메뉴 건너뛰기




Volumn 1768, Issue 12, 2007, Pages 3098-3106

Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better

Author keywords

Bicelle; Micelle; Multidrug resistance; Smr; Structure

Indexed keywords

MEMBRANE PROTEIN;

EID: 36849088540     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.09.006     Document Type: Review
Times cited : (103)

References (89)
  • 1
    • 33750918707 scopus 로고    scopus 로고
    • Recent developments in membrane-protein structural genomics
    • Gao F.P., and Cross T.A. Recent developments in membrane-protein structural genomics. Genome Biol. 6 (2005) 244
    • (2005) Genome Biol. , vol.6 , pp. 244
    • Gao, F.P.1    Cross, T.A.2
  • 2
    • 16244421653 scopus 로고    scopus 로고
    • Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP
    • Hwang P.M., and Kay L.E. Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP. Methods Enzymol. 394 (2005) 335-350
    • (2005) Methods Enzymol. , vol.394 , pp. 335-350
    • Hwang, P.M.1    Kay, L.E.2
  • 3
    • 33746217557 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins: practice and challenges
    • Sanders C.R., and Sönnichsen F. Solution NMR of membrane proteins: practice and challenges. Magn. Reson. Chem. 44 (2006) S24-S40
    • (2006) Magn. Reson. Chem. , vol.44
    • Sanders, C.R.1    Sönnichsen, F.2
  • 6
    • 0027970086 scopus 로고
    • Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump
    • Grinius L.L., and Goldberg E.B. Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump. J. Biol. Chem. 269 (1994) 29998-30004
    • (1994) J. Biol. Chem. , vol.269 , pp. 29998-30004
    • Grinius, L.L.1    Goldberg, E.B.2
  • 7
    • 3042561938 scopus 로고    scopus 로고
    • The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state
    • Butler P.J.G., Ubarretxena-Belandia I., Warne T., and Tate C.G. The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state. J. Mol. Biol. 340 (2004) 797-808
    • (2004) J. Mol. Biol. , vol.340 , pp. 797-808
    • Butler, P.J.G.1    Ubarretxena-Belandia, I.2    Warne, T.3    Tate, C.G.4
  • 8
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz Y., Steiner-Mordoch S., Danieli T., and Schuldiner S. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 1519-1524
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 9
    • 0346874401 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer
    • Ubarretxena-Belandia I., Baldwin J.M., Schuldiner S., and Tate C.G. Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer. EMBO J. 22 (2003) 6175-6181
    • (2003) EMBO J. , vol.22 , pp. 6175-6181
    • Ubarretxena-Belandia, I.1    Baldwin, J.M.2    Schuldiner, S.3    Tate, C.G.4
  • 11
    • 33646147814 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination
    • Columbus L., Lipfert J., Klock H., Millett I., Doniach S., and Lesley S.A. Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination. Protein Sci. 15 (2006) 961-975
    • (2006) Protein Sci. , vol.15 , pp. 961-975
    • Columbus, L.1    Lipfert, J.2    Klock, H.3    Millett, I.4    Doniach, S.5    Lesley, S.A.6
  • 13
    • 0032060715 scopus 로고    scopus 로고
    • On choosing a detergent for solution NMR studies of membrane proteins
    • Vinogradova O., Sönnichsen F., and Sanders C.R. On choosing a detergent for solution NMR studies of membrane proteins. J. Biomol. NMR 11 (1998) 381-386
    • (1998) J. Biomol. NMR , vol.11 , pp. 381-386
    • Vinogradova, O.1    Sönnichsen, F.2    Sanders, C.R.3
  • 14
    • 0034629489 scopus 로고    scopus 로고
    • Building a thermostable membrane protein
    • Zhou Y., and Bowie J.U. Building a thermostable membrane protein. J. Biol. Chem. 275 (2000) 6975-6979
    • (2000) J. Biol. Chem. , vol.275 , pp. 6975-6979
    • Zhou, Y.1    Bowie, J.U.2
  • 18
    • 3042707182 scopus 로고    scopus 로고
    • The integral membrane enzyme PagP alternates between two dynamically distinct states
    • Hwang P.M., Bishop R.E., and Kay L.E. The integral membrane enzyme PagP alternates between two dynamically distinct states. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9618-9623
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9618-9623
    • Hwang, P.M.1    Bishop, R.E.2    Kay, L.E.3
  • 19
    • 33645504750 scopus 로고    scopus 로고
    • NMR study of the tetrameric KcsA potassium channel in detergent micelles
    • Chill J.H., Louis J.M., Miller C., and Bax A. NMR study of the tetrameric KcsA potassium channel in detergent micelles. Protein Sci. 15 (2006) 684-698
