메뉴 건너뛰기




Volumn 49, Issue 43, 2010, Pages 9190-9198

Lipid-protein correlations in nanoscale phospholipid bilayers determined by solid-state nuclear magnetic resonance

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPATHIC; BILAYER FRAGMENTS; BIOPHYSICAL CHARACTERIZATION; CORRELATION SPECTRA; HELICAL PROTEINS; HETERONUCLEAR; LIPID PHASE TRANSITIONS; LIPID VESICLES; MEMBRANE PROTEINS; NANO SCALE; NANODISCS; PHOSPHOLIPID BILAYER; PROTEIN INTERFACES; PROTEIN PARTICLES; SCAFFOLDING PROTEINS; SOLID-STATE NUCLEAR MAGNETIC RESONANCE; STRUCTURAL STUDIES; TRANSVERSE RELAXATION;

EID: 78049311379     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1013722     Document Type: Article
Times cited : (27)

References (87)
  • 2
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • Shaw, A. W., Pureza, V. S., Sligar, S. G., and Morrissey, J. H. (2007) The local phospholipid environment modulates the activation of blood clotting J. Biol. Chem. 282, 6556-6563
    • (2007) J. Biol. Chem. , vol.282 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 3
    • 0032529219 scopus 로고    scopus 로고
    • Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid
    • Yun, C. H., Ahn, T., and Guengerich, F. P. (1998) Conformational change and activation of cytochrome P450 2B1 induced by salt and phospholipid Arch. Biochem. Biophys. 356, 229-238
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 229-238
    • Yun, C.H.1    Ahn, T.2    Guengerich, F.P.3
  • 4
    • 0346333300 scopus 로고    scopus 로고
    • Membrane properties induced by anionic phospholipids and phosphatidylethanolamine are critical for the membrane binding and catalytic activity of human cytochrome P450 3A4
    • Kim, K. H., Ahn, T., and Yun, C. H. (2003) Membrane properties induced by anionic phospholipids and phosphatidylethanolamine are critical for the membrane binding and catalytic activity of human cytochrome P450 3A4 Biochemistry 42, 15377-15387
    • (2003) Biochemistry , vol.42 , pp. 15377-15387
    • Kim, K.H.1    Ahn, T.2    Yun, C.H.3
  • 5
    • 0032530954 scopus 로고    scopus 로고
    • Membrane insertion of cytochrome P450 1A2 promoted by anionic phospholipids
    • Ahn, T., Guengerich, F. P., and Yun, C. H. (1998) Membrane insertion of cytochrome P450 1A2 promoted by anionic phospholipids Biochemistry 37, 12860-12866
    • (1998) Biochemistry , vol.37 , pp. 12860-12866
    • Ahn, T.1    Guengerich, F.P.2    Yun, C.H.3
  • 6
    • 67649306770 scopus 로고    scopus 로고
    • G-protein coupled receptors, cholesterol and palmitoylation: Facts about fats
    • Chini, B. and Parenti, M. (2009) G-protein coupled receptors, cholesterol and palmitoylation: Facts about fats J. Mol. Endocrinol. 42, 9
    • (2009) J. Mol. Endocrinol. , vol.42 , pp. 9
    • Chini, B.1    Parenti, M.2
  • 8
    • 60349118364 scopus 로고    scopus 로고
    • + channel subunits using a protein-lipid overlay assay
    • + channel subunits using a protein-lipid overlay assay Methods Mol. Biol. 491, 103-111
    • (2008) Methods Mol. Biol. , vol.491 , pp. 103-111
    • Thomas, A.M.1    Tinker, A.2
  • 9
    • 7244257317 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1
    • Mani, R., Buffy, J. J., Waring, A. J., Lehrer, R. I., and Hong, M. (2004) Solid-state NMR investigation of the selective disruption of lipid membranes by protegrin-1 Biochemistry 43, 13839-13848
    • (2004) Biochemistry , vol.43 , pp. 13839-13848
    • Mani, R.1    Buffy, J.J.2    Waring, A.J.3    Lehrer, R.I.4    Hong, M.5
  • 10
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • Matsuzaki, K., Murase, O., and Miyajima, K. (1995) Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers Biochemistry 34, 12553-12559
    • (1995) Biochemistry , vol.34 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 11
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner, E. J., Lewis, R. N., and McElhaney, R. N. (1999) The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes Biochim. Biophys. Acta 1462, 201-221
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.2    McElhaney, R.N.3
  • 13
    • 0032060715 scopus 로고    scopus 로고
    • On choosing a detergent for solution NMR studies of membrane proteins
    • Vinogradova, O., Sonnichsen, F., and Sanders, C. R. (1998) On choosing a detergent for solution NMR studies of membrane proteins J. Biomol. NMR 11, 381-386
