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy J. Magn. Reson. 214 2012 111 118
    • (2012) J. Magn. Reson. , vol.214 , pp. 111-118
    • Son, W.S.1    Park, S.H.2    Nothnagel, H.J.3    Lu, G.J.4    Wang, Y.5    Zhang, H.6    Cook, G.A.7    Howell, S.C.8    Opella, S.J.9
  • 241
    • 81355146334 scopus 로고    scopus 로고
    • Interactions of interleukin-8 with the human chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy
    • S.H. Park, F. Casagrande, L. Cho, L. Albrecht, and S.J. Opella Interactions of interleukin-8 with the human chemokine receptor CXCR1 in phospholipid bilayers by NMR spectroscopy J. Mol. Biol. 414 2011 194 203
    • (2011) J. Mol. Biol. , vol.414 , pp. 194-203
    • Park, S.H.1    Casagrande, F.2    Cho, L.3    Albrecht, L.4    Opella, S.J.5
  • 242
    • 45749128574 scopus 로고    scopus 로고
    • Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-state NMR
    • DOI 10.1021/bi800362b
    • R. Mahalakshmi, and F.M. Marassi Orientation of the Escherichia coli outer membrane protein OmpX in phospholipid bilayer membranes determined by solid-state NMR Biochemistry 47 2008 6531 6538 (Pubitemid 351874280)
    • (2008) Biochemistry , vol.47 , Issue.25 , pp. 6531-6538
    • Mahalakshmi, R.1    Marassi, F.M.2
  • 243
    • 74249122726 scopus 로고    scopus 로고
    • Anesthetic effects on the structure and dynamics of the second transmembrane domains of nAChR α4β2
    • T.X. Cui, C.G. Canlas, Y. Xu, and P. Tang Anesthetic effects on the structure and dynamics of the second transmembrane domains of nAChR α4β2 Biochim. Biophys. Acta 1798 2010 161 166
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 161-166
    • Cui, T.X.1    Canlas, C.G.2    Xu, Y.3    Tang, P.4
  • 244
    • 78650269727 scopus 로고
    • Comparative NMR studies demonstrate profound differences between two viroporins: P7 of HCV and Vpu of HIV-1
    • G.A. Cook, H. Zhang, S.H. Park, Y. Wang, and S.J. Opella Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1 Biochim. Biophys. Acta 2011 1808 554 560
    • (1808) Biochim. Biophys. Acta , vol.2011 , pp. 554-560
    • Cook, G.A.1    Zhang, H.2    Park, S.H.3    Wang, Y.4    Opella, S.J.5
  • 245
    • 33748775215 scopus 로고    scopus 로고
    • Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy
    • DOI 10.1021/ja063640w
    • A.A. de Angelis, S.C. Howell, A.A. Nevzorov, and S.J. Opella Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy J. Am. Chem. Soc. 128 2006 12256 12267 (Pubitemid 44413857)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.37 , pp. 12256-12267
    • De Angelis, A.A.1    Howell, S.C.2    Nevzorov, A.A.3    Opella, S.J.4
  • 247
    • 78449242888 scopus 로고    scopus 로고
    • d of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy
    • d of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy J. Am. Chem. Soc. 132 2010 15945 15956
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15945-15956
    • Walther, T.H.1    Grage, S.L.2    Roth, N.3    Ulrich, A.S.4
  • 248
    • 77956582409 scopus 로고    scopus 로고
    • Structure and dynamics of the membrane-bound form of Pf1 coat protein: Implications of structural rearrangement for virus assembly
    • S.H. Park, F.M. Marassi, D. Black, and S.J. Opella Structure and dynamics of the membrane-bound form of Pf1 coat protein: implications of structural rearrangement for virus assembly Biophys. J. 99 2010 1465 1474
    • (2010) Biophys. J. , vol.99 , pp. 1465-1474
    • Park, S.H.1    Marassi, F.M.2    Black, D.3    Opella, S.J.4
  • 250
    • 36849051197 scopus 로고    scopus 로고
    • 5 and their reductases-Promising targets for structural studies by advanced solid-state NMR spectroscopy
