메뉴 건너뛰기




Volumn 89, Issue 2, 2005, Pages 1120-1131

Determination of the orientation and dynamics of ergosterol in model membranes using uniform 13C labeling and dynamically averaged 13C chemical shift anisotropies as experimental restraints

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; DEUTERIUM; ERGOSTEROL; PROTON;

EID: 23244440382     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.059857     Document Type: Article
Times cited : (20)

References (76)
  • 1
    • 0003100206 scopus 로고
    • P. L. Yeagle, editor. Academic Publishers, Boca Raton, FL
    • Dahl, C., and J. Dahl. 1988. Biology of Cholesterol. P. L. Yeagle, editor. Academic Publishers, Boca Raton, FL. 147-172.
    • (1988) Biology of Cholesterol , pp. 147-172
    • Dahl, C.1    Dahl, J.2
  • 2
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle, P. L. 1985. Cholesterol and the cell membrane. Biochim. Biophys. Acta. 822:267-287.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 3
    • 0028936690 scopus 로고
    • Biochemical and physiological effects of sterol alterations in yeast - A review
    • Parks, L. W., S. J. Smith, and J. H. Crowley. 1995. Biochemical and physiological effects of sterol alterations in yeast - a review. Lipids. 30:227-230.
    • (1995) Lipids , vol.30 , pp. 227-230
    • Parks, L.W.1    Smith, S.J.2    Crowley, J.H.3
  • 4
    • 0033385497 scopus 로고    scopus 로고
    • Use of sterol mutants as probes for sterol functions in the yeast, Saccharomyces cerevisiae
    • Parks, L. W., J. H. Crowley, F. W. Leak, S. J. Smith, and M. E. Tomeo. 1999. Use of sterol mutants as probes for sterol functions in the yeast, Saccharomyces cerevisiae. Crit. Rev. Biochem. Mol. Biol. 34:399-404.
    • (1999) Crit. Rev. Biochem. Mol. Biol. , vol.34 , pp. 399-404
    • Parks, L.W.1    Crowley, J.H.2    Leak, F.W.3    Smith, S.J.4    Tomeo, M.E.5
  • 6
    • 0014464329 scopus 로고
    • The interaction energies of cholesterol and lecithin in spread mixed monolayers at the air-water interface
    • Joos, P., and R. A. Demel. 1969. The interaction energies of cholesterol and lecithin in spread mixed monolayers at the air-water interface. Biochim. Biophys. Acta. 183:447-457.
    • (1969) Biochim. Biophys. Acta , vol.183 , pp. 447-457
    • Joos, P.1    Demel, R.A.2
  • 7
    • 0031660245 scopus 로고    scopus 로고
    • Plant sterols: A neutron diffraction study of sitosterol and stigmasterol in soybean phosphatidylcholine membranes
    • Marsan, M. P., E. Bellet-Amalric, I. Muller, G. Zaccai, and A. Milon. 1998. Plant sterols: a neutron diffraction study of sitosterol and stigmasterol in soybean phosphatidylcholine membranes. Biophys. Chem. 75:45-55.
    • (1998) Biophys. Chem. , vol.75 , pp. 45-55
    • Marsan, M.P.1    Bellet-Amalric, E.2    Muller, I.3    Zaccai, G.4    Milon, A.5
  • 8
    • 0028100636 scopus 로고
    • Cholesterol's interfacial interactions with sphingomyelins and phosphatidylcholines: Hydrocarbon chain structure determines the magnitude of condensation
    • Smaby, J. M., H. L. Brockman, and R. E. Brown. 1994. Cholesterol's interfacial interactions with sphingomyelins and phosphatidylcholines: hydrocarbon chain structure determines the magnitude of condensation. Biochemistry. 33:9135-9142.
    • (1994) Biochemistry , vol.33 , pp. 9135-9142
    • Smaby, J.M.1    Brockman, H.L.2    Brown, R.E.3
  • 9
    • 0017008120 scopus 로고
    • A deuterium nuclear magnetic resonance study of the condensing effect of cholesterol on egg phosphatidylcholine bilayer membranes. I. Perdeuterated fatty acid probes
    • Stockton, G. W., and I. C. Smith. 1976. A deuterium nuclear magnetic resonance study of the condensing effect of cholesterol on egg phosphatidylcholine bilayer membranes. I. Perdeuterated fatty acid probes. Chem. Phys. Lipids. 17:251-263.
    • (1976) Chem. Phys. Lipids , vol.17 , pp. 251-263
    • Stockton, G.W.1    Smith, I.C.2
  • 10
    • 0017192580 scopus 로고
    • The function of sterols in membranes
    • Demel, R. A., and B. De Kruyff. 1976. The function of sterols in membranes. Biochim. Biophys. Acta. 457:109-132.