    • (2006) Protein Sci. , vol.15 , pp. 684-698
    • Chill, J.H.1    Louis, J.M.2    Miller, C.3    Bax, A.4
  • 20
    • 33749162032 scopus 로고    scopus 로고
    • 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel
    • 15N relaxation in the detergent-solubilized tetrameric KcsA potassium channel. J. Biomol. NMR 36 (2006) 123-136
    • (2006) J. Biomol. NMR , vol.36 , pp. 123-136
    • Chill, J.H.1    Louis, J.M.2    Baber, J.L.3    Bax, A.4
  • 21
    • 0030739227 scopus 로고    scopus 로고
    • Tetrameric stoichiometry of a prokaryotic K+ channel
    • Heginbotham L., Odessey E., and Miller C. Tetrameric stoichiometry of a prokaryotic K+ channel. Biochemistry 36 (1997) 10335-10342
    • (1997) Biochemistry , vol.36 , pp. 10335-10342
    • Heginbotham, L.1    Odessey, E.2    Miller, C.3
  • 22
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating
    • Cortes D.M., Cuello L.G., and Perozo E. Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117 (2001) 165-180
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 23
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution
    • Zhou Y., Morais-Cabral J.H., Kaufman A., and MacKinnon R. Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 Å resolution. Nature 414 (2001) 43-48
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 24
    • 33750022623 scopus 로고    scopus 로고
    • The structure of the ζζ transmembrane dimer reveals features essential for its assembly with the T cell receptor
    • Call M.E., Schnell J.R., Xu C., Lutz R.A., Chou J.J., and Wucherpfennig K.W. The structure of the ζζ transmembrane dimer reveals features essential for its assembly with the T cell receptor. Cell 127 (2006) 355-368
    • (2006) Cell , vol.127 , pp. 355-368
    • Call, M.E.1    Schnell, J.R.2    Xu, C.3    Lutz, R.A.4    Chou, J.J.5    Wucherpfennig, K.W.6
  • 26
    • 33847678076 scopus 로고    scopus 로고
    • Isotropic bicelles stabilize the functional form of a small multidrug-resistance pump for NMR structural studies
    • Poget S.F., Cahill S.M., and Girvin M.E. Isotropic bicelles stabilize the functional form of a small multidrug-resistance pump for NMR structural studies. J. Am. Chem. Soc. 129 (2007) 1232-1233
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1232-1233
    • Poget, S.F.1    Cahill, S.M.2    Girvin, M.E.3
  • 27
    • 0028986717 scopus 로고
    • EmrE, an Escherichia-coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents
    • Yerushalmi H., Lebendiker M., and Schuldiner S. EmrE, an Escherichia-coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents. J. Biol. Chem. 270 (1995) 6856-6863
    • (1995) J. Biol. Chem. , vol.270 , pp. 6856-6863
    • Yerushalmi, H.1    Lebendiker, M.2    Schuldiner, S.3
  • 28
    • 0033026167 scopus 로고    scopus 로고
    • Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values
    • Ottiger M., and Bax A. Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values. J. Biomol. NMR 13 (1999) 187-191
    • (1999) J. Biomol. NMR , vol.13 , pp. 187-191
    • Ottiger, M.1    Bax, A.2
  • 29
    • 0031112791 scopus 로고    scopus 로고
    • Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides
    • Vold R.R., Prosser R.S., and Deese A.J. Isotropic solutions of phospholipid bicelles: a new membrane mimetic for high-resolution NMR studies of polypeptides. J. Biomol. NMR 9 (1997) 329-335
    • (1997) J. Biomol. NMR , vol.9 , pp. 329-335
    • Vold, R.R.1    Prosser, R.S.2    Deese, A.J.3
  • 30
    • 0032177257 scopus 로고    scopus 로고
    • Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules
    • Losonczi J.A., and Prestegard J.H. Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules. J. Biomol. NMR 12 (1998) 447-451
    • (1998) J. Biomol. NMR , vol.12 , pp. 447-451
    • Losonczi, J.A.1    Prestegard, J.H.2
  • 31
    • 32344432998 scopus 로고    scopus 로고
    • Reconstitution and alignment by a magnetic field of a beta-barrel membrane protein in bicelles
    • Triba M.N., Zoonens M., Popot J.L., Devaux P.F., and Warschawski D.E. Reconstitution and alignment by a magnetic field of a beta-barrel membrane protein in bicelles. Eur. Biophys. J. 35 (2006) 268-275
    • (2006) Eur. Biophys. J. , vol.35 , pp. 268-275
    • Triba, M.N.1    Zoonens, M.2    Popot, J.L.3    Devaux, P.F.4    Warschawski, D.E.5
  • 32