    • (1998) J. Biomol. NMR , vol.11 , pp. 381-386
    • Vinogradova, O.1    Sonnichsen, F.2    Sanders, C.R.3
  • 15
    • 0032170742 scopus 로고    scopus 로고
    • Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer
    • Bayburt, T. H., Carlson, J. W., and Sligar, S. G. (1998) Reconstitution and imaging of a membrane protein in a nanometer-size phospholipid bilayer J. Struct. Biol. 123, 37-44
    • (1998) J. Struct. Biol. , vol.123 , pp. 37-44
    • Bayburt, T.H.1    Carlson, J.W.2    Sligar, S.G.3
  • 16
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt, T. H., Grinkova, Y. V., and Sligar, S. G. (2002) Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins Nano Lett. 2, 853-856
    • (2002) Nano Lett. , vol.2 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 17
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • Baas, B. J., Denisov, I. G., and Sligar, S. G. (2004) Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment Arch. Biochem. Biophys. 430, 218-228
    • (2004) Arch. Biochem. Biophys. , vol.430 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 18
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size
    • Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size J. Am. Chem. Soc. 126, 3477-3487
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 19
    • 0347985761 scopus 로고    scopus 로고
    • Phospholipid phase transitions in homogeneous nanometer scale bilayer discs
    • Shaw, A. W., McLean, M. A., and Sligar, S. G. (2004) Phospholipid phase transitions in homogeneous nanometer scale bilayer discs FEBS Lett. 556, 260-264
    • (2004) FEBS Lett. , vol.556 , pp. 260-264
    • Shaw, A.W.1    McLean, M.A.2    Sligar, S.G.3
  • 21
    • 33744928866 scopus 로고    scopus 로고
    • Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs
    • Bayburt, T. H., Grinkova, Y. V., and Sligar, S. G. (2006) Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs Arch. Biochem. Biophys. 450, 215-222
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 215-222
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 22
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath, A., Atkins, W. M., and Sligar, S. G. (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins Biochemistry 46, 2059-2069
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 23
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt, T. H., Leitz, A. J., Xie, G., Oprian, D. D., and Sligar, S. G. (2007) Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins J. Biol. Chem. 282, 14875-14881
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 24
    • 11244346546 scopus 로고    scopus 로고
    • Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins
    • Shih, A. Y., Denisov, I. G., Phillips, J. C., Sligar, S. G., and Schulten, K. (2005) Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins Biophys. J. 88, 548-556
    • (2005) Biophys. J. , vol.88 , pp. 548-556
    • Shih, A.Y.1    Denisov, I.G.2    Phillips, J.C.3    Sligar, S.G.4    Schulten, K.5
  • 26
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation
    • Denisov, I. G., Baas, B. J., Grinkova, Y. V., and Sligar, S. G. (2007) Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation J. Biol. Chem. 282, 7066-7076
    • (2007) J. Biol. Chem. , vol.282 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4
  • 27
    • 0042691480 scopus 로고    scopus 로고
    • Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers
    • Civjan, N. R., Bayburt, T. H., Schuler, M. A., and Sligar, S. G. (2003) Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers BioTechniques 35 (556-560) 562-553
    • (2003) BioTechniques , vol.35 , Issue.556-560 , pp. 562-553
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 28
    • 35349009104 scopus 로고    scopus 로고
    • Ligand binding to cytochrome P450 3A4 in phospholipid bilayer nanodiscs: The effect of model membranes
    • Nath, A., Grinkova, Y. V., Sligar, S. G., and Atkins, W. M. (2007) Ligand binding to cytochrome P450 3A4 in phospholipid bilayer nanodiscs: The effect of model membranes J. Biol. Chem. 282, 28309-28320
    • (2007) J. Biol. Chem. , vol.282 , pp. 28309-28320
    • Nath, A.1    Grinkova, Y.V.2    Sligar, S.G.3    Atkins, W.M.4
  • 29