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 109-132
    • Demel, R.A.1    De Kruyff, B.2
  • 11
    • 0018791545 scopus 로고
    • Permeability properties of sterol-containing liposomes from analogues of phosphatidylcholine-lacking acyl groups
    • Clejan, S., R. Bittman, P. W. Deroo, Y. A. Isaacson, and A. F. Rosenthal. 1979. Permeability properties of sterol-containing liposomes from analogues of phosphatidylcholine-lacking acyl groups. Biochemistry. 18:2118-2125.
    • (1979) Biochemistry , vol.18 , pp. 2118-2125
    • Clejan, S.1    Bittman, R.2    Deroo, P.W.3    Isaacson, Y.A.4    Rosenthal, A.F.5
  • 12
    • 0025835715 scopus 로고
    • Differential effects of plant sterols on water permeability and on acyl chain ordering of soybean phosphatidylcholine bilayers
    • Schuler, I., A. Milon, Y. Nakatani, G. Ourisson, A. M. Albrecht, P. Benveniste, and M. A. Hartmann. 1991. Differential effects of plant sterols on water permeability and on acyl chain ordering of soybean phosphatidylcholine bilayers. Proc. Natl. Acad. Sci. USA. 88:6926-6930.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6926-6930
    • Schuler, I.1    Milon, A.2    Nakatani, Y.3    Ourisson, G.4    Albrecht, A.M.5    Benveniste, P.6    Hartmann, M.A.7
  • 13
    • 0029195996 scopus 로고
    • Time and distance scales of membrane domain organization
    • Bloom, M., and J. L. Thewait. 1995. Time and distance scales of membrane domain organization. Mol. Membr. Biol. 12:9-13.
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 9-13
    • Bloom, M.1    Thewait, J.L.2
  • 14
    • 0018803817 scopus 로고
    • Lipid lateral diffusion by pulsed nuclear magnetic resonance
    • Kuo, A. L., and C. G. Wade. 1979. Lipid lateral diffusion by pulsed nuclear magnetic resonance. Biochemistry. 18:2300-2308.
    • (1979) Biochemistry , vol.18 , pp. 2300-2308
    • Kuo, A.L.1    Wade, C.G.2
  • 15
    • 0036840281 scopus 로고    scopus 로고
    • Lateral diffusion of cholesterol and dimyristoylphosphatidylcholine in a lipid bilayer measured by pulsed field gradient NMR spectroscopy
    • Oradd, G., G. Lindblom, and P. W. Westerman. 2002. Lateral diffusion of cholesterol and dimyristoylphosphatidylcholine in a lipid bilayer measured by pulsed field gradient NMR spectroscopy. Biophys. J. 83:2702-2704.
    • (2002) Biophys. J. , vol.83 , pp. 2702-2704
    • Oradd, G.1    Lindblom, G.2    Westerman, P.W.3
  • 16
    • 0037962802 scopus 로고    scopus 로고
    • The effect of cholesterol on the lateral diffusion of phospholipids in oriented bilayers
    • Filippov, A., G. Oradd, and G. Lindblom. 2003. The effect of cholesterol on the lateral diffusion of phospholipids in oriented bilayers. Biophys. J. 84:3079-3086.
    • (2003) Biophys. J. , vol.84 , pp. 3079-3086
    • Filippov, A.1    Oradd, G.2    Lindblom, G.3
  • 17
    • 0018338906 scopus 로고
    • Lateral diffusion in binary mixtures of cholesterol and phosphatidylcholines
    • Rubenstein, J. L., B. A. Smith, and H. M. McConnell. 1979. Lateral diffusion in binary mixtures of cholesterol and phosphatidylcholines. Proc. Natl. Acad. Sci. USA. 76:15-18.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 15-18
    • Rubenstein, J.L.1    Smith, B.A.2    McConnell, H.M.3
  • 18
    • 0025128695 scopus 로고
    • Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H nuclear magnetic resonance and differential scanning calorimetry
    • Vist, M. R., and J. H. Davis. 1990. Phase equilibria of cholesterol/dipalmitoylphosphatidylcholine mixtures: 2H nuclear magnetic resonance and differential scanning calorimetry. Biochemistry. 29:451-464.
    • (1990) Biochemistry , vol.29 , pp. 451-464
    • Vist, M.R.1    Davis, J.H.2
  • 19
    • 0027788047 scopus 로고
    • A 13C and 2H nuclear magnetic resonance study of phosphatidylcholine/ cholesterol interactions: Characterization of liquid-gel phases
    • Huang, T. H., C. W. Lee, S. K. Das Gupta, A. Blume, and R. G. Griffin. 1993. A 13C and 2H nuclear magnetic resonance study of phosphatidylcholine/ cholesterol interactions: characterization of liquid-gel phases. Biochemistry. 32:13277-13287.