    • 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. Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers. Biotechniques 261 (2003) 556-563
    • (2003) Biotechniques , vol.261 , pp. 556-563
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 33
    • 0023035961 scopus 로고
    • sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence
    • Walsh J.P., and Bell R.M. sn-1,2-Diacylglycerol kinase of Escherichia coli. Structural and kinetic analysis of the lipid cofactor dependence. J. Biol. Chem. 261 (1986) 15062-15069
    • (1986) J. Biol. Chem. , vol.261 , pp. 15062-15069
    • Walsh, J.P.1    Bell, R.M.2
  • 34
    • 33745261286 scopus 로고    scopus 로고
    • Phospholipid requirement and pH optimum for the in vitro enzymatic activity of the E. coli P-type ATPase ZntA
    • Zimmer J., and Doyle D.A. Phospholipid requirement and pH optimum for the in vitro enzymatic activity of the E. coli P-type ATPase ZntA. Biochim. Biophys. Acta 1758 (2006) 645-652
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 645-652
    • Zimmer, J.1    Doyle, D.A.2
  • 35
    • 27344442574 scopus 로고    scopus 로고
    • Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane
    • Lee S., Lee A., Chen J., and MacKinnon R. Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15441-15446
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15441-15446
    • Lee, S.1    Lee, A.2    Chen, J.3    MacKinnon, R.4
  • 36
    • 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., Meins T., Zeth K., and Kleinschmidt J.H. Correct folding of the beta-barrel of the human membrane protein VDAC requires a lipid bilayer. J. Mol. Biol. 368 (2007) 66-78
    • (2007) J. Mol. Biol. , vol.368 , pp. 66-78
    • Shanmugavadivu, B.1    Apell, H.2    Meins, T.3    Zeth, K.4    Kleinschmidt, J.H.5
  • 37
    • 0038303147 scopus 로고    scopus 로고
    • A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis
    • Zhang H., Kurisu G., Smith J.L., and Cramer W.A. A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5160-5163
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5160-5163
    • Zhang, H.1    Kurisu, G.2    Smith, J.L.3    Cramer, W.A.4
  • 39
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., Campbell E.B., and Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 41
    • 0034633264 scopus 로고    scopus 로고
    • Functionality of a membrane protein in bicelles
    • Czerski L., and Sanders C.R. Functionality of a membrane protein in bicelles. Anal. Biochem. 284 (2000) 327-333
    • (2000) Anal. Biochem. , vol.284 , pp. 327-333
    • Czerski, L.1    Sanders, C.R.2
  • 42
    • 16344376576 scopus 로고    scopus 로고
    • NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system
    • Howell S.C., Mesleh M.F., and Opella S.J. NMR structure determination of a membrane protein with two transmembrane helices in micelles: MerF of the bacterial mercury detoxification system. Biochemistry 44 (2005) 5196-5206
    • (2005) Biochemistry , vol.44 , pp. 5196-5206
    • Howell, S.C.1    Mesleh, M.F.2    Opella, S.J.3
  • 43
    • 33746045690 scopus 로고    scopus 로고
    • Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins
    • Prosser R.S., Evanics F., Kitevski J.L., and Al-Abdul-Wahid M.S. Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins. Biochemistry 45 (2006) 8453-8465
    • (2006) Biochemistry , vol.45 , pp. 8453-8465
    • Prosser, R.S.1    Evanics, F.2    Kitevski, J.L.3    Al-Abdul-Wahid, M.S.4
  • 45
    • 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
    • De Angelis A.A., Howell S.C., Nevzorov A.A., and Opella S.J. 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
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12256-12267
    • De Angelis, A.A.1    Howell, S.C.2    Nevzorov, A.A.3    Opella, S.J.4
  • 47
    • 33749511249 scopus 로고    scopus 로고
    • Three-dimensional structure of the trans-membrane domain of Vpu from HIV-1 in aligned phospholipid bicelles
    • Park S.H., De Angelis A.A., Nevzorov A.A., Wu C.H., and Opella S.J. Three-dimensional structure of the trans-membrane domain of Vpu from HIV-1 in aligned phospholipid bicelles. Biophys. J. 91 (2006) 3032-3042
    • (2006) Biophys. J. , vol.91 , pp. 3032-3042
    • Park, S.H.1    De Angelis, A.A.2    Nevzorov, A.A.3    Wu, C.H.4    Opella, S.J.5
  • 48
    • 34249819355 scopus 로고    scopus 로고
    • Solid-state NMR reveals structural and dynamical properties of a membrane-anchored electron-carrier protein, cytochrome b(5)
