메뉴 건너뛰기




Volumn 199, Issue 2, 2009, Pages 225-232

High-resolution solid-state NMR of anisotropically mobile molecules under very low-power 1H decoupling and moderate magic-angle spinning

Author keywords

Lipid membranes; Low power decoupling; Membrane peptides; Solid state NMR; Uniaxial diffusion

Indexed keywords

LIPID MEMBRANES; LOW-POWER DECOUPLING; MEMBRANE PEPTIDES; SOLID-STATE NMR; UNIAXIAL DIFFUSION;

EID: 67649446260     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2009.05.006     Document Type: Article
Times cited : (5)

References (31)
  • 1
    • 0001764214 scopus 로고    scopus 로고
    • Low-power decoupling in fast magic-angle spinning NMR
    • Ernst M., Samoson A., and Meier B. Low-power decoupling in fast magic-angle spinning NMR. Chem. Phys. Lett. 348 (2001) 293-302
    • (2001) Chem. Phys. Lett. , vol.348 , pp. 293-302
    • Ernst, M.1    Samoson, A.2    Meier, B.3
  • 2
    • 0042530514 scopus 로고    scopus 로고
    • Low-power XiX decoupling in MAS NMR experiments
    • Ernst M., Samoson A., and Meier B. Low-power XiX decoupling in MAS NMR experiments. J. Magn. Reson. 163 (2003) 332-339
    • (2003) J. Magn. Reson. , vol.163 , pp. 332-339
    • Ernst, M.1    Samoson, A.2    Meier, B.3
  • 3
    • 1842863045 scopus 로고    scopus 로고
    • Low-power high-resolution solid-state NMR of peptides and proteins
    • Ernst M., Meier M., Tuherm T., Samoson A., and Meier B. Low-power high-resolution solid-state NMR of peptides and proteins. J. Am. Chem. Soc. 126 (2004) 4764-4765
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4764-4765
    • Ernst, M.1    Meier, M.2    Tuherm, T.3    Samoson, A.4    Meier, B.5
  • 4
    • 25144475562 scopus 로고    scopus 로고
    • Heteronuclear decoupling under fast MAS by a rotor-synchronized Hahn-echo pulse train
    • Filip X., Tripon C., and Filip C. Heteronuclear decoupling under fast MAS by a rotor-synchronized Hahn-echo pulse train. J. Magn. Reson. 176 (2005) 239-243
    • (2005) J. Magn. Reson. , vol.176 , pp. 239-243
    • Filip, X.1    Tripon, C.2    Filip, C.3
  • 5
    • 38849197930 scopus 로고    scopus 로고
    • Efficient low-power heteronuclear decoupling in 13C high-resolution solid-state NMR under fast magic angle spinning
    • Kotecha M., Wickramasinghe N.P., and Ishii Y. Efficient low-power heteronuclear decoupling in 13C high-resolution solid-state NMR under fast magic angle spinning. Magn. Reson. Chem. 45 (2007) S221-S230
    • (2007) Magn. Reson. Chem. , vol.45
    • Kotecha, M.1    Wickramasinghe, N.P.2    Ishii, Y.3
  • 6
    • 0000785903 scopus 로고
    • Rotary resonance recoupling of dipolar interactions in solid-state NMR spectroscopy
    • Oas T.G., Griffin R.G., and Levitt M.H. Rotary resonance recoupling of dipolar interactions in solid-state NMR spectroscopy. J. Chem. Phys. 89 (1988) 692-695
    • (1988) J. Chem. Phys. , vol.89 , pp. 692-695
    • Oas, T.G.1    Griffin, R.G.2    Levitt, M.H.3
  • 8
    • 0031466742 scopus 로고    scopus 로고
    • High-resolution magic-angle spinning 1H nuclear magnetic resonance studies of lipid dispersions using spherical glass ampoules
    • Zhou Z., Sayer B.G., Stark R.E., and Epand R.M. High-resolution magic-angle spinning 1H nuclear magnetic resonance studies of lipid dispersions using spherical glass ampoules. Chem. Phys. Lipids 90 (1997) 45-53
    • (1997) Chem. Phys. Lipids , vol.90 , pp. 45-53
    • Zhou, Z.1    Sayer, B.G.2    Stark, R.E.3    Epand, R.M.4
  • 9
    • 0028859424 scopus 로고
    • High-speed magic angle spinning solid-state 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers
    • Brouchard M., Davis J., and Auger M. High-speed magic angle spinning solid-state 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers. Biophys. J. 69 (1995) 1933-1938
    • (1995) Biophys. J. , vol.69 , pp. 1933-1938
    • Brouchard, M.1    Davis, J.2    Auger, M.3
  • 10
    • 0028970552 scopus 로고
    • High-resolution 1H nuclear magnetic resonance of a transmembrane peptide
    • Davis J., Auger M., and Hodges R. High-resolution 1H nuclear magnetic resonance of a transmembrane peptide. Biophys. J. 69 (1995) 1917-1932
    • (1995) Biophys. J. , vol.69 , pp. 1917-1932
    • Davis, J.1    Auger, M.2    Hodges, R.3
  • 11
    • 0344033630 scopus 로고    scopus 로고
    • Detection of natural abundance 1H-13C correlations of cholesterol in its membrane environment using a gradient enhanced HSQC experiment under high resolution magic angle spinning