    • (1993) Biochemistry , vol.32 , pp. 13277-13287
    • Huang, T.H.1    Lee, C.W.2    Das Gupta, S.K.3    Blume, A.4    Griffin, R.G.5
  • 20
    • 0027506564 scopus 로고
    • Differential scanning calorimetric study of the effect of cholesterol on the thermotropic phase behavior of a homologous series of linear saturated phosphatidylcholines
    • McMullen, T. P., R. N. Lewis, and R. N. McElhaney. 1993. Differential scanning calorimetric study of the effect of cholesterol on the thermotropic phase behavior of a homologous series of linear saturated phosphatidylcholines. Biochemistry. 32:516-522.
    • (1993) Biochemistry , vol.32 , pp. 516-522
    • McMullen, T.P.1    Lewis, R.N.2    McElhaney, R.N.3
  • 21
    • 0030971833 scopus 로고    scopus 로고
    • Differential scanning calorimetric studies of the interaction of cholesterol with distearoyl and dielaidoyl molecular species of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine
    • McMullen, T. P., and R. N. McElhaney. 1997. Differential scanning calorimetric studies of the interaction of cholesterol with distearoyl and dielaidoyl molecular species of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine. Biochemistry. 36:4979-4986.
    • (1997) Biochemistry , vol.36 , pp. 4979-4986
    • McMullen, T.P.1    McElhaney, R.N.2
  • 22
    • 0032946243 scopus 로고    scopus 로고
    • Cholesterol orientation and dynamics in dimyristoylphosphatidylcholine bilayers: A solid state deuterium NMR analysis
    • Marsan, M. P., I. Muller, C. Ramos, F. Rodriguez, E. J. Dufourc, J. Czaplicki, and A. Milon. 1999. Cholesterol orientation and dynamics in dimyristoylphosphatidylcholine bilayers: a solid state deuterium NMR analysis. Biophys. J. 76:351-359.
    • (1999) Biophys. J. , vol.76 , pp. 351-359
    • Marsan, M.P.1    Muller, I.2    Ramos, C.3    Rodriguez, F.4    Dufourc, E.J.5    Czaplicki, J.6    Milon, A.7
  • 23
    • 0025633287 scopus 로고
    • Modulation of phospholipid acyl chain order by cholesterol. A solid-state 2H nuclear magnetic resonance study
    • Sankaram, M. B., and T. E. Thompson. 1990. Modulation of phospholipid acyl chain order by cholesterol. A solid-state 2H nuclear magnetic resonance study. Biochemistry. 29:10676-10684.
    • (1990) Biochemistry , vol.29 , pp. 10676-10684
    • Sankaram, M.B.1    Thompson, T.E.2
  • 24
    • 0002672736 scopus 로고
    • A spin label study of the effects of sterols on egg lecithin bilayers
    • Semer, R., and E. Gelerinter. 1979. A spin label study of the effects of sterols on egg lecithin bilayers. Chem. Phys. Lipids. 23:201-211.
    • (1979) Chem. Phys. Lipids , vol.23 , pp. 201-211
    • Semer, R.1    Gelerinter, E.2
  • 25
    • 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. A., S. Pekerar, H. B. Le, J. Patterson, B. Montez, and E. Oldfield. 1995. 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. 1238:163-176.
    • (1995) Biochim. Biophys. Acta , vol.1238 , pp. 163-176
    • Urbina, J.A.1    Pekerar, S.2    Le, H.B.3    Patterson, J.4    Montez, B.5    Oldfield, E.6
  • 28
    • 0015505766 scopus 로고
    • Monolayer interactions of individual lecithins with natural sterols
    • Ghosh, D., and J. Tinoco. 1972. Monolayer interactions of individual lecithins with natural sterols. Biochim. Biophys. Acta. 266:41-49.
    • (1972) Biochim. Biophys. Acta , vol.266 , pp. 41-49
    • Ghosh, D.1    Tinoco, J.2
  • 29
    • 0025179076 scopus 로고
    • Soybean phosphatidylcholine vesicles containing plant sterols: A fluorescence anisotropy study
    • Schuler, I., G. Duportail, N. Glasser, P. Benveniste, and M. A. Hartmann. 1990. Soybean phosphatidylcholine vesicles containing plant sterols: a fluorescence anisotropy study. Biochim. Biophys. Acta. 1028:82-88.
