메뉴 건너뛰기




Volumn 61, Issue 3-4, 2015, Pages 299-310

Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR

Author keywords

2D lipid crystals; MAS; Recoupling; VDAC

Indexed keywords

LIPID BILAYER; MICELLE; VDAC1 PROTEIN, HUMAN; VOLTAGE DEPENDENT ANION CHANNEL 1;

EID: 84939943994     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-015-9903-1     Document Type: Article
Times cited : (37)

References (87)
  • 3
    • 77955576540 scopus 로고    scopus 로고
    • Magic angle spinning NMR investigation of influenza A M2(18-60): Support for an allosteric mechanism of inhibition
    • Andreas LB, Eddy MT, Pielak RM, Chou J, Griffin RG (2010) Magic angle spinning NMR investigation of influenza A M2(18-60): support for an allosteric mechanism of inhibition. J Am Chem Soc 132(32):10958-10960
    • (2010) J Am Chem Soc , vol.132 , Issue.32 , pp. 10958-10960
    • Andreas, L.B.1    Eddy, M.T.2    Pielak, R.M.3    Chou, J.4    Griffin, R.G.5
  • 4
    • 25144453329 scopus 로고    scopus 로고
    • Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy
    • Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M (2005) Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J Am Chem Soc 127(37):12965-12974
    • (2005) J Am Chem Soc , vol.127 , Issue.37 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 5
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein. A transmembrane domain by NMR spectroscopy
    • Arora A, Abildgaard F, Bushweller JH, Tamm LK (2001) Structure of outer membrane protein. A transmembrane domain by NMR spectroscopy. Nat Struct Biol 8(4):334-338
    • (2001) Nat Struct Biol , vol.8 , Issue.4 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 6
    • 67249096746 scopus 로고    scopus 로고
    • Functional and shunt states of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solid-state NMR
    • 2009PNAS.106.9244B
    • Bajaj VS, Mak-Jurkauskas ML, Belenky M, Herzfeld J, Griffin RG (2009) Functional and shunt states of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solid-state NMR. Proc Natl Acad Sci USA 106(23):9244-9249
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.23 , pp. 9244-9249
    • Bajaj, V.S.1    Mak-Jurkauskas, M.L.2    Belenky, M.3    Herzfeld, J.4    Griffin, R.G.5
  • 7
    • 0000368822 scopus 로고    scopus 로고
    • Cross polarization in the tilted frame: Assignment and spectral simplification in heteronuclear spin systems
    • 1998MolPh.95.1197B
    • Baldus M, Petkova AT, Herzfeld J, Griffin RG (1998) Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems. Mol Phys 95(6):1197-1207
    • (1998) Mol Phys , vol.95 , Issue.6 , pp. 1197-1207
    • Baldus, M.1    Petkova, A.T.2    Herzfeld, J.3    Griffin, R.G.4
  • 12
    • 84866560561 scopus 로고    scopus 로고
    • Protonation state of E71 in KcsA and its role for channel collapse and inactivation
    • 2012PNAS.10915265B
    • Bhate MP, McDermott AE (2012) Protonation state of E71 in KcsA and its role for channel collapse and inactivation. Proc Natl Acad Sci USA 109(38):15265-15270
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.38 , pp. 15265-15270
    • Bhate, M.P.1    McDermott, A.E.2
  • 13
    • 77955087369 scopus 로고    scopus 로고
    • Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration
    • Bhate MP, Wylie BJ, Tian L, Mcdermott AE (2010) Conformational dynamics in the selectivity filter of KcsA in response to potassium ion concentration. J Mol Biol 401:1-12
    • (2010) J Mol Biol , vol.401 , pp. 1-12
    • Bhate, M.P.1    Wylie, B.J.2    Tian, L.3    McDermott, A.E.4
  • 14
    • 84918807150 scopus 로고    scopus 로고
    • X-ray structure of a calcium-activated TMEM16 lipid scramblase
    • 2014Natur.516.207B
    • Brunner JD, Lim NK, Schenck S, Duerst A, Dutzler R (2014) X-ray structure of a calcium-activated TMEM16 lipid scramblase. Nature 516(7530):207-212
    • (2014) Nature , vol.516 , Issue.7530 , pp. 207-212
    • Brunner, J.D.1    Lim, N.K.2    Schenck, S.3    Duerst, A.4    Dutzler, R.5
  • 16
    • 84894189160 scopus 로고    scopus 로고
    • Solid state NMR: The essential technology for helical membrane protein structural characterization