    • DOI 10.1016/j.bbamem.2007.08.007, PII S0005273607002945
    • 5 and their reductases - Promising targets for structural studies by advanced solid-state NMR spectroscopy Biochim. Biophys. Acta 1768 2007 3235 3259 (Pubitemid 350236080)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.12 , pp. 3235-3259
    • Durr, U.H.N.1    Waskell, L.2    Ramamoorthy, A.3
  • 253
    • 77955788885 scopus 로고    scopus 로고
    • INEPT-based separated-local-field NMR spectroscopy: A unique approach to elucidate side-chain dynamics of membrane-associated proteins
    • J.D. Xu, R. Soong, S.-C. Im, L. Waskell, and A. Ramamoorthy INEPT-based separated-local-field NMR spectroscopy: a unique approach to elucidate side-chain dynamics of membrane-associated proteins J. Am. Chem. Soc. 132 2010 9944 9947
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9944-9947
    • Xu, J.D.1    Soong, R.2    Im, S.-C.3    Waskell, L.4    Ramamoorthy, A.5
  • 255
    • 0000961515 scopus 로고    scopus 로고
    • Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution
    • G. Wider Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution Prog. Nucl. Magn. Reson. Spectrosc. 32 1998 193 275
    • (1998) Prog. Nucl. Magn. Reson. Spectrosc. , vol.32 , pp. 193-275
    • Wider, G.1
  • 256
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • PII S0079656598000259
    • M. Sattler, J. Schleucher, and C. Griesinger Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients Prog. Nucl. Magn. Reson. Spectrosc. 34 1999 93 158 (Pubitemid 129595216)
    • (1999) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.34 , Issue.2 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 260
    • 33847678076 scopus 로고    scopus 로고
    • Isotropic bicelles stabilize the functional form of a small multidrug-resistance pump for NMR structural studies
    • DOI 10.1021/ja0679836
    • S.F. Poget, S.M. Cahill, and M.E. Girvin Isotropic bicelles stabilize the functional form of a small multidrug-resistance pump for NMR structural studies J. Am. Chem. Soc. 129 2007 2432 2433 (Pubitemid 46364038)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.9 , pp. 2432-2433
    • Poget, S.F.1    Cahill, S.M.2    Girvin, M.E.3
  • 261
    • 36849088540 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better
    • DOI 10.1016/j.bbamem.2007.09.006, PII S0005273607003495
    • S.F. Poget, and M.E. Girvin Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better Biochim. Biophys. Acta 1768 2007 3098 3106 (Pubitemid 350236093)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.12 , pp. 3098-3106
    • Poget, S.F.1    Girvin, M.E.2
  • 262
    • 77957966284 scopus 로고    scopus 로고
    • 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation
    • 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation Biomol. NMR Assign. 4 2010 139 142
    • (2010) Biomol. NMR Assign. , vol.4 , pp. 139-142
    • Poget, S.F.1    Harris, R.2    Cahill, S.M.3    Girvin, M.E.4
  • 263
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • DOI 10.1016/j.bbamem.2004.04.011, PII S0005273604001610, Lipid-Protein Interactions
    • A.M. Seddon, P. Curnow, and P.J. Booth Membrane proteins, lipids and detergents: not just a soap opera Biochim. Biophys. Acta 1666 2004 105 117 (Pubitemid 39425201)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1666 , Issue.1-2 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 264
    • 49749095639 scopus 로고    scopus 로고
    • Lipids and membrane protein structures
    • C. Hunte, and S. Richers Lipids and membrane protein structures Curr. Opin. Struct. Biol. 18 2008 406 411
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 406-411