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 82-88
    • Schuler, I.1    Duportail, G.2    Glasser, N.3    Benveniste, P.4    Hartmann, M.A.5
  • 30
    • 21144453569 scopus 로고    scopus 로고
    • The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: A deuterium NMR and calorimetric study
    • Hsueh, Y., K. Gilbert, C. Trandum, M. Zuckermann, and J. Thewait. 2005. The effect of ergosterol on dipalmitoylphosphatidylcholine bilayers: a deuterium NMR and calorimetric study. Biophys. J. 88:1799-1808.
    • (2005) Biophys. J. , vol.88 , pp. 1799-1808
    • Hsueh, Y.1    Gilbert, K.2    Trandum, C.3    Zuckermann, M.4    Thewait, J.5
  • 31
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from Influenza A virus: An intrinsic property
    • Kovacs, F. A., J. K. Denny, Z. Song, J. R. Quine, and T. A. Cross. 2000. Helix tilt of the M2 transmembrane peptide from Influenza A virus: an intrinsic property. J. Mol. Biol. 295:117-125.
    • (2000) J. Mol. Biol. , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 32
    • 0034866022 scopus 로고    scopus 로고
    • Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance
    • Bak, M., R. P. Bywater, M. Hohwy, J. K. Thomsen, K. Adelhorst, H. J. Jakobsen, O. W. Sorensen, and N. C. Nielsen. 2001. Conformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance. Biophys. J. 81:1684-1698.
    • (2001) Biophys. J. , vol.81 , pp. 1684-1698
    • Bak, M.1    Bywater, R.P.2    Hohwy, M.3    Thomsen, J.K.4    Adelhorst, K.5    Jakobsen, H.J.6    Sorensen, O.W.7    Nielsen, N.C.8
  • 33
    • 0034183383 scopus 로고    scopus 로고
    • Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly N-15-labeled helical membrane proteins in oriented lipid bilayers
    • Marassi, F. M., C. Ma, J. J. Gesell, and S. J. Opella. 2000. Three-dimensional solid-state NMR spectroscopy is essential for resolution of resonances from in-plane residues in uniformly N-15-labeled helical membrane proteins in oriented lipid bilayers. J. Magn. Reson. 144:156-161.
    • (2000) J. Magn. Reson. , vol.144 , pp. 156-161
    • Marassi, F.M.1    Ma, C.2    Gesell, J.J.3    Opella, S.J.4
  • 34
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an anti-microbial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • Yamaguchi, S., D. Huster, A. Waring, R. I. Lehrer, W. Kearney, B. F. Tack, and M. Hong. 2001. Orientation and dynamics of an anti-microbial peptide in the lipid bilayer by solid-state NMR spectroscopy. Biophys. J. 81:2203-2214.
    • (2001) Biophys. J. , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 35
    • 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., A. A. Morse, A. A. Nevzorov, M. F. Mesleh, M. Oblatt-Montal, M. Montal, and S. J. Opella. 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    Morse, A.A.2    Nevzorov, A.A.3    Mesleh, M.F.4    Oblatt-Montal, M.5    Montal, M.6    Opella, S.J.7
  • 36
    • 0343185890 scopus 로고    scopus 로고
    • Structural and orientational information of the membrane-embedded M13 coat protein by C-13-MAS NMR spectroscopy
    • Glaubitz, C., G. Grobner, and A. Watts. 2000. Structural and orientational information of the membrane-embedded M13 coat protein by C-13-MAS NMR spectroscopy. Biochim. Biophys. Acta. 1463:151-161.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 151-161
    • Glaubitz, C.1    Grobner, G.2    Watts, A.3
  • 37
    • 0037047148 scopus 로고    scopus 로고
    • (1)H and (13)C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin
    • Creemers, A. F., S. Kiihne, P. H. Bovee-Geurts, W. J. DeGrip, J. Lugtenburg, and H. J. de Groot. 2002. (1)H and (13)C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin. Proc. Natl. Acad. Sci. USA. 99:9101-9106.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9101-9106
    • Creemers, A.F.1    Kiihne, S.2    Bovee-Geurts, P.H.3    Degrip, W.J.4    Lugtenburg, J.5    De Groot, H.J.6
  • 38
    • 0027519297 scopus 로고
    • Low-cost production of perdeuterated biomass using methylotrophic yeasts
    • Haon, S., S. Augé, M. Tropis, A. Milon, and N. Lindley. 1993. Low-cost production of perdeuterated biomass using methylotrophic yeasts. J. Label. Comp. Rad. 33:1053-1063.
    • (1993) J. Label. Comp. Rad. , vol.33 , pp. 1053-1063
    • Haon, S.1    Augé, S.2    Tropis, M.3    Milon, A.4    Lindley, N.5
  • 40
    • 0032869411 scopus 로고    scopus 로고
    • Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts
    • Massou, S., V. Puech, F. Talmont, P. Demange, N. D. Lindley, M. Tropis, and A. Milon. 1999. Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts. J. Biomol. NMR. 14:231-239.