    • Soubias O., Piotto M., Saurel O., Assemat O., Reat V., and Milon A. Detection of natural abundance 1H-13C correlations of cholesterol in its membrane environment using a gradient enhanced HSQC experiment under high resolution magic angle spinning. J. Magn. Reson. 165 (2003) 303-308
    • (2003) J. Magn. Reson. , vol.165 , pp. 303-308
    • Soubias, O.1    Piotto, M.2    Saurel, O.3    Assemat, O.4    Reat, V.5    Milon, A.6
  • 12
    • 0037174081 scopus 로고    scopus 로고
    • 15N, 1H heteronuclear correlation NMR of gramicidin A in DMPC-d67
    • Fares C., Sharom F., and Davis J. 15N, 1H heteronuclear correlation NMR of gramicidin A in DMPC-d67. J. Am. Chem. Soc. 124 (2002) 11232-11233
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11232-11233
    • Fares, C.1    Sharom, F.2    Davis, J.3
  • 13
    • 0028181687 scopus 로고
    • Influenza A virus M2 ion channel protein: a structure-function analysis
    • Holsinger L.J., Nichani D., Pinto L.H., and Lamb R.A. Influenza A virus M2 ion channel protein: a structure-function analysis. J. Virol. 68 (1994) 1551-1563
    • (1994) J. Virol. , vol.68 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 14
    • 34247847729 scopus 로고    scopus 로고
    • Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: a 2H, 13C, and 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle
    • Cady S.D., Goodman C., Tatko C., DeGrado W.F., and Hong M. Determining the orientation of uniaxially rotating membrane proteins using unoriented samples: a 2H, 13C, and 15N 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.3    DeGrado, W.F.4    Hong, M.5
  • 15
    • 58149345493 scopus 로고    scopus 로고
    • Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantidine binding
    • Cady S., Mishanina T., and Hong M. Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantidine binding. J. Mol. Biol. 385 (2009) 1127-1141
    • (2009) J. Mol. Biol. , vol.385 , pp. 1127-1141
    • Cady, S.1    Mishanina, T.2    Hong, M.3
  • 16
    • 40349105892 scopus 로고    scopus 로고
    • Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel
    • Cady S.D., and Hong M. Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proc. Natl. Acad. Sci. USA 105 (2008) 1483-1488
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1483-1488
    • Cady, S.D.1    Hong, M.2
  • 17
    • 48749147783 scopus 로고
    • An improved sequence for broadband decoupling: WALTZ-16
    • Shaka A.J., Keeler J., Frenkiel T., and Freeman R. An improved sequence for broadband decoupling: WALTZ-16. J. Magn. Reson. 52 (1983) 335-338
    • (1983) J. Magn. Reson. , vol.52 , pp. 335-338
    • Shaka, A.J.1    Keeler, J.2    Frenkiel, T.3    Freeman, R.4
  • 19
    • 0028785466 scopus 로고
    • Study of phospholipid structure by 1H, 13C, and 31P dipolar couplings from 2D NMR
    • Hong M., Schmidt-Rohr K., and Nanz D. Study of phospholipid structure by 1H, 13C, and 31P dipolar couplings from 2D NMR. Biophys. J. 69 (1995) 1939-1950
    • (1995) Biophys. J. , vol.69 , pp. 1939-1950
    • Hong, M.1    Schmidt-Rohr, K.2    Nanz, D.3
  • 20
    • 0029274597 scopus 로고
    • NMR measurement of signs and magnitudes of C-H dipolar couplings in lecithin
    • Hong M., Schmidt-Rohr K., and Pines A. NMR measurement of signs and magnitudes of C-H dipolar couplings in lecithin. J. Am. Chem. Soc. 117 (1995) 3310-3311
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3310-3311
    • Hong, M.1    Schmidt-Rohr, K.2    Pines, A.3
  • 21
    • 0031989985 scopus 로고    scopus 로고
    • High-speed magic-angle spinning 13C MAS NMR spectra of adamantane: self-decoupling of the heteronuclear scalar interaction and proton spin diffusion
    • Ernst M., Verhoeven A., and Meier B.H. High-speed magic-angle spinning 13C MAS NMR spectra of adamantane: self-decoupling of the heteronuclear scalar interaction and proton spin diffusion. J. Magn. Reson. 130 (1998) 176-185
    • (1998) J. Magn. Reson. , vol.130 , pp. 176-185
    • Ernst, M.1    Verhoeven, A.2    Meier, B.H.3
  • 22
    • 0027788047 scopus 로고
    • A 13C and 2H nuclear magnetic resonance study of phosphatidylcholine/cholesterol interactions: characterization of liquid-gel phases
    • Huang T.-H., Lee C.W.B., Des Gupta S.K., Blume A., and Griffin R.G. A 13C and 2H nuclear magnetic resonance study of phosphatidylcholine/cholesterol interactions: characterization of liquid-gel phases. Biochemistry 32 (1993) 13277-13287
    • (1993) Biochemistry , vol.32 , pp. 13277-13287
    • Huang, T.-H.1    Lee, C.W.B.2    Des Gupta, S.K.3    Blume, A.4    Griffin, R.G.5