    • Dürr U.H.N., Yamamoto K., Im S., Waskell L., and Ramamoorthy A. Solid-state NMR reveals structural and dynamical properties of a membrane-anchored electron-carrier protein, cytochrome b(5). J. Am. Chem. Soc. 129 (2007) 6670-6671
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6670-6671
    • Dürr, U.H.N.1    Yamamoto, K.2    Im, S.3    Waskell, L.4    Ramamoorthy, A.5
  • 49
    • 33947171594 scopus 로고    scopus 로고
    • NMR of membrane proteins in micelles and bilayers: the FXYD family proteins
    • Franzin C.M., Gong X., Thai K., Yu J., and Marassi F.M. NMR of membrane proteins in micelles and bilayers: the FXYD family proteins. Methods 41 (2007) 398-408
    • (2007) Methods , vol.41 , pp. 398-408
    • Franzin, C.M.1    Gong, X.2    Thai, K.3    Yu, J.4    Marassi, F.M.5
  • 50
    • 34447135010 scopus 로고    scopus 로고
    • Structural similarity of a membrane protein in micelles and membranes
    • Franzin C.M., Teriete P., and Marassi F.M. Structural similarity of a membrane protein in micelles and membranes. J. Am. Chem. Soc. 129 (2007) 8078-8079
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8078-8079
    • Franzin, C.M.1    Teriete, P.2    Marassi, F.M.3
  • 51
    • 33846595904 scopus 로고
    • High resolution heteronuclear dipolar solid-state NMR spectroscopy
    • Wu C.H., Ramamoorthy A., and Opella S.J. High resolution heteronuclear dipolar solid-state NMR spectroscopy. J. Magn. Reson., Ser. A 109 (1994) 270-272
    • (1994) J. Magn. Reson., Ser. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 52
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella S.J., and Marassi F.M. 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
  • 55
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora A., Abildgaard F., Bushweller J.H., and Tamm L.K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 8 (2001) 334-338
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 56
    • 14544292475 scopus 로고    scopus 로고
    • NMR structure of Mistic, a membrane-integrating protein for membrane protein expression
    • Roosild T.P., Greenwald J., Vega M., Castronovo S., Riek R., and Choe S. NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science 307 (2005) 1317-1321
    • (2005) Science , vol.307 , pp. 1317-1321
    • Roosild, T.P.1    Greenwald, J.2    Vega, M.3    Castronovo, S.4    Riek, R.5    Choe, S.6
  • 57
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • Oxenoid K., and Chou J.J. The structure of phospholamban pentamer reveals a channel-like architecture in membranes. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 10870-10875
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.J.2
  • 60
    • 1942489643 scopus 로고    scopus 로고
    • A combinatorial selective labeling method for the assignment of backbone amide NMR resonances
    • Parker M.J., Aulton-Jones M., Hounslow A.M., and Craven C.J. A combinatorial selective labeling method for the assignment of backbone amide NMR resonances. J. Am. Chem. Soc. 126 (2004) 5020-5021
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5020-5021
    • Parker, M.J.1    Aulton-Jones, M.2    Hounslow, A.M.3    Craven, C.J.4
  • 61
    • 0038324522 scopus 로고    scopus 로고
    • A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using C-13 spectroscopy
    • Eletsky A., Moreira O., Kovacs H., and Pervushin K. A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using C-13 spectroscopy. J. Biomol. NMR 26 (2003) 167-179
    • (2003) J. Biomol. NMR , vol.26 , pp. 167-179
    • Eletsky, A.1    Moreira, O.2    Kovacs, H.3    Pervushin, K.4
  • 62
    • 34247860719 scopus 로고    scopus 로고
    • Spin-state selective carbon-detected HNCO with TROSY optimization in all dimensions and double echo-antiecho sensitivity enhancement in both indirect dimensions
    • Hu K., Vögeli B., and Clore G.M. Spin-state selective carbon-detected HNCO with TROSY optimization in all dimensions and double echo-antiecho sensitivity enhancement in both indirect dimensions. J. Am. Chem. Soc. 129 (2007) 5484-5491
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5484-5491
    • Hu, K.1    Vögeli, B.2    Clore, G.M.3
  • 63
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 64
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data
    • Battiste J.L., and Wagner G. Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data. Biochemistry 39 (2000) 5355-5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 65
