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Volumn 198, Issue 1, 2009, Pages 1-7

Determining the helical tilt of membrane peptides using electron paramagnetic resonance spectroscopy

Author keywords

Alignment; EPR; Membrane protein

Indexed keywords

ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPIES; EPR; EPR SPECTRUM; HELICAL AXIS; HELICAL MEMBRANES; HELICAL MOTIONS; HYPERFINE SPLITTING; MEMBRANE PEPTIDES; MEMBRANE PROTEIN; PERIODIC VARIATIONS; SPIN LABELS; THEORETICAL CALCULATIONS; TILT ANGLES;

EID: 63349105151     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2008.12.007     Document Type: Article
Times cited : (11)

References (37)
  • 3
    • 0034636180 scopus 로고    scopus 로고
    • Mapping the oligomeric interface of diacylglycerol kinase by engineered thiol cross-linking: homologous sites in the transmembrane domain
    • Nagy J.K., Lau F.W., Bowie J.U., and Sanders C.R. Mapping the oligomeric interface of diacylglycerol kinase by engineered thiol cross-linking: homologous sites in the transmembrane domain. Biochemistry 39 (2000) 4154-4164
    • (2000) Biochemistry , vol.39 , pp. 4154-4164
    • Nagy, J.K.1    Lau, F.W.2    Bowie, J.U.3    Sanders, C.R.4
  • 7
    • 0036086351 scopus 로고    scopus 로고
    • The alpha-helix and the organization and gating of channels
    • Spencer R.H., and Rees D.C. The alpha-helix and the organization and gating of channels. Ann. Rev. Biophys. Biomol. Struct. 31 (2002) 207-233
    • (2002) Ann. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 207-233
    • Spencer, R.H.1    Rees, D.C.2
  • 8
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 angstrom resolution
    • Zhou Y.F., 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 angstrom resolution. Nature 414 (2001) 43-48
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.F.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 11
    • 0028921479 scopus 로고
    • Acetylcholine-receptor channel imaged in the open state
    • Unwin N. Acetylcholine-receptor channel imaged in the open state. Nature 373 (1995) 37-43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 12
    • 0034806920 scopus 로고    scopus 로고
    • Magnetically aligned phospholipid bilayers at the parallel and perpendicular orientations for X-band spin-label EPR studies
    • Cardon T.B., Tiburu E.K., Padmanabhan A., Howard K.P., and Lorigan G.A. Magnetically aligned phospholipid bilayers at the parallel and perpendicular orientations for X-band spin-label EPR studies. J. Am. Chem. Soc. 123 (2001) 2913-2914
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2913-2914
    • Cardon, T.B.1    Tiburu, E.K.2    Padmanabhan, A.3    Howard, K.P.4    Lorigan, G.A.5
  • 13
    • 0033531682 scopus 로고    scopus 로고
    • Magnetically oriented phospholipid bilayers for spin label EPR studies
    • Garber S.M., Lorigan G.A., and Howard K.P. Magnetically oriented phospholipid bilayers for spin label EPR studies. J. Am. Chem. Soc. 121 (1999) 3240-3241
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3240-3241
    • Garber, S.M.1    Lorigan, G.A.2    Howard, K.P.3
  • 14
  • 15
    • 34347252219 scopus 로고    scopus 로고
    • Determining the helical tilt angle of a transmembrane helix in mechanically aligned lipid bilayers using EPR spectroscopy
    • Inbaraj J.J., Laryukhin M., and Lorigan G.A. Determining the helical tilt angle of a transmembrane helix in mechanically aligned lipid bilayers using EPR spectroscopy. J Am. Chem. Soc. 129 (2007) 7710-7711
    • (2007) J Am. Chem. Soc. , vol.129 , pp. 7710-7711
    • Inbaraj, J.J.1    Laryukhin, M.2    Lorigan, G.A.3
  • 16
    • 0034718082 scopus 로고    scopus 로고
    • Spectroscopic characterization of spin-labeled magnetically oriented phospholipid bilayers by EPR spectroscopy
    • Mangels M.L., Cardon T.B., Harper A.C., Howard K.P., and Lorigan G.A. Spectroscopic characterization of spin-labeled magnetically oriented phospholipid bilayers by EPR spectroscopy. J. Am. Chem. Soc. 122 (2000) 7052-7058
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7052-7058
