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Volumn 28, Issue 20, 2012, Pages 7788-7796

Effect of divalent cations on DMPC/DHPC bicelle formation and alignment

Author keywords

[No Author keywords available]

Indexed keywords

BICELLE MIXTURES; BICELLES; DIVALENT CATION; DIVALENT IONS; LOW CONCENTRATIONS; MIMETICS; OPTIMAL ACTIVITY; SOLID STATE NMR; SOLUTION COMPONENTS; STRUCTURAL STUDIES;

EID: 84861401075     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la300885u     Document Type: Article
Times cited : (8)

References (59)
  • 3
    • 77949905333 scopus 로고    scopus 로고
    • Controlling ribozyme activity by metal ions
    • Schnabl, J.; O., S. R. K. Controlling ribozyme activity by metal ions Curr. Opin. Chem. Biol. 2010, 14, 269-275
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 269-275
    • Schnabl, J.1    K, O.S.R.2
  • 4
    • 82355171862 scopus 로고    scopus 로고
    • Processing and translation initiation of non-long terminal repeat retrotransposons by hepatitis delta virus (HDV)-like self-cleaving ribozymes
    • not supplied.
    • Ruminski, D. J.; Webb, C.-H. T.; Riccitelli, N. J.; Lupták, A. Processing and translation initiation of non-long terminal repeat retrotransposons by hepatitis delta virus (HDV)-like self-cleaving ribozymes. J. Biol. Chem. 2011, not supplied.
    • (2011) J. Biol. Chem.
    • Ruminski, D.J.1    Webb, C.-H.T.2    Riccitelli, N.J.3    Lupták, A.4
  • 5
    • 0033601233 scopus 로고    scopus 로고
    • The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin
    • Singh, B. B.; Patel, H. H.; Roepman, R.; Schick, D.; Ferreira, P. A. The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin J. Mol. Biol. 1999, 274, 37370-37378
    • (1999) J. Mol. Biol. , vol.274 , pp. 37370-37378
    • Singh, B.B.1    Patel, H.H.2    Roepman, R.3    Schick, D.4    Ferreira, P.A.5
  • 6
    • 0033545869 scopus 로고    scopus 로고
    • Two distinct classes of Ran-binding sites on the nucleoporin Nup-358
    • Yaseen, N. R.; Blobel, G. Two distinct classes of Ran-binding sites on the nucleoporin Nup-358 Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 5516-5521
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5516-5521
    • Yaseen, N.R.1    Blobel, G.2
  • 7
    • 0029088008 scopus 로고
    • Cyclophilin-A is a zinc-dependent DNA binding protein in macrophages
    • Krummrei, U.; Bang, R.; Schmidtchen, R.; Brune, K.; Bang, H. Cyclophilin-A is a zinc-dependent DNA binding protein in macrophages FEBS Lett. 1995, 371, 47-51
    • (1995) FEBS Lett. , vol.371 , pp. 47-51
    • Krummrei, U.1    Bang, R.2    Schmidtchen, R.3    Brune, K.4    Bang, H.5
  • 8
    • 84861381638 scopus 로고    scopus 로고
    • Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase
    • Kotaka, M.; Gover, S.; Vandeputte-Rutten, L.; Au, S. W.; Lam, V. M.; Adams, M. J. Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase Biol. Crystallogr. 2005, 51, 495-504
    • (2005) Biol. Crystallogr. , vol.51 , pp. 495-504
    • Kotaka, M.1    Gover, S.2    Vandeputte-Rutten, L.3    Au, S.W.4    Lam, V.M.5    Adams, M.J.6
  • 9
    • 0016810162 scopus 로고
    • Effects of Magnesium on the Kinetic Properties of Bovine Heart Glycogen Synthase D
    • Nakai, C.; Thomas, J. A. Effects of Magnesium on the Kinetic Properties of Bovine Heart Glycogen Synthase D J. Mol. Biol. 1975, 250, 4081-4085
    • (1975) J. Mol. Biol. , vol.250 , pp. 4081-4085
    • Nakai, C.1    Thomas, J.A.2
  • 10
    • 80051664755 scopus 로고    scopus 로고
    • Fast methionine-based solution structure determination of calcium-calmodulin complexes
    • Gifford, J. L.; Ishida, H.; Vogel, H. J. Fast methionine-based solution structure determination of calcium-calmodulin complexes J. Biomol. NMR 2011, 50, 71-81
    • (2011) J. Biomol. NMR , vol.50 , pp. 71-81
    • Gifford, J.L.1    Ishida, H.2    Vogel, H.J.3
  • 11
    • 0034753415 scopus 로고    scopus 로고
    • Solution structure of Ca2+-calmodulin reveals flexible hand-like prperties of its domains
    • Chou, J. J.; Li, S.; Klee, C. B.; Bax, A. Solution structure of Ca2+-calmodulin reveals flexible hand-like prperties of its domains Nat. Struct. Biol. 2001, 8, 990-7
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 990-997
    • Chou, J.J.1    Li, S.2    Klee, C.B.3    Bax, A.4
  • 12
    • 78649761509 scopus 로고    scopus 로고
    • Structural Basis for the Differential Effects of CaBP1 and Calmodulin on CaV1.2 Calcium-Dependent Inactivation
    • Findeisen, F.; Minor, D. L., Jr. Structural Basis for the Differential Effects of CaBP1 and Calmodulin on CaV1.2 Calcium-Dependent Inactivation Structure 2010, 18, 1617-1631
    • (2010) Structure , vol.18 , pp. 1617-1631
    • Findeisen, F.1    Minor Jr., D.L.2
  • 13
    • 0028928357 scopus 로고
    • The S100 Protein Family: History, Function and Expression