    • (1999) J. Biomol. NMR. , vol.14 , pp. 231-239
    • Massou, S.1    Puech, V.2    Talmont, F.3    Demange, P.4    Lindley, N.D.5    Tropis, M.6    Milon, A.7
  • 41
    • 0030361977 scopus 로고    scopus 로고
    • Ab initio calculations of the NMR chemical shift
    • de Dios, A. C. 1996. Ab initio calculations of the NMR chemical shift. Prog. Nucl. Magn. Spectrosc. 29:229-278.
    • (1996) Prog. Nucl. Magn. Spectrosc. , vol.29 , pp. 229-278
    • De Dios, A.C.1
  • 42
  • 43
    • 0033485482 scopus 로고    scopus 로고
    • Through-bond carbon-carbon connectivities in disordered solids by NMR
    • Lesage, A., M. Bardet, and L. Emsley. 1999. Through-bond carbon-carbon connectivities in disordered solids by NMR. J. Am. Chem. Soc. 121:10987-10993.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10987-10993
    • Lesage, A.1    Bardet, M.2    Emsley, L.3
  • 45
    • 9644299771 scopus 로고    scopus 로고
    • Understanding sterol-membrane interactions. I. Hartree-Fock versus DFT calculations of 13C and 1H NMR isotropic chemical shifts of sterols in solution and hydrogen bonding effects analysis
    • Jolibois, F., O. Soubias, V. Réat, and A. Milon. 2004. Understanding sterol-membrane interactions. I. Hartree-Fock versus DFT calculations of 13C and 1H NMR isotropic chemical shifts of sterols in solution and hydrogen bonding effects analysis. Chem. Eur. J. 10:5996-6004.
    • (2004) Chem. Eur. J. , vol.10 , pp. 5996-6004
    • Jolibois, F.1    Soubias, O.2    Réat, V.3    Milon, A.4
  • 46
    • 0006627015 scopus 로고    scopus 로고
    • Static and magic angle spinning NMR of membrane peptides and proteins
    • Davis, J. H., and M. Auger. 1999. Static and magic angle spinning NMR of membrane peptides and proteins. Progr. Nucl. Magn. Res. Spectrosc. 35:1-84.
    • (1999) Progr. Nucl. Magn. Res. Spectrosc. , vol.35 , pp. 1-84
    • Davis, J.H.1    Auger, M.2
  • 47
    • 9644266958 scopus 로고    scopus 로고
    • Understanding sterol-membrane interactions. II. Complete 1H and 13C assignments by solid state NMR and determination of hydrogen bonding partners of cholesterol in a lipid bilayer
    • Soubias, O., F. Jolibois, V. Réat, and A. Milon. 2004. Understanding sterol-membrane interactions. II. Complete 1H and 13C assignments by solid state NMR and determination of hydrogen bonding partners of cholesterol in a lipid bilayer. Chem. Eur. J. 10:6005-6014.
    • (2004) Chem. Eur. J. , vol.10 , pp. 6005-6014
    • Soubias, O.1    Jolibois, F.2    Réat, V.3    Milon, A.4
  • 48
    • 0036756342 scopus 로고    scopus 로고
    • High resolution 13C NMR spectra on oriented lipid bilayers: From quantifying the various sources of line broadening to performing two-dimensional experiments with 0.2-0.3 ppm resolution in the carbon dimension
    • Soubias, O., O. Saurel, V. Réat, and A. Milon. 2002. High resolution 13C NMR spectra on oriented lipid bilayers: from quantifying the various sources of line broadening to performing two-dimensional experiments with 0.2-0.3 ppm resolution in the carbon dimension. J. Biomol. NMR. 24:15-30.
    • (2002) J. Biomol. NMR , vol.24 , pp. 15-30
    • Soubias, O.1    Saurel, O.2    Réat, V.3    Milon, A.4
  • 49
    • 48749145034 scopus 로고
    • Chemical shift anisotropy in powdered solids studied by two-dimensional FT NMR with flipping of the spinning axis
    • Bax, A., N. M. Szeverenyi, and G. E. Maciel. 1983. Chemical shift anisotropy in powdered solids studied by two-dimensional FT NMR with flipping of the spinning axis. J. Magn. Reson. 55:494-497.
    • (1983) J. Magn. Reson. , vol.55 , pp. 494-497
    • Bax, A.1    Szeverenyi, N.M.2    Maciel, G.E.3
  • 50
    • 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., J.-D. Mao, and K. Schmidt-Rohr. 2002. A robust technique for two-dimensional separation, of undistorted chemical-shift anisotropy powder patterns in magic-angle-spinning NMR. J. Magn. Reson. 155:15-18.