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • Alami, M., Dalal, K., Lelj-Garolla, B., Sligar, S. G., and Duong, F. (2007) Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA EMBO J. 26, 1995-2004
    • (2007) EMBO J. , vol.26 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 30
    • 33745511381 scopus 로고    scopus 로고
    • Functional reconstitution of β2-adrenergic receptors utilizing self-assembling Nanodisc technology
    • Leitz, A. J., Bayburt, T. H., Barnakov, A. N., Springer, B. A., and Sligar, S. G. (2006) Functional reconstitution of β2-adrenergic receptors utilizing self-assembling Nanodisc technology BioTechniques 40, 601-612
    • (2006) BioTechniques , vol.40 , pp. 601-612
    • Leitz, A.J.1    Bayburt, T.H.2    Barnakov, A.N.3    Springer, B.A.4    Sligar, S.G.5
  • 31
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog, T., Grimme, S., Li, M., Sligar, S. G., and Hazelbauer, G. L. (2006) Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties Proc. Natl. Acad. Sci. U.S.A. 103, 11509-11514
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 32
    • 33751237696 scopus 로고    scopus 로고
    • Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy
    • Li, Y., Kijac, A. Z., Sligar, S. G., and Rienstra, C. M. (2006) Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy Biophys. J. 91, 3819-3828
    • (2006) Biophys. J. , vol.91 , pp. 3819-3828
    • Li, Y.1    Kijac, A.Z.2    Sligar, S.G.3    Rienstra, C.M.4
  • 33
    • 36849083490 scopus 로고    scopus 로고
    • Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4
    • Kijac, A. Z., Li, Y., Sligar, S. G., and Rienstra, C. M. (2007) Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4 Biochemistry 46, 13696-13703
    • (2007) Biochemistry , vol.46 , pp. 13696-13703
    • Kijac, A.Z.1    Li, Y.2    Sligar, S.G.3    Rienstra, C.M.4
  • 35
    • 78049317172 scopus 로고    scopus 로고
    • Reconstituted high density lipoprotein particles: A promising medium for high-resolution NMR investigations of membrane proteins and membrane-active peptides
    • Lyukmanova, E. N., Shenkarev, Z. O., Ovchinnikova, T. V., Chupin, V. V., Blommers, M. J. J., and Arseniev, A. S. (2008) Reconstituted high density lipoprotein particles: A promising medium for high-resolution NMR investigations of membrane proteins and membrane-active peptides FEBS J. 275, 171
    • (2008) FEBS J. , vol.275 , pp. 171
    • Lyukmanova, E.N.1    Shenkarev, Z.O.2    Ovchinnikova, T.V.3    Chupin, V.V.4    Blommers, M.J.J.5    Arseniev, A.S.6
  • 37
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog, T., Grimme, S., Li, M., Sligar, S. G., and Hazelbauer, G. L. (2006) Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties Proc. Natl. Acad. Sci. U.S.A. 103, 11509-11514
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 38
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • Shaw, A. W., Pureza, V. S., Sligar, S. G., and Morrissey, J. H. (2007) The local phospholipid environment modulates the activation of blood clotting J. Biol. Chem. 282, 6556-6563
    • (2007) J. Biol. Chem. , vol.282 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 39
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • Baas, B. J., Denisov, I. G., and Sligar, S. G. (2004) Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment Arch. Biochem. Biophys. 430, 218-228
    • (2004) Arch. Biochem. Biophys. , vol.430 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 40
    • 33747736671 scopus 로고    scopus 로고
    • The ferrous-dioxygen intermediate in human cytochrome P450 3A4. Substrate dependence of formation and decay kinetics
    • Denisov, I. G., Grinkova, Y. V., Baas, B. J., and Sligar, S. G. (2006) The ferrous-dioxygen intermediate in human cytochrome P450 3A4. Substrate dependence of formation and decay kinetics J. Biol. Chem. 281, 23313-23318
    • (2006) J. Biol. Chem. , vol.281 , pp. 23313-23318
    • Denisov, I.G.1    Grinkova, Y.V.2    Baas, B.J.3    Sligar, S.G.4
  • 41
    • 27144459868 scopus 로고    scopus 로고
    • Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization
    • Davydov, D. R., Fernando, H., Baas, B. J., Sligar, S. G., and Halpert, J. R. (2005) Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization Biochemistry 44, 13902-13913
    • (2005) Biochemistry , vol.44 , pp. 13902-13913