    • Hunte, C.1    Richers, S.2
  • 265
    • 41949140686 scopus 로고    scopus 로고
    • NMR of membrane-associated peptides and proteins
    • G. Wang NMR of membrane-associated peptides and proteins Curr. Prot. Pept. Sci. 9 2008 50 69
    • (2008) Curr. Prot. Pept. Sci. , vol.9 , pp. 50-69
    • Wang, G.1
  • 266
    • 77955981439 scopus 로고    scopus 로고
    • Nonmicellar systems for solution NMR spectroscopy of membrane proteins
    • T. Raschle, S. Hiller, M. Etzkorn, and G. Wagner Nonmicellar systems for solution NMR spectroscopy of membrane proteins Curr. Opin. Struct. Biol. 20 2010 471 479
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 471-479
    • Raschle, T.1    Hiller, S.2    Etzkorn, M.3    Wagner, G.4
  • 267
    • 70349745154 scopus 로고    scopus 로고
    • Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins
    • H.J. Kim, S.C. Howell, W.D. Van Horn, Y.H. Jeon, and C.R. Sanders Recent advances in the application of solution NMR spectroscopy to multi-span integral membrane proteins Prog. Nucl. Magn. Reson. Spectrosc. 55 2009 335 360
    • (2009) Prog. Nucl. Magn. Reson. Spectrosc. , vol.55 , pp. 335-360
    • Kim, H.J.1    Howell, S.C.2    Van Horn, W.D.3    Jeon, Y.H.4    Sanders, C.R.5
  • 268
    • 84859899405 scopus 로고    scopus 로고
    • Contemporary methods in structure determination of membrane proteins by solution NMR
    • T. Qureshi, and N.K. Goto Contemporary methods in structure determination of membrane proteins by solution NMR Top. Curr. Chem. 326 2012 123 185
    • (2012) Top. Curr. Chem. , vol.326 , pp. 123-185
    • Qureshi, T.1    Goto, N.K.2
  • 269
    • 77953286311 scopus 로고    scopus 로고
    • Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy
    • A. Gautier, H.R. Mott, M.J. Bostock, J.P. Kirkpatrick, and D. Nietlispach Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy Nat. Struct. Biol. 17 2010 768 774
    • (2010) Nat. Struct. Biol. , vol.17 , pp. 768-774
    • Gautier, A.1    Mott, H.R.2    Bostock, M.J.3    Kirkpatrick, J.P.4    Nietlispach, D.5
  • 271
    • 81855226606 scopus 로고    scopus 로고
    • Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin
    • G. Xie, A.M. D'Antona, P.C. Edwards, M. Fransen, J. Standfuss, G.F.X. Schertler, and D.D. Oprian Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin Biochemistry 50 2011 10399 10407
    • (2011) Biochemistry , vol.50 , pp. 10399-10407
    • Xie, G.1    D'Antona, A.M.2    Edwards, P.C.3    Fransen, M.4    Standfuss, J.5    Schertler, G.F.X.6    Oprian, D.D.7
  • 272
  • 273
    • 84855774075 scopus 로고
    • Reconstitution of integral membrane proteins into isotropic bicelles with improved sample stability and expanded lipid composition profile
    • E.A. Morrison, and K.A. Henzler-Wildman Reconstitution of integral membrane proteins into isotropic bicelles with improved sample stability and expanded lipid composition profile Biochim. Biophys. Acta 2012 1818 814 820
    • (1818) Biochim. Biophys. Acta , vol.2012 , pp. 814-820
    • Morrison, E.A.1    Henzler-Wildman, K.A.2
  • 276
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin αiIbβ3 transmembrane complex explains integrin transmembrane signalling
    • T.-L. Lau, C. Kim, M.H. Ginsberg, and T.S. Ulmer The structure of the integrin αIIbβ3 transmembrane complex explains integrin transmembrane signalling EMBO J. 28 2009 1351 1361
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.-L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 279
    • 81855192140 scopus 로고
    • Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy
    • M. Gustavsson, N.J. Traaseth, and G. Veglia Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy Biochim. Biophys. Acta 2012 1818 146 153
    • (1818) Biochim. Biophys. Acta , vol.2012 , pp. 146-153
    • Gustavsson, M.1    Traaseth, N.J.2    Veglia, G.3
  • 280
    • 4344648452 scopus 로고    scopus 로고
    • Residual dipolar couplings in structure determination of biomolecules
    • J.H. Prestegard, C.M. Bougault, and A.I. Kishore Residual dipolar couplings in structure determination of biomolecules Chem. Rev. 104 2004 3519 3540
    • (2004) Chem. Rev. , vol.104 , pp. 3519-3540
    • Prestegard, J.H.1    Bougault, C.M.2    Kishore, A.I.3
  • 281
    • 33646931175 scopus 로고    scopus 로고
    • NMR residual dipolar couplings as probes of biomolecular dynamics
    • DOI 10.1021/cr040429z
    • J.R. Tolman, and K. Ruan NMR residual dipolar couplings as probes of biomolecular dynamics Chem. Rev. 106 2006 1720 1736 (Pubitemid 43792777)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1720-1736
    • Tolman, J.R.1    Ruan, K.2
  • 282
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR [11]
    • DOI 10.1021/ja0000908
    • M. Zweckstetter, and A. Bax Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR J. Am. Chem. Soc. 122 2000 3791 3792 (Pubitemid 30233459)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.15 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 283
    • 2942653357 scopus 로고    scopus 로고
    • Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases
    • DOI 10.1529/biophysj.103.035790
    • M. Zweckstetter, G. Hummer, and A. Bax Prediction of charge-induced molecular alignment of biomolecules dissolved in liquid-crystalline phases Biophys. J. 86 2004 3444 3460 (Pubitemid 38780229)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3444-3460
    • Zweckstetter, M.1    Hummer, G.2    Bax, A.3
  • 284
    • 42149130389 scopus 로고    scopus 로고
    • NMR: Prediction of molecular alignment from structure using the PALES software
    • DOI 10.1038/nprot.2008.36, PII NPROT.2008.36
    • M. Zweckstetter NMR: prediction of molecular alignment from structure using the PALES software Nat. Prot. 3 2008 679 690 (Pubitemid 351522648)
    • (2008) Nature Protocols , vol.3 , Issue.4 , pp. 679-690
    • Zweckstetter, M.1
  • 285
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • DOI 10.1126/science.278.5340.1111
    • N. Tjandra, and A. Bax Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science 278 1997 1111 1114 (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 286
    • 34748876721 scopus 로고    scopus 로고
    • Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings
    • G. Bouvignies, P.R.L. Markwick, and M. Blackledge Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings ChemPhysChem 8 2007 1901 1909
    • (2007) ChemPhysChem , vol.8 , pp. 1901-1909
    • Bouvignies, G.1    Markwick, P.R.L.2    Blackledge, M.3
  • 287
    • 34547820982 scopus 로고    scopus 로고
    • NMR studies of RNA dynamics and structural plasticity using NMR residual diopolar couplings
    • DOI 10.1002/bip.20765
    • M. Getz, X. Sun, A. Casiano-Negroni, Q. Zhang, and H.M. Al-Hashimi NMR studies of RNA dynamics and structural plasticity using NMR residual dipolar couplings Biopolymers 86 2007 384 402 (Pubitemid 47237806)
    • (2007) Biopolymers , vol.86 , Issue.5-6 , pp. 384-402
    • Getz, M.1    Sun, X.2    Casiano-Negroni, A.3    Zhang, Q.4    Al-Hashimi, H.M.5
  • 289
    • 0033551495 scopus 로고    scopus 로고
    • Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
    • M.W.F. Fischer, J.A. Losonczi, J.L. Weaver, and J.H. Prestegard Domain orientation and dynamics in multidomain proteins from residual dipolar couplings Biochemistry 38 1999 9013 9022