    • (2002) J. Magn. Reson. , vol.155 , pp. 15-18
    • Liu, S.-F.1    Mao, J.-D.2    Schmidt-Rohr, K.3
  • 51
    • 0001424097 scopus 로고
    • Switching-angle sample-spinning NMR spectroscopy for obtaining powder-pattern-resolved two-dimensional spectra: Measurements of 13C chemical-shift anisotropies in powdered 3,4-dimethoxybenzaldehyde
    • Terao, T., T. Fujii, T. Onodera, and A. Saika. 1984. Switching-angle sample-spinning NMR spectroscopy for obtaining powder-pattern-resolved two-dimensional spectra: measurements of 13C chemical-shift anisotropies in powdered 3,4-dimethoxybenzaldehyde. Chem. Phys. Lett. 107:145-148.
    • (1984) Chem. Phys. Lett. , vol.107 , pp. 145-148
    • Terao, T.1    Fujii, T.2    Onodera, T.3    Saika, A.4
  • 52
    • 0000782602 scopus 로고
    • Determination of chemical-shift-anisotropy lineshapes in a two-dimensional magic-angle-spinning NMR experiment
    • Tycko, R., G. Dabbagh, and P. A. Mirau. 1989. Determination of chemical-shift-anisotropy lineshapes in a two-dimensional magic-angle-spinning NMR experiment. J. Magn. Reson. 85:265-274.
    • (1989) J. Magn. Reson. , vol.85 , pp. 265-274
    • Tycko, R.1    Dabbagh, G.2    Mirau, P.A.3
  • 53
    • 0036018845 scopus 로고    scopus 로고
    • Determination of the chemical shielding tensor orientation from two or one of the three conventional rotations of a single crystal
    • Shekar, S. C., A. Ramamoorthy, and R. J. Wittebort. 2002. Determination of the chemical shielding tensor orientation from two or one of the three conventional rotations of a single crystal. J. Magn. Reson. 155:257-262.
    • (2002) J. Magn. Reson. , vol.155 , pp. 257-262
    • Shekar, S.C.1    Ramamoorthy, A.2    Wittebort, R.J.3
  • 54
    • 0031264701 scopus 로고    scopus 로고
    • Coupling amplification in two-dimensional MAS NMR and its application to torsion angle determination in peptides
    • Hong, M., J. D. Gross, C. M. Rienstra, R. G. Griffin, K. K. Kumashiro, and K. Schmidt-Rohr. 1997. Coupling amplification in two-dimensional MAS NMR and its application to torsion angle determination in peptides. J. Magn. Reson. 129:85-92.
    • (1997) J. Magn. Reson. , vol.129 , pp. 85-92
    • Hong, M.1    Gross, J.D.2    Rienstra, C.M.3    Griffin, R.G.4    Kumashiro, K.K.5    Schmidt-Rohr, K.6
  • 55
    • 0034241424 scopus 로고    scopus 로고
    • 15N chemical shift tensor magnitude and orientation in the molecular frame of uracil determined via MAS NMR
    • Leppert, J., B. Heise, and R. Ramachandran. 2000. 15N chemical shift tensor magnitude and orientation in the molecular frame of uracil determined via MAS NMR. J. Magn. Reson. 145:307-314.
    • (2000) J. Magn. Reson. , vol.145 , pp. 307-314
    • Leppert, J.1    Heise, B.2    Ramachandran, R.3
  • 56
    • 0009579981 scopus 로고    scopus 로고
    • One-dimensional dipolar-shift spectroscopy under magic angle spinning to determine the chemical-shift anisotropy tensors
    • Wei, Y. F., D. K. Lee, and A. Ramamoorthy. 2000. One-dimensional dipolar-shift spectroscopy under magic angle spinning to determine the chemical-shift anisotropy tensors. Chem. Phys. Lett. 324:20-24.
    • (2000) Chem. Phys. Lett. , vol.324 , pp. 20-24
    • Wei, Y.F.1    Lee, D.K.2    Ramamoorthy, A.3
  • 57
    • 0035119590 scopus 로고    scopus 로고
    • Two-dimensional relayed anisotropy correlation NMR: Characterization of the C-13′ chemical shift tensor orientation in the peptide plane of the dipeptide AibAib
    • Heise, B., J. Leppert, H. Wenschuh, O. Ohlenschlager, M. Gorlach, and R. Ramachandran. 2001. Two-dimensional relayed anisotropy correlation NMR: characterization of the C-13′ chemical shift tensor orientation in the peptide plane of the dipeptide AibAib. J. Biomol. NMR. 19:167-179.