    • 2014JMagR.239.100C
    • Cross TA, Ekanayake V, Paulino J, Wright A (2014) Solid state NMR: the essential technology for helical membrane protein structural characterization. J Magn Reson 239(C):100-109
    • (2014) J Magn Reson , vol.239 , Issue.C , pp. 100-109
    • Cross, T.A.1    Ekanayake, V.2    Paulino, J.3    Wright, A.4
  • 17
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3):277-293
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 18
    • 0032875663 scopus 로고    scopus 로고
    • Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids
    • Dolder M, Zeth K, Tittmann P, Gross H, Welte W, Wallimann T (1999) Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids. J Struct Biol 127(1):64-71
    • (1999) J Struct Biol , vol.127 , Issue.1 , pp. 64-71
    • Dolder, M.1    Zeth, K.2    Tittmann, P.3    Gross, H.4    Welte, W.5    Wallimann, T.6
  • 20
    • 84904259912 scopus 로고    scopus 로고
    • Membranes, peptides, and disease. Unraveling the mechanisms of viral proteins with solid state nuclear magnetic resonance spectroscopy
    • Eddy MT, Yu T-Y (2014) Membranes, peptides, and disease. Unraveling the mechanisms of viral proteins with solid state nuclear magnetic resonance spectroscopy. Solid State Nucl Magn Reson 61-62:1-7
    • (2014) Solid State Nucl Magn Reson , vol.61-62 , Issue.C , pp. 1-7
    • Eddy, M.T.1    Yu, T.-Y.2
  • 22
    • 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 OC, Seidel K, Engelhard M, 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(3):459-462
    • (2007) Angew Chem Int Ed , vol.46 , Issue.3 , pp. 459-462
    • Etzkorn, M.1    Martell, S.2    Andronesi, O.C.3    Seidel, K.4    Engelhard, M.5    Baldus, M.6
  • 23
    • 0035956956 scopus 로고    scopus 로고
    • Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
    • 2001PNAS.98.2358F
    • Fernández C, Adeishvili K, Wüthrich K (2001) Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc Natl Acad Sci USA 98(5):2358-2363
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.5 , pp. 2358-2363
    • Fernández, C.1    Adeishvili, K.2    Wüthrich, K.3
  • 25
    • 33749177428 scopus 로고    scopus 로고
    • Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex: E. Coli cytochrome bo3 oxidase
    • Frericks HL, Zhou DH, Yap LL, Gennis RB, Rienstra CM (2006) Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex: E. coli cytochrome bo3 oxidase. J Biomol NMR 36(1):55-71
    • (2006) J Biomol NMR , vol.36 , Issue.1 , pp. 55-71
    • Frericks, H.L.1    Zhou, D.H.2    Yap, L.L.3    Gennis, R.B.4    Rienstra, C.M.5
  • 27
    • 0034681198 scopus 로고    scopus 로고
    • Structural investigation of the active site in bacteriorhodopsin: Geometric constraints on the roles of Asp-85 and Asp-212 in the proton-pumping mechanism from solid state NMR
    • Griffiths J, Bennett A, Engelhard M, Siebert F, Raap J, Lugtenburg J, Herzfeld J, Griffin R (2000a) Structural investigation of the active site in bacteriorhodopsin: geometric constraints on the roles of Asp-85 and Asp-212 in the proton-pumping mechanism from solid state NMR. Biochemistry 39(2):362-371
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 362-371
    • Griffiths, J.1    Bennett, A.2    Engelhard, M.3    Siebert, F.4    Raap, J.5    Lugtenburg, J.6    Herzfeld, J.7    Griffin, R.8
  • 28
    • 0034681198 scopus 로고    scopus 로고
    • Structural investigation of the active site of bacteriorhodopsin: Geometric constraints on the roles of Asp-85 and Asp-212 in the proton pumping mechanism from solid-state NMR
    • Griffiths JM, Bennett AE, Engelhard M, Siebert F, Raap J, Lugtenburg J, Herzfeld J, Griffin RG (2000b) Structural investigation of the active site of bacteriorhodopsin: geometric constraints on the roles of Asp-85 and Asp-212 in the proton pumping mechanism from solid-state NMR. Biochemistry 39:362-371
    • (2000) Biochemistry , vol.39 , pp. 362-371
    • Griffiths, J.M.1    Bennett, A.E.2    Engelhard, M.3    Siebert, F.4    Raap, J.5    Lugtenburg, J.6    Herzfeld, J.7    Griffin, R.G.8
  • 30
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR
    • 2005PNAS.10215871H
    • Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, Baldus M (2005) Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 102(44):15871-15876
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.44 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 31
    • 68349098894 scopus 로고    scopus 로고
    • Assigning large proteins in the solid state: A MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins
    • Higman VA, Flinders J, Hiller M, Jehle S, Markovic S, Fiedler S, Rossum B-J, Oschkinat H (2009) Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins. J Biomol NMR 44(4):245-260
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 245-260
    • Higman, V.A.1    Flinders, J.2    Hiller, M.3    Jehle, S.4    Markovic, S.5    Fiedler, S.6    Rossum, B.-J.7    Oschkinat, H.8
  • 33
    • 40149084899 scopus 로고    scopus 로고
    • [2,3-(13)C]-labeling of aromatic residues-getting a head start in the magic-angle-spinning NMR assignment of membrane proteins
    • Hiller M, Higman VA, Jehle S, van Rossum B-J, Kühlbrandt W, Oschkinat H (2008a) [2,3-(13)C]-labeling of aromatic residues-getting a head start in the magic-angle-spinning NMR assignment of membrane proteins. J Am Chem Soc 130(2):408-409
    • (2008) J Am Chem Soc , vol.130 , Issue.2 , pp. 408-409
    • Hiller, M.1    Higman, V.A.2    Jehle, S.3    Van Rossum, B.-J.4    Kühlbrandt, W.5    Oschkinat, H.6
  • 34
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • 2008Sci.321.1206H
    • Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G (2008b) Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science (New York, NY) 321(5893):1206-1210
    • (2008) Science (New York, NY) , vol.321 , Issue.5893 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 35
    • 77951877832 scopus 로고    scopus 로고
    • Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1
    • Hiller S, Malia TJ, Garces RG, Orekhov VY, Wagner G (2010) Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1. Biomol NMR Assign 4(1):29-32
    • (2010) Biomol NMR Assign , vol.4 , Issue.1 , pp. 29-32
    • Hiller, S.1    Malia, T.J.2    Garces, R.G.3    Orekhov, V.Y.4    Wagner, G.5
  • 36
    • 43949171911 scopus 로고
    • Measurement of heteronuclear dipolar coupling by transferred-echo double-resonance NMR
    • 1993JMagR.103.151H
    • Hing A, Vega S, Schaefer J (1993) Measurement of heteronuclear dipolar coupling by transferred-echo double-resonance NMR. J Magn Reson Ser A 103(2):151-162
    • (1993) J Magn Reson ser A , vol.103 , Issue.2 , pp. 151-162
    • Hing, A.1    Vega, S.2    Schaefer, J.3
  • 38
    • 0030958679 scopus 로고    scopus 로고
    • Regulation of metabolite flux through voltage-gating of VDAC channels
    • Hodge T, Colombini M (1997) Regulation of metabolite flux through voltage-gating of VDAC channels. J Membr Biol 157(3):271-279
    • (1997) J Membr Biol , vol.157 , Issue.3 , pp. 271-279
    • Hodge, T.1    Colombini, M.2
  • 39
    • 84859912916 scopus 로고    scopus 로고
    • Membrane Protein Structure and Dynamics from NMR Spectroscopy
    • 2012ARPC.63.1H
    • Hong M, Zhang Y, Hu F (2012) Membrane Protein Structure and Dynamics from NMR Spectroscopy. Annu Rev Phys Chem 63(1):1-24
    • (2012) Annu Rev Phys Chem , vol.63 , Issue.1 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 42
    • 0037063498 scopus 로고    scopus 로고
    • 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly 13C, 15 N-labeled solids
    • Jaroniec C, Filip C, Griffin R (2002a) 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly 13C, 15 N-labeled solids. J Am Chem Soc 124(36):10728-10742
    • (2002) J Am Chem Soc , vol.124 , Issue.36 , pp. 10728-10742
    • Jaroniec, C.1    Filip, C.2    Griffin, R.3
  • 43
    • 0037063498 scopus 로고    scopus 로고
    • 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C, (15)N-labeled solids
    • Jaroniec CP, Filip C, Griffin RG (2002b) 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C, (15)N-labeled solids. J Am Chem Soc 124(36):10728-10742
    • (2002) J Am Chem Soc , vol.124 , Issue.36 , pp. 10728-10742
    • Jaroniec, C.P.1    Filip, C.2    Griffin, R.G.3
  • 44
    • 67649365444 scopus 로고    scopus 로고
    • Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy
    • Krabben L, van BJ Rossum, Jehle S, Bocharov E, Lyukmanova EN, Schulga AA, Arseniev A, Hucho F, Oschkinat H (2009) Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy. J Mol Biol 390(4):662-671
    • (2009) J Mol Biol , vol.390 , Issue.4 , pp. 662-671
    • Krabben, L.1    Van Bj, R.2    Jehle, S.3    Bocharov, E.4    Lyukmanova, E.N.5    Schulga, A.A.6    Arseniev, A.7    Hucho, F.8    Oschkinat, H.9
  • 45
  • 46
    • 33845190562 scopus 로고    scopus 로고
    • Two-dimensional solid-state nmr applied to a chimeric potassium channel
    • Lange A, Giller K, Pongs O, Becker S, Baldus M (2006) Two-dimensional solid-state nmr applied to a chimeric potassium channel. J Recept Signal Transduct 26(5-6):379-393
    • (2006) J Recept Signal Transduct , vol.26 , Issue.5-6 , pp. 379-393
    • Lange, A.1    Giller, K.2    Pongs, O.3    Becker, S.4    Baldus, M.5
  • 47
    • 0037080338 scopus 로고    scopus 로고
    • Chromophore distortions in the bacteriorhodopsin photocycle: Evolution of the H-C14-C15-H dihedral angle measured by solid-state NMR
    • Lansing JC, Hohwy M, Jaroniec CP, Creemers AFL, Lugtenburg J, Herzfeld J, Griffin RG (2002) Chromophore distortions in the bacteriorhodopsin photocycle: evolution of the H-C14-C15-H dihedral angle measured by solid-state NMR. Biochemistry 41(2):431-438
    • (2002) Biochemistry , vol.41 , Issue.2 , pp. 431-438
    • Lansing, J.C.1    Hohwy, M.2    Jaroniec, C.P.3    Afl, C.4    Lugtenburg, J.5    Herzfeld, J.6    Griffin, R.G.7
  • 48
    • 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 DA, Gennis RB, Rienstra CM (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(2):199-204
    • (2008) Protein Sci , vol.17 , Issue.2 , pp. 199-204
    • Li, Y.1    Berthold, D.A.2    Gennis, R.B.3    Rienstra, C.M.4
  • 49
    • 36048971123 scopus 로고    scopus 로고
    • Structure of outer membrane protein G by solution NMR spectroscopy
    • 2007PNAS.10416140L
    • Liang B, Tamm LK (2007) Structure of outer membrane protein G by solution NMR spectroscopy. Proc Natl Acad Sci USA 104(41):16140-16145
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.41 , pp. 16140-16145
    • Liang, B.1    Tamm, L.K.2
  • 51
    • 33846207499 scopus 로고    scopus 로고
    • NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL
    • Malia TJ, Wagner G (2007) NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL. Biochemistry 46(2):514-525
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 514-525
    • Malia, T.J.1    Wagner, G.2
  • 52
    • 0031448082 scopus 로고    scopus 로고
    • Minireview: On the structure and gating mechanism of the mitochondrial channel, VDAC
    • Mannella CA (1997) Minireview: on the structure and gating mechanism of the mitochondrial channel, VDAC. J Bioenerg Biomembr 29(6):525-531
    • (1997) J Bioenerg Biomembr , vol.29 , Issue.6 , pp. 525-531
    • Mannella, C.A.1
  • 53
    • 4744357287 scopus 로고    scopus 로고
    • Structural and dynamic studies of proteins by solid-state NMR spectroscopy: Rapid movement forward
    • McDermott AE (2004) Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward. Curr Opin Struct Biol 14(5):554-561
    • (2004) Curr Opin Struct Biol , vol.14 , Issue.5 , pp. 554-561
    • McDermott, A.E.1
  • 54
    • 67650285019 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR
    • 2525550
    • McDermott A (2009) Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR. Annu Rev Biophys 38:385-403
    • (2009) Annu Rev Biophys , vol.38 , pp. 385-403
    • McDermott, A.1
  • 55
    • 2942614815 scopus 로고    scopus 로고
    • Diluting abundant spins by isotope edited radio frequency field assisted diffusion
    • Morcombe CR, Gaponenko V, Byrd RA, Zilm KW (2004) Diluting abundant spins by isotope edited radio frequency field assisted diffusion. J Am Chem Soc 126(23):7196-7197
    • (2004) J Am Chem Soc , vol.126 , Issue.23 , pp. 7196-7197
    • Morcombe, C.R.1    Gaponenko, V.2    Byrd, R.A.3    Zilm, K.W.4
  • 56
    • 33845560617 scopus 로고
    • Enhancement of nuclear magnetic resonance signals by polarization transfer