    • (1999) Biochemistry , vol.38 , pp. 9013-9022
    • Fischer, M.W.F.1    Losonczi, J.A.2    Weaver, J.L.3    Prestegard, J.H.4
  • 290
    • 80053025476 scopus 로고    scopus 로고
    • Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings
    • M. Maciejewski, N. Tjandra, and P.N. Barlow Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings Biochemistry 50 2011 8138 8149
    • (2011) Biochemistry , vol.50 , pp. 8138-8149
    • Maciejewski, M.1    Tjandra, N.2    Barlow, P.N.3
  • 292
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • DOI 10.1021/ja017875d
    • J.J. Chou, J.D. Kaufmann, S.J. Stahl, P.T. Wingfield, and A. Bax Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement on stretched polyacrylamide gel J. Am. Chem. Soc. 124 2002 2450 2451 (Pubitemid 34251754)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.11 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 293
    • 45149147257 scopus 로고    scopus 로고
    • Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins
    • DOI 10.1021/ja801729f
    • J. Lorieau, L. Yao, and A. Bax Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins J. Am. Chem. Soc. 130 2008 7536 7537 (Pubitemid 351842104)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.24 , pp. 7536-7537
    • Lorieau, J.1    Yao, L.2    Bax, A.3
  • 294
    • 58149177285 scopus 로고    scopus 로고
    • Structure and membrane interaction of myristoylated ARF1
    • Y. Liu, R.A. Kahn, and J.H. Prestegard Structure and membrane interaction of myristoylated ARF1 Structure 17 2009 79 87
    • (2009) Structure , vol.17 , pp. 79-87
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 296
    • 0036918932 scopus 로고    scopus 로고
    • Bicelles in structure-function studies of membrane-associated proteins
    • DOI 10.1016/S0045-2068(02)00527-8
    • J.A. Whiles, R. Deems, R.R. Vold, and E.A. Dennis Bicelles in structure-function studies of membrane-associated proteins Bioorg. Chem. 30 2002 431 442 (Pubitemid 36294219)
    • (2002) Bioorganic Chemistry , vol.30 , Issue.6 , pp. 431-442
    • Whiles, J.A.1    Deems, R.2    Vold, R.R.3    Dennis, E.A.4
  • 297
    • 33644958800 scopus 로고    scopus 로고
    • Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions
    • T. Lührs, R. Zahn, and K. Wüthrich Amyloid formation by recombinant full-length prion proteins in phospholipid bicelle solutions J. Mol. Biol. 357 2006 833 841
    • (2006) J. Mol. Biol. , vol.357 , pp. 833-841
    • Lührs, T.1    Zahn, R.2    Wüthrich, K.3
  • 298
    • 77954729517 scopus 로고    scopus 로고
    • Lipid domains in bicelles containing unsaturated lipids and cholesterol
    • H.S. Cho, J.L. Dominick, and M.M. Spence Lipid domains in bicelles containing unsaturated lipids and cholesterol J. Phys. Chem. B 114 2010 9238 9245
    • (2010) J. Phys. Chem. B , vol.114 , pp. 9238-9245
    • Cho, H.S.1    Dominick, J.L.2    Spence, M.M.3
  • 299
    • 79953695955 scopus 로고    scopus 로고
    • Synthesis of organic-inorganic hybrid bicelles - Lipid bilayer nanodiscs encompassed by siloxane surfaces
    • K. Yasuhara, S. Miki, H. Nakazono, A. Ohta, and J.-I. Kikuchi Synthesis of organic-inorganic hybrid bicelles - lipid bilayer nanodiscs encompassed by siloxane surfaces Chem. Commun. 47 2011 4691 4693
    • (2011) Chem. Commun. , vol.47 , pp. 4691-4693
    • Yasuhara, K.1    Miki, S.2    Nakazono, H.3    Ohta, A.4    Kikuchi, J.-I.5
  • 302
    • 84856192298 scopus 로고    scopus 로고
    • Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit fold similar to the protein in the cell membrane