    • 33645472931 scopus 로고    scopus 로고
    • Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy
    • Liang B., Bushweller J.H., and Tamm L.K. Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 4389-4397
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4389-4397
    • Liang, B.1    Bushweller, J.H.2    Tamm, L.K.3
  • 66
    • 28544434796 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex
    • Yu L., Sun C., Song D., Shen J., Xu N., Gunasekera A., Hajduk P.J., and Olejniczak E.T. Nuclear magnetic resonance structural studies of a potassium channel-charybdotoxin complex. Biochemistry 44 (2005) 15834-15841
    • (2005) Biochemistry , vol.44 , pp. 15834-15841
    • Yu, L.1    Sun, C.2    Song, D.3    Shen, J.4    Xu, N.5    Gunasekera, A.6    Hajduk, P.J.7    Olejniczak, E.T.8
  • 67
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution
    • Tolman J.R., Flanagan J.M., Kennedy M.A., and Prestegard J.H. Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 9279-9283
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9279-9283
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 68
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra N., and Bax A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278 (1997) 1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 69
    • 10344256212 scopus 로고    scopus 로고
    • Charged gels as orienting media for measurement of residual dipolar couplings in soluble and integral membrane proteins
    • Cierpicki T., and Bushweller J.H. Charged gels as orienting media for measurement of residual dipolar couplings in soluble and integral membrane proteins. J. Am. Chem. Soc. 126 (2004) 16259-16266
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16259-16266
    • Cierpicki, T.1    Bushweller, J.H.2
  • 70
    • 33744814357 scopus 로고    scopus 로고
    • Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A
    • Cierpicki T., Liang B., Tamm L.K., and Bushweller J.H. Increasing the accuracy of solution NMR structures of membrane proteins by application of residual dipolar couplings. High-resolution structure of outer membrane protein A. J. Am. Chem. Soc. 128 (2006) 6947-6951
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6947-6951
    • Cierpicki, T.1    Liang, B.2    Tamm, L.K.3    Bushweller, J.H.4
  • 71
    • 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
    • Chou J.J., Kaufman J.D., Stahl S.J., Wingfield P.T., and Bax A. Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J. Am. Chem. Soc. 124 (2002) 2450-2451
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 72
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • Chou J.J., Gaemers S., Howder B., Louis J.M., and Bax A. A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles. J. Biomol. NMR 21 (2001) 377-382
    • (2001) J. Biomol. NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 73
    • 0034721465 scopus 로고    scopus 로고
    • Alignment of biopolymers in strained gels: a new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR
    • Tycko R., Blanco F., and Ishii Y. Alignment of biopolymers in strained gels: a new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR. J. Am. Chem. Soc. 122 (2000) 9340-9341
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9340-9341
    • Tycko, R.1    Blanco, F.2    Ishii, Y.3
  • 74
    • 33847254896 scopus 로고    scopus 로고
    • Multiple alignment of membrane proteins for measuring residual dipolar couplings using lanthanide ions bound to a small metal chelator
    • Kamen D.E., Cahill S.M., and Girvin M.E. Multiple alignment of membrane proteins for measuring residual dipolar couplings using lanthanide ions bound to a small metal chelator. J. Am. Chem. Soc. 129 (2007) 1846-1847
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1846-1847
    • Kamen, D.E.1    Cahill, S.M.2    Girvin, M.E.3
  • 75
    • 34249856814 scopus 로고    scopus 로고
    • DNA-nanotube-induced alignment of membrane proteins for NMR structure determination
    • Douglas S.M., Chou J.J., and Shih W.M. DNA-nanotube-induced alignment of membrane proteins for NMR structure determination. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 6644-6648
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6644-6648
    • Douglas, S.M.1    Chou, J.J.2    Shih, W.M.3
  • 76
    • 0034731004 scopus 로고    scopus 로고
    • Lanthanide ion binding to adventitious sites aligns membrane proteins in micelles for solution NMR spectroscopy