    • Mangels, M.L.1    Cardon, T.B.2    Harper, A.C.3    Howard, K.P.4    Lorigan, G.A.5
  • 17
    • 34250217114 scopus 로고    scopus 로고
    • Characterization of lipid bilayer formation in aligned nanoporous aluminum oxide nanotube arrays
    • Karp E.S., Newstadt J.P., Chu S., and Lorigan G.A. Characterization of lipid bilayer formation in aligned nanoporous aluminum oxide nanotube arrays. J. Magn. Reson. 187 (2007) 112-119
    • (2007) J. Magn. Reson. , vol.187 , pp. 112-119
    • Karp, E.S.1    Newstadt, J.P.2    Chu, S.3    Lorigan, G.A.4
  • 18
    • 33750707584 scopus 로고    scopus 로고
    • Phospholamban and its phosphorylated form interact differently with lipid bilayers: A P-31, H-2, and C-13 solid-state NMR spectroscopic study
    • Abu-Baker S., and Lorigan G.A. Phospholamban and its phosphorylated form interact differently with lipid bilayers: A P-31, H-2, and C-13 solid-state NMR spectroscopic study. Biochemistry 45 (2006) 13312-13322
    • (2006) Biochemistry , vol.45 , pp. 13312-13322
    • Abu-Baker, S.1    Lorigan, G.A.2
  • 19
    • 3543102159 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays
    • Lorigan G.A., Dave P.C., Tiburu E.K., Damodaran K., Abu-Baker S., Karp E.S., Gibbons W.J., and Minto R.E. Solid-state NMR spectroscopic studies of an integral membrane protein inserted into aligned phospholipid bilayer nanotube arrays. J. Am. Chem. Soc. 126 (2004) 9504-9505
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9504-9505
    • Lorigan, G.A.1    Dave, P.C.2    Tiburu, E.K.3    Damodaran, K.4    Abu-Baker, S.5    Karp, E.S.6    Gibbons, W.J.7    Minto, R.E.8
  • 20
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane protein structure and topology
    • Marassi F.M., and Opella S.J. A solid-state NMR index of helical membrane protein structure and topology. J. Magn. Reson. 144 (2000) 150-155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 21
    • 35649016222 scopus 로고    scopus 로고
    • The structural topology of wild-type phospholamban in oriented lipid bilayers using N-15 solid-state NMR spectroscopy
    • Abu-Baker S., Lu J.X., Chu S., Shetty K.K., Gor'kov P.L., and Lorigan G.A. The structural topology of wild-type phospholamban in oriented lipid bilayers using N-15 solid-state NMR spectroscopy. Protein Sci. 16 (2007) 2345-2349
    • (2007) Protein Sci. , vol.16 , pp. 2345-2349
    • Abu-Baker, S.1    Lu, J.X.2    Chu, S.3    Shetty, K.K.4    Gor'kov, P.L.5    Lorigan, G.A.6
  • 22
    • 33748758458 scopus 로고    scopus 로고
    • Electron paramagnetic resonance studies of an integral membrane peptide inserted into aligned phospholipid bilayer nanotube arrays
    • Karp E.S., Inbaraj J.J., Laryukhin M., and Lorigan G.A. Electron paramagnetic resonance studies of an integral membrane peptide inserted into aligned phospholipid bilayer nanotube arrays. J. Am. Chem. Soc. 128 (2006) 12070-12071
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12070-12071
    • Karp, E.S.1    Inbaraj, J.J.2    Laryukhin, M.3    Lorigan, G.A.4
  • 25
    • 0034191459 scopus 로고    scopus 로고
    • TOAC: a useful C-alpha-tetrasubstituted alpha-amino acid for peptide conformational analysis by CD spectroscopy in the visible region. Part I
    • Bui T.T.T., Formaggio F., Crisma M., Monaco V., Toniolo C., Hussain R., and Siligardi G. TOAC: a useful C-alpha-tetrasubstituted alpha-amino acid for peptide conformational analysis by CD spectroscopy in the visible region. Part I. J. Chem. Soc. Perkin. Trans. 2 5 (2000) 1043-1046
    • (2000) J. Chem. Soc. Perkin. Trans. 2 , vol.5 , pp. 1043-1046
    • Bui, T.T.T.1    Formaggio, F.2    Crisma, M.3    Monaco, V.4    Toniolo, C.5    Hussain, R.6    Siligardi, G.7
  • 26
    • 0029938988 scopus 로고    scopus 로고
    • Crystallographic characterization of geometry and conformation of TOAC, a nitroxide spin-labelled C(alpha,alpha)-disubstituted glycine, in simple derivatives and model peptides
    • Flippen-Anderson J.L., George C., Valle G., Valente E., Bianco A., Formaggio F., Crisma M., and Toniolo C. Crystallographic characterization of geometry and conformation of TOAC, a nitroxide spin-labelled C(alpha,alpha)-disubstituted glycine, in simple derivatives and model peptides. Int. J. Peptide Protein Res. 47 (1996) 231-238