    • Davydov, D.R.1    Fernando, H.2    Baas, B.J.3    Sligar, S.G.4    Halpert, J.R.5
  • 42
    • 33744928866 scopus 로고    scopus 로고
    • Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs
    • Bayburt, T. H., Grinkova, Y. V., and Sligar, S. G. (2006) Assembly of single bacteriorhodopsin trimers in bilayer nanodiscs Arch. Biochem. Biophys. 450, 215-222
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 215-222
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 43
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt, T. H., Leitz, A. J., Xie, G., Oprian, D. D., and Sligar, S. G. (2007) Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins J. Biol. Chem. 282, 14875-14881
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 44
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • Alami, M., Dalal, K., Lelj-Garolla, B., Sligar, S. G., and Duong, F. (2007) Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA EMBO J. 26, 1995-2004
    • (2007) EMBO J. , vol.26 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 46
    • 1642463798 scopus 로고    scopus 로고
    • Co-incorporation of heterologously expressed Arabidopsis cytochrome P450 and P450 reductase into soluble nanoscale lipid bilayers
    • Duan, H., Civjan, N. R., Sligar, S. G., and Schuler, M. A. (2004) Co-incorporation of heterologously expressed Arabidopsis cytochrome P450 and P450 reductase into soluble nanoscale lipid bilayers Arch. Biochem. Biophys. 424, 141-153
    • (2004) Arch. Biochem. Biophys. , vol.424 , pp. 141-153
    • Duan, H.1    Civjan, N.R.2    Sligar, S.G.3    Schuler, M.A.4
  • 47
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation
    • Denisov, I. G., Baas, B. J., Grinkova, Y. V., and Sligar, S. G. (2007) Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation J. Biol. Chem. 282, 7066-7076
    • (2007) J. Biol. Chem. , vol.282 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4
  • 48
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • Bayburt, T. H. and Sligar, S. G. (2010) Membrane protein assembly into Nanodiscs FEBS Lett. 584, 1721-1727
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 49
    • 70349437270 scopus 로고    scopus 로고
    • The nanodisc: A novel tool for membrane protein studies
    • Borch, J. and Hamann, T. (2009) The nanodisc: A novel tool for membrane protein studies Biol. Chem. 390, 805-814
    • (2009) Biol. Chem. , vol.390 , pp. 805-814
    • Borch, J.1    Hamann, T.2
  • 50
    • 38649130606 scopus 로고    scopus 로고
    • Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy
    • Li, Y., Berthold, D. A., Gennis, R. B., and Rienstra, C. M. (2008) Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy Protein Sci. 17, 199-204
    • (2008) Protein Sci. , vol.17 , pp. 199-204
    • Li, Y.1    Berthold, D.A.2    Gennis, R.B.3    Rienstra, C.M.4
  • 52
    • 60149086516 scopus 로고    scopus 로고
    • Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump: Structural insights
    • Shi, L., Ahmed, M. A., Zhang, W., Whited, G., Brown, L. S., and Ladizhansky, V. (2009) Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump: Structural insights J. Mol. Biol. 386, 1078-1093
    • (2009) J. Mol. Biol. , vol.386 , pp. 1078-1093
    • Shi, L.1    Ahmed, M.A.2    Zhang, W.3    Whited, G.4    Brown, L.S.5    Ladizhansky, V.6
  • 53
    • 33846430490 scopus 로고    scopus 로고
    • Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy
    • Etzkorn, M., Martell, S., Andronesi, O. C., Seidel, K., Engelhard, M., and Baldus, M. (2007) Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy Angew. Chem., Int. Ed. 46, 459-462
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 459-462
    • Etzkorn, M.1    Martell, S.2    Andronesi, O.C.3    Seidel, K.4    Engelhard, M.5    Baldus, M.6
  • 54
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • Wasmer, C., Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R., and Meier, B. H. (2008) Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core Science 319, 1523-1526
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 55
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils
    • Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W. M., Mattson, M. P., and Tycko, R. (2005) Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils Science 307, 262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 56