    • E.M. Uhlemann, H.E. Pierson, R.H. Fillingame, and O.Y. Dmitriev Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit fold similar to the protein in the cell membrane Prot. Sci. 21 2012 279 288
    • (2012) Prot. Sci. , vol.21 , pp. 279-288
    • Uhlemann, E.M.1    Pierson, H.E.2    Fillingame, R.H.3    Dmitriev, O.Y.4
  • 311
    • 75149195391 scopus 로고    scopus 로고
    • Functional delivery of a membrane protein into oocyte membranes using bicelles
    • C. Kang, C.G. Vanoye, R.C. Welch, W.D. Van Horn, and C.R. Sanders Functional delivery of a membrane protein into oocyte membranes using bicelles Biochemistry 49 2010 653 655
    • (2010) Biochemistry , vol.49 , pp. 653-655
    • Kang, C.1    Vanoye, C.G.2    Welch, R.C.3    Van Horn, W.D.4    Sanders, C.R.5
  • 312
    • 61849105337 scopus 로고    scopus 로고
    • Directed covalent asssembly of rigid organic nanodisks using self-assembled temporary scaffolds
    • S. Tekobo, and E. Pinkhassik Directed covalent asssembly of rigid organic nanodisks using self-assembled temporary scaffolds Chem. Commun. 2009 1112 1114
    • (2009) Chem. Commun. , pp. 1112-1114
    • Tekobo, S.1    Pinkhassik, E.2
  • 315
    • 69249216546 scopus 로고    scopus 로고
    • Self-assembly formation of multiple DNA-tethered lipid bilayers
    • S.R. Tabaei, P. Jönsson, M. Brändén, and F. Höök Self-assembly formation of multiple DNA-tethered lipid bilayers J. Struct. Biol. 168 2009 200 206
    • (2009) J. Struct. Biol. , vol.168 , pp. 200-206
    • Tabaei, S.R.1    Jönsson, P.2    Brändén, M.3    Höök, F.4
  • 317
    • 36549062001 scopus 로고    scopus 로고
    • Membrane lipid polymorphism: Relationship to bilayer properties and protein function
    • DOI 10.1385/1-59745-519-9:15, Methods in Membrane Lipids
    • R.M. Epand Membrane lipid polymorphism: relationship to bilayer properties and protein function Meth. Mol. Biol. 400 2007 15 26 (Pubitemid 350183680)
    • (2007) Methods in Molecular Biology , vol.400 , pp. 15-26
    • Epand, R.M.1
  • 318
    • 84864346743 scopus 로고    scopus 로고
    • Cholesterol increases the magnetic aligning of bicellar disks from an aqueous mixture of DMPC and DMPE-DTPA with complexed thulium ions
    • M. Liebi, J. Kohlbrecher, T. Ishikawa, P. Fischer, P. Walde, and E.J. Windhab Cholesterol increases the magnetic aligning of bicellar disks from an aqueous mixture of DMPC and DMPE-DTPA with complexed thulium ions Langmuir 28 2012 10905 10915
    • (2012) Langmuir , vol.28 , pp. 10905-10915
    • Liebi, M.1    Kohlbrecher, J.2    Ishikawa, T.3    Fischer, P.4    Walde, P.5    Windhab, E.J.6
  • 319
    • 84861401075 scopus 로고    scopus 로고
    • Effect of divalent cations on DMPC/DHPC bicelle formation and alignment
    • A.J. Brindley, and R.W. Martin Effect of divalent cations on DMPC/DHPC bicelle formation and alignment Langmuir 28 2012 7788 7796
    • (2012) Langmuir , vol.28 , pp. 7788-7796
    • Brindley, A.J.1    Martin, R.W.2
  • 320
    • 84864223306 scopus 로고    scopus 로고
    • Three-dimensional structure of glycolipids in biological membranes
    • M.L. DeMarco Three-dimensional structure of glycolipids in biological membranes Biochemistry 51 2012 5725 5732
    • (2012) Biochemistry , vol.51 , pp. 5725-5732
    • Demarco, M.L.1
  • 321
    • 0028767570 scopus 로고
    • NMR measurement of resolved heteronuclear dipole couplings in liquid crystals and lipids
    • K. Schmidt-Rohr, D. Nanz, L. Emsley, and A. Pines NMR measurement of resolved heteronuclear dipole couplings in liquid crystals and lipids J. Phys. Chem. 98 1994 6668 6670
    • (1994) J. Phys. Chem. , vol.98 , pp. 6668-6670
    • Schmidt-Rohr, K.1    Nanz, D.2    Emsley, L.3    Pines, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.