    • (1996) Int. J. Peptide Protein Res. , vol.47 , pp. 231-238
    • Flippen-Anderson, J.L.1    George, C.2    Valle, G.3    Valente, E.4    Bianco, A.5    Formaggio, F.6    Crisma, M.7    Toniolo, C.8
  • 27
    • 0037048672 scopus 로고    scopus 로고
    • Dap-SL: a new site-directed nitroxide spin labeling approach for determining structure and motions in synthesized peptides and proteins
    • McNulty J.C., Thompson D.A., Carrasco M.R., and Millhauser G.L. Dap-SL: a new site-directed nitroxide spin labeling approach for determining structure and motions in synthesized peptides and proteins. FEBS Lett. 529 (2002) 243-248
    • (2002) FEBS Lett. , vol.529 , pp. 243-248
    • McNulty, J.C.1    Thompson, D.A.2    Carrasco, M.R.3    Millhauser, G.L.4
  • 29
    • 0002844265 scopus 로고
    • Theory of slow tumbling ESR spectra for nitroxides
    • Berliner L.J. (Ed), Academic Press, New York
    • Freed J.H. Theory of slow tumbling ESR spectra for nitroxides. In: Berliner L.J. (Ed). Spin Labeling Theory and Applications (1976), Academic Press, New York 53-130
    • (1976) Spin Labeling Theory and Applications , pp. 53-130
    • Freed, J.H.1
  • 30
    • 52449112128 scopus 로고    scopus 로고
    • Extended model free approach to analyze correlation functions of multidomain proteins in the presence of motional coupling
    • Chen K., and Tjandra N. Extended model free approach to analyze correlation functions of multidomain proteins in the presence of motional coupling. J. Am. Chem. Soc. 130 (2008) 12745-12751
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12745-12751
    • Chen, K.1    Tjandra, N.2
  • 31
    • 15844395368 scopus 로고    scopus 로고
    • Periodicity, planarity, residual dipolar coupling, and structures
    • Walsh J.D., Kuszweski J., and Wang Y.X. Periodicity, planarity, residual dipolar coupling, and structures. J. Magn. Reson. 174 (2005) 152-162
    • (2005) J. Magn. Reson. , vol.174 , pp. 152-162
    • Walsh, J.D.1    Kuszweski, J.2    Wang, Y.X.3
  • 33
    • 34247847729 scopus 로고    scopus 로고
    • Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: A H-2, C-13, and N-15 solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle
    • Cady S.D., Goodman C., Tatko C.D., DeGrado W.F., and Hong M. Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: A H-2, C-13, and N-15 solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle. J. Am. Chem. Soc. 129 (2007) 5719-5729
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5719-5729
    • Cady, S.D.1    Goodman, C.2    Tatko, C.D.3    DeGrado, W.F.4    Hong, M.5
  • 34
    • 0036298936 scopus 로고    scopus 로고
    • A robust technique for two-dimensional separation of undistorted chemical-shift anisotropy powder patterns in magic-angle-spinning NMR
    • Liu S.F., Mao J.D., and Schmidt-Rohr K. A robust technique for two-dimensional separation of undistorted chemical-shift anisotropy powder patterns in magic-angle-spinning NMR. J. Magn. Reson. 155 (2002) 15-28
    • (2002) J. Magn. Reson. , vol.155 , pp. 15-28
    • Liu, S.F.1    Mao, J.D.2    Schmidt-Rohr, K.3
  • 35
    • 0000782602 scopus 로고
    • Determination of chemical-shift-anisotropy lineshapes in a two-dimensional-magic-angle-spinning NMR experiment
    • Tycko R., Dabbagh G., and Mirau P.A. Determination of chemical-shift-anisotropy lineshapes in a two-dimensional-magic-angle-spinning NMR experiment. J. Magn. Reson. 85 (1989) 265-274
    • (1989) J. Magn. Reson. , vol.85 , pp. 265-274
    • Tycko, R.1    Dabbagh, G.2    Mirau, P.A.3
  • 36
    • 43049088174 scopus 로고    scopus 로고
    • Transmembrane helix uniformity examined by spectral mapping of torsion angles
    • Page R.C., Sanguk K., and Cross T.A. Transmembrane helix uniformity examined by spectral mapping of torsion angles. Structure 16 (2008) 787-797
    • (2008) Structure , vol.16 , pp. 787-797
    • Page, R.C.1    Sanguk, K.2    Cross, T.A.3


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