    • Morris G, Freeman R (1979) Enhancement of nuclear magnetic resonance signals by polarization transfer. J Am Chem Soc 101(3):760-762
    • (1979) J Am Chem Soc , vol.101 , Issue.3 , pp. 760-762
    • Morris, G.1    Freeman, R.2
  • 57
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • 2005PNAS.10210870O
    • Oxenoid K, Chou JJ (2005) The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc Natl Acad Sci USA 102(31):10870-10875
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.31 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 59
    • 36849106840 scopus 로고
    • Proton-enhanced NMR of dilute spins in solids
    • 1973JChPh.59.569P
    • Pines A, Gibby M, Waugh J (1973) Proton-enhanced NMR of dilute spins in solids. J Chem Phys 59(2):569-590
    • (1973) J Chem Phys , vol.59 , Issue.2 , pp. 569-590
    • Pines, A.1    Gibby, M.2    Waugh, J.3
  • 62
    • 57749192468 scopus 로고    scopus 로고
    • Solution State NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications
    • Renault M, Saurel O, Czaplicki J, Demange P, Gervais V, Löhr F, Réat V, Piotto M, Milon A (2009) Solution State NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications. J Mol Biol 385(1):117-130
    • (2009) J Mol Biol , vol.385 , Issue.1 , pp. 117-130
    • Renault, M.1    Saurel, O.2    Czaplicki, J.3    Demange, P.4    Gervais, V.5    Löhr, F.6    Réat, V.7    Piotto, M.8    Milon, A.9
  • 64
    • 0029854155 scopus 로고    scopus 로고
    • ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane
    • Rostovtseva T, Colombini M (1996) ATP flux is controlled by a voltage-gated channel from the mitochondrial outer membrane. J Biol Chem 271(45):28006-28008
    • (1996) J Biol Chem , vol.271 , Issue.45 , pp. 28006-28008
    • Rostovtseva, T.1    Colombini, M.2
  • 65
    • 0017054558 scopus 로고
    • Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria
    • Schein SJ, Colombini M, Finkelstein A (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J Membr Biol 30(2):99-120
    • (1976) J Membr Biol , vol.30 , Issue.2 , pp. 99-120
    • Schein, S.J.1    Colombini, M.2    Finkelstein, A.3
  • 69
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • 2008Natur.451.591S
    • Schnell JR, Chou JJ (2008) Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451(7178):591-595
    • (2008) Nature , vol.451 , Issue.7178 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 70
    • 33947324465 scopus 로고    scopus 로고
    • Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer
    • Shanmugavadivu B, Apell H-J, Meins T, Zeth K, Kleinschmidt JH (2007) Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer. J Mol Biol 368(1):66-78
    • (2007) J Mol Biol , vol.368 , Issue.1 , pp. 66-78
    • Shanmugavadivu, B.1    Apell, H.-J.2    Meins, T.3    Zeth, K.4    Kleinschmidt, J.H.5
  • 71
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213-223
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 72
    • 43649102166 scopus 로고    scopus 로고
    • Resolution enhancement by homonuclear J-decoupling: Application to three-dimensional solid-state magic angle spinning NMR spectroscopy
    • Shi L, Peng X, Ahmed MAM, Edwards D, Brown LS, Ladizhansky V (2008) Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy. J Biomol NMR 41(1):9-15
    • (2008) J Biomol NMR , vol.41 , Issue.1 , pp. 9-15
    • Shi, L.1    Peng, X.2    Ahmed, M.A.M.3    Edwards, D.4    Brown, L.S.5    Ladizhansky, V.6
  • 73
    • 60149086516 scopus 로고    scopus 로고
    • Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump-structural insights
    • Shi L, Ahmed MAM, Zhang W, Whited G, Brown LS, Ladizhansky V (2009a) Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump-structural insights. J Mol Biol 386(4):1078-1093
    • (2009) J Mol Biol , vol.386 , Issue.4 , pp. 1078-1093
    • Shi, L.1    Ahmed, M.A.M.2    Zhang, W.3    Whited, G.4    Brown, L.S.5    Ladizhansky, V.6
  • 74
    • 71749093086 scopus 로고    scopus 로고
    • Solid-state NMR study of proteorhodopsin in the lipid environment: Secondary structure and dynamics