    • (2001) J. Biomol. NMR. , vol.19 , pp. 167-179
    • Heise, B.1    Leppert, J.2    Wenschuh, H.3    Ohlenschlager, O.4    Gorlach, M.5    Ramachandran, R.6
  • 58
    • 0037138977 scopus 로고    scopus 로고
    • Determination of Cα chemical shift tensor orientation in peptides by dipolar-modulated chemical shift recoupling NMR spectroscopy
    • Yao, X., and M. Hong. 2002. Determination of Cα chemical shift tensor orientation in peptides by dipolar-modulated chemical shift recoupling NMR spectroscopy. J. Am. Chem. Soc. 124:2730-2738.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2730-2738
    • Yao, X.1    Hong, M.2
  • 59
    • 0141483325 scopus 로고    scopus 로고
    • Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis
    • Castellani, F., B.-J. van Rossum, A. Diehl, K. Rehbein, and H. Oschkinat. 2003. Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis. Biochemistry. 42:11476-11483.
    • (2003) Biochemistry , vol.42 , pp. 11476-11483
    • Castellani, F.1    Van Rossum, B.-J.2    Diehl, A.3    Rehbein, K.4    Oschkinat, H.5
  • 60
    • 0035944465 scopus 로고    scopus 로고
    • An experimental and theoretical investigation of the chemical shielding tensors of C-13(a) of alanine, valine, and leucine residues in solid peptides and in proteins in solution
    • Havlin, R. H., D. D. Laws, H. M. L. Bitter, L. K. Sanders, H. H. Sun, J. S. Grimley, D. E. Wemmer, A. Pines, and E. Oldfield. 2001. An experimental and theoretical investigation of the chemical shielding tensors of C-13(a) of alanine, valine, and leucine residues in solid peptides and in proteins in solution. J. Am. Chem. Soc. 123:10362-10369.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10362-10369
    • Havlin, R.H.1    Laws, D.D.2    Bitter, H.M.L.3    Sanders, L.K.4    Sun, H.H.5    Grimley, J.S.6    Wemmer, D.E.7    Pines, A.8    Oldfield, E.9
  • 61
    • 0036025444 scopus 로고    scopus 로고
    • Chemical shifts in amino acids, peptides, and proteins: From quantum chemistry to drug design
    • Oldfield, E. 2002. Chemical shifts in amino acids, peptides, and proteins: from quantum chemistry to drug design. Annu. Rev. Phys. Chem. 53:349-378.
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 349-378
    • Oldfield, E.1
  • 62
    • 2342535099 scopus 로고    scopus 로고
    • Efficient and accurate determination of the overall rotational diffusion tensor of a molecule from N-15 relaxation data using computer program ROTDIF
    • Walker, O., R. Varadan, and D. Fushman. 2004. Efficient and accurate determination of the overall rotational diffusion tensor of a molecule from N-15 relaxation data using computer program ROTDIF. J. Magn. Reson. 168:336-345.
    • (2004) J. Magn. Reson. , vol.168 , pp. 336-345
    • Walker, O.1    Varadan, R.2    Fushman, D.3
  • 63
    • 0001212884 scopus 로고    scopus 로고
    • Side-band manipulation in magic angle spinning nuclear magnetic resonance
    • Antzukin, O. N. 1999. Side-band manipulation in magic angle spinning nuclear magnetic resonance. Prog. Nucl. Magn. Reson. Spectrosc. 35:203.
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.35 , pp. 203
    • Antzukin, O.N.1
  • 64
    • 0001282798 scopus 로고    scopus 로고
    • A sensitive, high-resolution magic-angle turning experiment for measuring chemical shift tensor principal values
    • Alderman, D. W., G. McGeorge, J. Z. Hu, R. J. Pugmire, and D. M. Grant. 1998. A sensitive, high-resolution magic-angle turning experiment for measuring chemical shift tensor principal values. Mol. Phys. 95:1113-1126.
    • (1998) Mol. Phys. , vol.95 , pp. 1113-1126
    • Alderman, D.W.1    McGeorge, G.2    Hu, J.Z.3    Pugmire, R.J.4    Grant, D.M.5
  • 65
    • 49049125926 scopus 로고
    • Correlation of isotropic shifts and chemical shift anisotropies by two-dimensional Fourier-transform magic-angle hopping NMR spectroscopy
    • Bax, A., N. M. Szeverenyi, and G. E. Maciel. 1983. Correlation of isotropic shifts and chemical shift anisotropies by two-dimensional Fourier-transform magic-angle hopping NMR spectroscopy. J. Magn. Reson. 52:147-152.