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • Castellani, F., van Rossum, B., Diehl, A., Schubert, M., Rehbein, K., and Oschkinat, H. (2002) Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy Nature 420, 98-102
    • (2002) Nature , vol.420 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschkinat, H.6
  • 57
    • 0141645622 scopus 로고    scopus 로고
    • Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1
    • Park, S. H., Mrse, A. A., Nevzorov, A. A., Mesleh, M. F., Oblatt-Montal, M., Montal, M., and Opella, S. J. (2003) Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1 J. Mol. Biol. 333, 409-424
    • (2003) J. Mol. Biol. , vol.333 , pp. 409-424
    • Park, S.H.1    Mrse, A.A.2    Nevzorov, A.A.3    Mesleh, M.F.4    Oblatt-Montal, M.5    Montal, M.6    Opella, S.J.7
  • 58
    • 11144221228 scopus 로고    scopus 로고
    • Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy
    • Kamihira, M., Vosegaard, T., Mason, A. J., Straus, S. K., Nielsen, N. C., and Watts, A. (2005) Structural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy J. Struct. Biol. 149, 7-16
    • (2005) J. Struct. Biol. , vol.149 , pp. 7-16
    • Kamihira, M.1    Vosegaard, T.2    Mason, A.J.3    Straus, S.K.4    Nielsen, N.C.5    Watts, A.6
  • 60
    • 23244445025 scopus 로고    scopus 로고
    • Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus
    • Liu, W., Crocker, E., Constantinescu, S. N., and Smith, S. O. (2005) Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus Biophys. J. 89, 1194-1202
    • (2005) Biophys. J. , vol.89 , pp. 1194-1202
    • Liu, W.1    Crocker, E.2    Constantinescu, S.N.3    Smith, S.O.4
  • 61
    • 0037306147 scopus 로고    scopus 로고
    • Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A
    • Liu, W., Crocker, E., Siminovitch, D. J., and Smith, S. O. (2003) Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A Biophys. J. 84, 1263-1271
    • (2003) Biophys. J. , vol.84 , pp. 1263-1271
    • Liu, W.1    Crocker, E.2    Siminovitch, D.J.3    Smith, S.O.4
  • 63
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • Mani, R., Cady, S. D., Tang, M., Waring, A. J., Lehrer, R. I., and Hong, M. (2006) Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR Proc. Natl. Acad. Sci. U.S.A. 103, 16242-16247
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Tang, M.3    Waring, A.J.4    Lehrer, R.I.5    Hong, M.6
  • 64
    • 0037028547 scopus 로고    scopus 로고
    • 1H spin diffusion from lipids using solid-state NMR spectroscopy
    • 1H spin diffusion from lipids using solid-state NMR spectroscopy J. Am. Chem. Soc. 124, 874-883
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 874-883
    • Huster, D.1    Yao, X.2    Hong, M.3
  • 67
    • 33845217043 scopus 로고    scopus 로고
    • Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR
    • Hong, M. (2006) Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR Structure 14, 1731-1740
    • (2006) Structure , vol.14 , pp. 1731-1740
    • Hong, M.1
  • 68
    • 0032572058 scopus 로고    scopus 로고
    • A novel tool for probing membrane protein structure: Solid-state NMR with proton spin diffusion and X-nucleus detection
    • Kumashiro, K. K., Schmidt-Rohr, K., Murphy, O. J., Ouellette, K. L., Cramer, W. A., and Thompson, L. K. (1998) A novel tool for probing membrane protein structure: Solid-state NMR with proton spin diffusion and X-nucleus detection J. Am. Chem. Soc. 120, 5043-5051
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5043-5051
    • Kumashiro, K.K.1    Schmidt-Rohr, K.2    Murphy, O.J.3    Ouellette, K.L.4    Cramer, W.A.5    Thompson, L.K.6
  • 70
    • 0001211725 scopus 로고
    • NMR cross-polarization by adiabatic passage through the Hartmann-Hahn condition (APHH)
    • Hediger, S., Meier, B. H., Kurur, N. D., Bodenhausen, G., and Ernst, R. R. (1994) NMR cross-polarization by adiabatic passage through the Hartmann-Hahn condition (APHH) Chem. Phys. Lett. 223, 283-288
    • (1994) Chem. Phys. Lett. , vol.223 , pp. 283-288
    • Hediger, S.1    Meier, B.H.2    Kurur, N.D.3    Bodenhausen, G.4    Ernst, R.R.5
  • 72
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on Unix pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on Unix pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 73