    • Shi L, Lake EMR, Ahmed MAM, Brown LS, Ladizhansky V (2009b) Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics. Biochim Biophys Acta 1788(12):2563-2574
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.12 , pp. 2563-2574
    • Shi, L.1    Lake, E.M.R.2    Ahmed, M.A.M.3    Brown, L.S.4    Ladizhansky, V.5
  • 75
    • 84977769527 scopus 로고    scopus 로고
    • Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump-structural insights-supporting Info
    • Shi L, Ahmed MAM, Zhang W, Whited G, Brown LS, Ladizhansky V (2009b) Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump-structural insights-supporting Info. J Mol Biol 1-9
    • (2009) J Mol Biol , pp. 1-9
    • Shi, L.1    Mam, A.2    Zhang, W.3    Whited, G.4    Brown, L.S.5    Ladizhansky, V.6
  • 77
    • 0000953276 scopus 로고    scopus 로고
    • C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR
    • 2001CPL.344.631T
    • Takegoshi K, Nakamura S, Terao T (2001) C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem Phys Lett 344(5-6):631-637
    • (2001) Chem Phys Lett , vol.344 , Issue.5-6 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 80
    • 57049142593 scopus 로고    scopus 로고
    • Measurement of sample temperatures under magic-angle spinning from the chemical shift and spin-lattice relaxation rate of 79Br in KBr powder
    • 2009JMagR.196.84T
    • Thurber KR, Tycko R (2009) Measurement of sample temperatures under magic-angle spinning from the chemical shift and spin-lattice relaxation rate of 79Br in KBr powder. J Magn Reson 196(1):84-87
    • (2009) J Magn Reson , vol.196 , Issue.1 , pp. 84-87
    • Thurber, K.R.1    Tycko, R.2
  • 81
    • 56649099192 scopus 로고    scopus 로고
    • The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating
    • 2008PNAS.10517742U
    • Ujwal R, Cascio D, Colletier J-P, Faham S, Zhang J, Toro L, Ping P, Abramson J (2008) The crystal structure of mouse VDAC1 at 2.3 A resolution reveals mechanistic insights into metabolite gating. Proc Natl Acad Sci USA 105(46):17742-17747
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.46 , pp. 17742-17747
    • Ujwal, R.1    Cascio, D.2    Colletier, J.-P.3    Faham, S.4    Zhang, J.5    Toro, L.6    Ping, P.7    Abramson, J.8
  • 82
    • 36849063098 scopus 로고    scopus 로고
    • Solid-state NMR study and assignments of the KcsA potassium ion channel of S. Lividans
    • Varga K, Tian L, McDermott AE (2007) Solid-state NMR study and assignments of the KcsA potassium ion channel of S. lividans. Biochim Biophys Acta 1774(12):1604-1613
    • (2007) Biochim Biophys Acta , vol.1774 , Issue.12 , pp. 1604-1613
    • Varga, K.1    Tian, L.2    McDermott, A.E.3
  • 83
    • 79959340086 scopus 로고    scopus 로고
    • Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method
    • 2011PNAS.108.9101V
    • Verardi R, Shi L, Traaseth NJ, Walsh N, Veglia G (2011) Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method. Proc Natl Acad Sci USA 108(22):9101-9106
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.22 , pp. 9101-9106
    • Verardi, R.1    Shi, L.2    Traaseth, N.J.3    Walsh, N.4    Veglia, G.5
  • 85
    • 2642642085 scopus 로고    scopus 로고
    • Probing the agonist binding pocket in the nicotinic acetylcholine receptor: A high-resolution solid-state NMR approach
    • Williamson PT, Gröbner G, Spooner PJ, Miller KW, Watts A (1998) Probing the agonist binding pocket in the nicotinic acetylcholine receptor: a high-resolution solid-state NMR approach. Biochemistry 37(30):10854-10859
    • (1998) Biochemistry , vol.37 , Issue.30 , pp. 10854-10859
    • Williamson, P.T.1    Gröbner, G.2    Spooner, P.J.3    Miller, K.W.4    Watts, A.5
  • 86
    • 36749085427 scopus 로고    scopus 로고
    • The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor
    • 2007PNAS.10418031W
    • Williamson PT, Verhoeven A, Miller KW, Meier BH, Watts A (2007) The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor. Proc Natl Acad Sci USA 104(46):18031-18036
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.46 , pp. 18031-18036
    • Williamson, P.T.1    Verhoeven, A.2    Miller, K.W.3    Meier, B.H.4    Watts, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.