    • (1983) J. Magn. Reson. , vol.52 , pp. 147-152
    • Bax, A.1    Szeverenyi, N.M.2    Maciel, G.E.3
  • 66
    • 85022234843 scopus 로고
    • High-resolution chemical shift and chemical shift anisotropy correlation in solids using slow magic angle spinning
    • Gan, Z. H. 1992. High-resolution chemical shift and chemical shift anisotropy correlation in solids using slow magic angle spinning. J. Am. Chem. Soc. 114:8307-8309.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8307-8309
    • Gan, Z.H.1
  • 67
    • 0011122411 scopus 로고    scopus 로고
    • Two-dimensional MAS-NMR spectra which correlate fast and slow magic angle spinning side-band patterns
    • Crockford, C., H. Geen, and J. I. Titman. 2001. Two-dimensional MAS-NMR spectra which correlate fast and slow magic angle spinning side-band patterns. Chem. Phys. Lett. 344:367-373.
    • (2001) Chem. Phys. Lett. , vol.344 , pp. 367-373
    • Crockford, C.1    Geen, H.2    Titman, J.I.3
  • 68
    • 0037736547 scopus 로고    scopus 로고
    • Correlation of fast and slow chemical shift spinning side-band patterns under fast magic-angle spinning
    • Elena, B., S. Hediger, and L. Emsley. 2003. Correlation of fast and slow chemical shift spinning side-band patterns under fast magic-angle spinning. J. Magn. Reson. 160:40-46.
    • (2003) J. Magn. Reson. , vol.160 , pp. 40-46
    • Elena, B.1    Hediger, S.2    Emsley, L.3
  • 70
    • 0035073937 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure of dimyristoylphosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol
    • Smondyrev, A. M., and M. L. Berkowitz. 2001. Molecular dynamics simulation of the structure of dimyristoylphosphatidylcholine bilayers with cholesterol, ergosterol, and lanosterol. Biophys. J. 80:1649-1658.
    • (2001) Biophys. J. , vol.80 , pp. 1649-1658
    • Smondyrev, A.M.1    Berkowitz, M.L.2
  • 71
    • 0036968507 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella, S. J., A. Nevzorov, M. F. Mesleb, and F. M. Marassi. 2002. Structure determination of membrane proteins by NMR spectroscopy. Biochem. Cell Biol. 80:597-604.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 597-604
    • Opella, S.J.1    Nevzorov, A.2    Mesleb, M.F.3    Marassi, F.M.4
  • 72
    • 0033646558 scopus 로고    scopus 로고
    • Biophysical investigations of membrane perturbations by polypeptides using solid-state NMR spectroscopy
    • Bechinger, B. 2000. Biophysical investigations of membrane perturbations by polypeptides using solid-state NMR spectroscopy. Mol. Membr. Biol. 17:135-142.
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 135-142
    • Bechinger, B.1
  • 73
    • 0026511937 scopus 로고
    • Dynamics of phosphate headgroups in biomembranes. Comprehensive analysis using phosphorus-31 nuclear magnetic resonance lineshape and relaxation time measurements
    • Dufourc, E. J., C. Mayer, J. Stohrer, G. Althoff, and G. Kothe. 1992. Dynamics of phosphate headgroups in biomembranes. Comprehensive analysis using phosphorus-31 nuclear magnetic resonance lineshape and relaxation time measurements. Biophys. J. 61:42-57.
    • (1992) Biophys. J. , vol.61 , pp. 42-57
    • Dufourc, E.J.1    Mayer, C.2    Stohrer, J.3    Althoff, G.4    Kothe, G.5
  • 74
    • 0026596491 scopus 로고
    • Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn-glycero-3-phosphocholine in bilayers: A 31P- and 2H-NMR study
    • Gale, P., and A. Watts. 1992. Effect of bacteriorhodopsin on the orientation of the headgroup of 1,2-dimyristoyl-sn-glycero-3-phosphocholine in bilayers: a 31P- and 2H-NMR study. Biochim. Biophys. Acta. 1106:317-324.
    • (1992) Biochim. Biophys. Acta , vol.1106 , pp. 317-324
    • Gale, P.1    Watts, A.2
  • 75
    • 0028260185 scopus 로고
    • Lipid specificity in the interaction of cytochrome-c with anionic phospholipid bilayers revealed by solid-state 31P NMR
    • Pinheiro, T. J., and A. Watts. 1994. Lipid specificity in the interaction of cytochrome-c with anionic phospholipid bilayers revealed by solid-state 31P NMR. Biochemistry. 33:2451-2458.
    • (1994) Biochemistry , vol.33 , pp. 2451-2458
    • Pinheiro, T.J.1    Watts, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.