  • 23
    • 0029047470 scopus 로고
    • Molecular order and dynamics of phosphatidylcholine bilayer membranes in the presence of cholesterol, ergosterol and lanosterol: a comparative study using 2H-, 13C- and 31P-NMR spectroscopy
    • Urbina J., Pekerar S., Le H., Patterson J., Montez B., and Oldfield E. Molecular order and dynamics of phosphatidylcholine bilayer membranes in the presence of cholesterol, ergosterol and lanosterol: a comparative study using 2H-, 13C- and 31P-NMR spectroscopy. Biochim. Biophys. Acta 1238 (1995) 163-176
    • (1995) Biochim. Biophys. Acta , vol.1238 , pp. 163-176
    • Urbina, J.1    Pekerar, S.2    Le, H.3    Patterson, J.4    Montez, B.5    Oldfield, E.6
  • 24
    • 33750935291 scopus 로고    scopus 로고
    • Orientation determination of membrane-disruptive proteins using powder samples and rotational diffusion: a simple solid-state NMR approach
    • Hong M., and Doherty T. Orientation determination of membrane-disruptive proteins using powder samples and rotational diffusion: a simple solid-state NMR approach. Chem. Phys. Lett. 432 (2006) 296-300
    • (2006) Chem. Phys. Lett. , vol.432 , pp. 296-300
    • Hong, M.1    Doherty, T.2
  • 25
    • 11444256357 scopus 로고    scopus 로고
    • Investigations of polypeptide rotational diffusion in aligned membranes by 2H and 15N solid-state NMR spectroscopy
    • Aisenbrey C., and Bechinger B. Investigations of polypeptide rotational diffusion in aligned membranes by 2H and 15N solid-state NMR spectroscopy. J. Am. Chem. Soc. 126 (2004) 16676-16683
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16676-16683
    • Aisenbrey, C.1    Bechinger, B.2
  • 26
    • 0021952593 scopus 로고
    • NMR structural analysis of a membrane protein: bacteriorhodopsin peptide backbone orientation and motion
    • Lewis B.A., Harbison G.S., Herzfeld J., and Griffin R.G. NMR structural analysis of a membrane protein: bacteriorhodopsin peptide backbone orientation and motion. Biochemistry 24 (1985) 4671-4679
    • (1985) Biochemistry , vol.24 , pp. 4671-4679
    • Lewis, B.A.1    Harbison, G.S.2    Herzfeld, J.3    Griffin, R.G.4
  • 27
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza A and B viruses
    • Pinto L.H., and Lamb R.A. The M2 proton channels of influenza A and B viruses. J. Biol. Chem. 281 (2006) 8997-9000
    • (2006) J. Biol. Chem. , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 28
    • 0030973121 scopus 로고    scopus 로고
    • The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer
    • Sakaguchi T., Tu Q., Pinto L.H., and Lamb R.A. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer. Proc. Natl. Acad. Sci. USA 94 (1997) 5000-5005
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5000-5005
    • Sakaguchi, T.1    Tu, Q.2    Pinto, L.H.3    Lamb, R.A.4
  • 29
    • 33744941313 scopus 로고    scopus 로고
    • Determination of the oligomeric number and intermolecular distances of membrane protein assemblies by anisotropic 1H-driven spin diffusion NMR spectroscopy
    • Luo W., and Hong M. Determination of the oligomeric number and intermolecular distances of membrane protein assemblies by anisotropic 1H-driven spin diffusion NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 7242-7251
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7242-7251
    • Luo, W.1    Hong, M.2
  • 30
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus
    • Hu J., Asbury T., Achuthan S., Li C., Bertram R., Quine J.R., Fu R., and Cross T.A. Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus. Biophys. J. 92 (2007) 4335-4343
    • (2007) Biophys. J. , vol.92 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Achuthan, S.3    Li, C.4    Bertram, R.5    Quine, J.R.6    Fu, R.7    Cross, T.A.8
  • 31
    • 9644266958 scopus 로고    scopus 로고
    • Understanding sterol-membrane interactions, part II: complete 1H and 13C assignments by solid-state NMR spectroscopy and determination of the hydrogen-bonding partners of cholesterol in a lipid bilayer
    • Soubias O., Jolibois F., Reat V., and Milon A. Understanding sterol-membrane interactions, part II: complete 1H and 13C assignments by solid-state NMR spectroscopy and determination of the hydrogen-bonding partners of cholesterol in a lipid bilayer. Chem. Eur. J. 10 (2004) 6005-6014
    • (2004) Chem. Eur. J. , vol.10 , pp. 6005-6014
    • Soubias, O.1    Jolibois, F.2    Reat, V.3    Milon, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.