    • Veglia G., and Opella S.J. Lanthanide ion binding to adventitious sites aligns membrane proteins in micelles for solution NMR spectroscopy. J. Am. Chem. Soc. 122 (2000) 11733-11734
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11733-11734
    • Veglia, G.1    Opella, S.J.2
  • 77
    • 0034293196 scopus 로고    scopus 로고
    • Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy
    • Ma C., and Opella S.J. Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy. J. Magn. Reson. 146 (2000) 381-384
    • (2000) J. Magn. Reson. , vol.146 , pp. 381-384
    • Ma, C.1    Opella, S.J.2
  • 78
    • 0037174538 scopus 로고    scopus 로고
    • Derivation of structural restraints using a thiol-reactive chelator
    • Dvoretsky A., Gaponenko V., and Rosevear P.R. Derivation of structural restraints using a thiol-reactive chelator. FEBS Lett. 528 (2002) 189-192
    • (2002) FEBS Lett. , vol.528 , pp. 189-192
    • Dvoretsky, A.1    Gaponenko, V.2    Rosevear, P.R.3
  • 80
    • 0037093851 scopus 로고    scopus 로고
    • Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide binding proteins
    • Barbieri R., Bertini I., Cavallaro G., Lee Y., Luchinat C., and Rosato A. Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide binding proteins. J. Am. Chem. Soc. 124 (2002) 5581-5587
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5581-5587
    • Barbieri, R.1    Bertini, I.2    Cavallaro, G.3    Lee, Y.4    Luchinat, C.5    Rosato, A.6
  • 81
    • 33947171595 scopus 로고    scopus 로고
    • Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies
    • Schwarz D., Klammt C., Koglin A., Löhr F., Schneider B., Dötsch V., and Bernhard F. Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies. Methods 41 (2007) 355-369
    • (2007) Methods , vol.41 , pp. 355-369
    • Schwarz, D.1    Klammt, C.2    Koglin, A.3    Löhr, F.4    Schneider, B.5    Dötsch, V.6    Bernhard, F.7
  • 83
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie K.R., Prestegard J.H., and Engelman D.M. A transmembrane helix dimer: structure and implications. Science 276 (1997) 131-133
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 84
    • 0037159196 scopus 로고    scopus 로고
    • Topology and secondary structure of the N-terminal domain of diacylglycerol kinase
    • Oxenoid K., Sönnichsen F.D., and Sanders C.R. Topology and secondary structure of the N-terminal domain of diacylglycerol kinase. Biochemistry 41 (2002) 12876-12882
    • (2002) Biochemistry , vol.41 , pp. 12876-12882
    • Oxenoid, K.1    Sönnichsen, F.D.2    Sanders, C.R.3
  • 85
    • 0035956956 scopus 로고    scopus 로고
    • Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
    • Fernández C., Adeishvili K., and Wüthrich K. Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 2358-2363
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2358-2363
    • Fernández, C.1    Adeishvili, K.2    Wüthrich, K.3
  • 86
    • 33846783122 scopus 로고    scopus 로고
    • A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance
    • Johansson M.U., Alioth S., Hu K., Walser R., Koebnik R., and Pervushin K. A minimal transmembrane beta-barrel platform protein studied by nuclear magnetic resonance. Biochemistry 46 (2007) 1128-1140
    • (2007) Biochemistry , vol.46 , pp. 1128-1140
    • Johansson, M.U.1    Alioth, S.2    Hu, K.3    Walser, R.4    Koebnik, R.5    Pervushin, K.6
  • 88
    • 0037020298 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: resonance assignment of native bacteriorhodopsin
    • Schubert M., Kolbe M., Kessler B., Oesterhelt D., and Schmieder P. Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: resonance assignment of native bacteriorhodopsin. ChemBioChem 3 (2002) 1019-1023
    • (2002) ChemBioChem , vol.3 , pp. 1019-1023
    • Schubert, M.1    Kolbe, M.2    Kessler, B.3    Oesterhelt, D.4    Schmieder, P.5
  • 89
    • 34447500703 scopus 로고    scopus 로고
    • Identification and characterization of the slow-exchanging pH-dependent conformational rearrangement in KcsA
    • Takeuchi K., Takahashi H., Kawano S., and Shimada I. Identification and characterization of the slow-exchanging pH-dependent conformational rearrangement in KcsA. J. Biol. Chem. 282 (2007) 15179-15186
    • (2007) J. Biol. Chem. , vol.282 , pp. 15179-15186
    • Takeuchi, K.1    Takahashi, H.2    Kawano, S.3    Shimada, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.