    • 0042995329 scopus 로고    scopus 로고
    • Chemical shift referencing in MAS solid state NMR
    • Morcombe, C. R. and Zilm, K. W. (2003) Chemical shift referencing in MAS solid state NMR J. Magn. Reson. 162, 479-486
    • (2003) J. Magn. Reson. , vol.162 , pp. 479-486
    • Morcombe, C.R.1    Zilm, K.W.2
  • 74
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD: Visual molecular dynamics J. Mol. Graphics 14 (33-38) 27-38
    • (1996) J. Mol. Graphics , vol.14 , Issue.33-38 , pp. 27-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 76
    • 68949093961 scopus 로고    scopus 로고
    • Water Replacement Hypothesis in Atomic Detail-Factors Determining the Structure of Dehydrated Bilayer Stacks
    • Golovina, E. A., Golovin, A. V., Hoekstra, F. A., and Faller, R. (2009) Water Replacement Hypothesis in Atomic Detail-Factors Determining the Structure of Dehydrated Bilayer Stacks Biophys. J. 97, 490-499
    • (2009) Biophys. J. , vol.97 , pp. 490-499
    • Golovina, E.A.1    Golovin, A.V.2    Hoekstra, F.A.3    Faller, R.4
  • 78
    • 4243917179 scopus 로고
    • Dry Dipalmitoylphosphatidylcholine and Trehalose Revisited
    • Crowe, L. M. and Crowe, J. H. (1988) Dry Dipalmitoylphosphatidylcholine and Trehalose Revisited Biophys. J. 53, A127
    • (1988) Biophys. J. , vol.53 , pp. 127
    • Crowe, L.M.1    Crowe, J.H.2
  • 79
    • 0001217756 scopus 로고
    • A Simple Multi-Nuclear NMR Thermometer
    • Ammann, C., Meier, P., and Merbach, A. E. (1982) A Simple Multi-Nuclear NMR Thermometer J. Magn. Reson. 46, 319-321
    • (1982) J. Magn. Reson. , vol.46 , pp. 319-321
    • Ammann, C.1    Meier, P.2    Merbach, A.E.3
  • 80
    • 0028048734 scopus 로고
    • Interactions between Soluble Sugars and Popc (1-Palmitoyl-2- Oleoylphosphatidylcholine) during Dehydration: Vitrification of Sugars Alters the Phase-Behavior of the Phospholipid
    • Koster, K. L., Webb, M. S., Bryant, G., and Lynch, D. V. (1994) Interactions between Soluble Sugars and Popc (1-Palmitoyl-2- Oleoylphosphatidylcholine) during Dehydration: Vitrification of Sugars Alters the Phase-Behavior of the Phospholipid Biochim. Biophys. Acta 1193, 143-150
    • (1994) Biochim. Biophys. Acta , vol.1193 , pp. 143-150
    • Koster, K.L.1    Webb, M.S.2    Bryant, G.3    Lynch, D.V.4
  • 82
    • 0347985761 scopus 로고    scopus 로고
    • Phospholipid phase transitions in homogeneous nanometer scale bilayer discs
    • Shaw, A. W., McLean, M. A., and Sligar, S. G. (2004) Phospholipid phase transitions in homogeneous nanometer scale bilayer discs FEBS Lett. 556, 260-264
    • (2004) FEBS Lett. , vol.556 , pp. 260-264
    • Shaw, A.W.1    McLean, M.A.2    Sligar, S.G.3
  • 83
    • 0000432697 scopus 로고    scopus 로고
    • Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy
    • Hohwy, M., Rienstra, C. M., Jaroniec, C. P., and Griffin, R. G. (1999) Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy J. Chem. Phys. 110, 7983-7992
    • (1999) J. Chem. Phys. , vol.110 , pp. 7983-7992
    • Hohwy, M.1    Rienstra, C.M.2    Jaroniec, C.P.3    Griffin, R.G.4
  • 84
    • 0023962259 scopus 로고
    • High-Field, High-Resolution Proton Magic-Angle Sample-Spinning Nuclear Magnetic-Resonance Spectroscopic Studies of Gel and Liquid-Crystalline Lipid Bilayers and the Effects of Cholesterol
    • Forbes, J., Husted, C., and Oldfield, E. (1988) High-Field, High-Resolution Proton Magic-Angle Sample-Spinning Nuclear Magnetic-Resonance Spectroscopic Studies of Gel and Liquid-Crystalline Lipid Bilayers and the Effects of Cholesterol J. Am. Chem. Soc. 110, 1059-1065
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1059-1065
    • Forbes, J.1    Husted, C.2    Oldfield, E.3
  • 86
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D. W., Rogers, D. P., Engler, J. A., and Brouillette, C. G. (1997) Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation Proc. Natl. Acad. Sci. U.S.A. 94, 12291-12296
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 87
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • Zhang, H., Neal, S., and Wishart, D. S. (2003) RefDB: A database of uniformly referenced protein chemical shifts J. Biomol. NMR 25, 173-195
    • (2003) J. Biomol. NMR , vol.25 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.