    • Zimmer, D. B.; Cornwall, E. H.; Landar, A.; Song, W. The S100 Protein Family: History, Function and Expression Brain Res. Bull. 1995, 37, 417-29
    • (1995) Brain Res. Bull. , vol.37 , pp. 417-429
    • Zimmer, D.B.1    Cornwall, E.H.2    Landar, A.3    Song, W.4
  • 14
    • 0036788520 scopus 로고    scopus 로고
    • Calcium-Dependent Conformational Rearrangements and Protein Stability in Chicken Annexin A5
    • Turnay, J.; Olmo, N.; Gasset, M.; Iloro, I.; Arrondo, J. L. R.; Lizarbe, M. A. Calcium-Dependent Conformational Rearrangements and Protein Stability in Chicken Annexin A5 Biophys. J. 2002, 83, 2280-2291
    • (2002) Biophys. J. , vol.83 , pp. 2280-2291
    • Turnay, J.1    Olmo, N.2    Gasset, M.3    Iloro, I.4    Arrondo, J.L.R.5    Lizarbe, M.A.6
  • 15
    • 52049083050 scopus 로고    scopus 로고
    • Crystal structure of metastasis-associated protein S100A4 in the active, calcium-bound form
    • Pathuri, P.; Vogeley, L.; Luecke, H. Crystal structure of metastasis-associated protein S100A4 in the active, calcium-bound form J. Mol. Biol. 2008, 383, 62-77
    • (2008) J. Mol. Biol. , vol.383 , pp. 62-77
    • Pathuri, P.1    Vogeley, L.2    Luecke, H.3
  • 16
    • 23344441824 scopus 로고    scopus 로고
    • The structure of phospholamban pentamer reveals a channel-like architecture in membranes
    • Oxenoid, K.; Chou, J. The structure of phospholamban pentamer reveals a channel-like architecture in membranes Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 10870-10875
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 10870-10875
    • Oxenoid, K.1    Chou, J.2
  • 17
    • 33746033794 scopus 로고    scopus 로고
    • The structural properties of the transmembrane segment of the integral membrane protein phospholamban utilizing 13C CP MAS, 2H, and REDOR solid-state NMR spectroscopy
    • Karp, E. S.; Tiburu, E. K.; Adu-Baker, S.; Lorigan, G. A. The structural properties of the transmembrane segment of the integral membrane protein phospholamban utilizing 13C CP MAS, 2H, and REDOR solid-state NMR spectroscopy Biochim. Biophys. Acta 2006, 772-780
    • (2006) Biochim. Biophys. Acta , pp. 772-780
    • Karp, E.S.1    Tiburu, E.K.2    Adu-Baker, S.3    Lorigan, G.A.4
  • 19
    • 67649865606 scopus 로고    scopus 로고
    • Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach
    • Traaseth, N.; Shi, L.; Verardi, R.; Mullen, D.; Barany, G.; Veglia, G. Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 10165-10170
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10165-10170
    • Traaseth, N.1    Shi, L.2    Verardi, R.3    Mullen, D.4    Barany, G.5    Veglia, G.6
  • 21
    • 71149098713 scopus 로고    scopus 로고
    • Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain
    • Sherratt, A. R.; Braganza, M. V.; Nguyen, E.; Ducat, T.; Goto, N. K. Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain Biochim. Biophys. Acta, Biomembr. 2009, 1788, 2444-2453
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , pp. 2444-2453
    • Sherratt, A.R.1    Braganza, M.V.2    Nguyen, E.3    Ducat, T.4    Goto, N.K.5
  • 22
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • Keller, S. L.; Bezrukov, S. M.; Gruner, S. M.; Tate, M.; Vodyanoy, I.; Parsegian, V. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids Biophys. J. 1993, 65, 23-27
    • (1993) Biophys. J. , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.4    Vodyanoy, I.5    Parsegian, V.6
  • 24
    • 0029768642 scopus 로고    scopus 로고
    • Metal and pH dependence of heptapeptide catalysis by human matrilysin
    • Cha, J.; Pedersen, M.; Auld, D. Metal and pH dependence of heptapeptide catalysis by human matrilysin Biochemistry 1996, 35, 15831-8
    • (1996) Biochemistry , vol.35 , pp. 15831-15838
    • Cha, J.1    Pedersen, M.2    Auld, D.3
  • 25
    • 70449726460 scopus 로고    scopus 로고
    • Effects of detergents on catalytic activity of human endometase/ Matrilysin-2 a putative cancer biomarker
    • Park, H. I.; Lee, S.; Ullah, A.; Cao, Q.; Sang, Q.-X. A. Effects of detergents on catalytic activity of human endometase/Matrilysin-2 a putative cancer biomarker Anal. Biochem. 2010, 396, 262-268
    • (2010) Anal. Biochem. , vol.396 , pp. 262-268
    • Park, H.I.1    Lee, S.2    Ullah, A.3    Cao, Q.4    Sang, Q.-X.A.5
  • 26
    • 79551597049 scopus 로고    scopus 로고
    • Influence of solubilizing environments on membrane protein structures
    • Cross, T. A.; Sharma, M.; Yi, M.; Zhou, H.-X. Influence of solubilizing environments on membrane protein structures Trends Biochem. Sci. 2011, 36, 117-125
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 117-125
    • Cross, T.A.1    Sharma, M.2    Yi, M.3    Zhou, H.-X.4
  • 27
    • 77955783648 scopus 로고    scopus 로고
    • Bicelle-Enabled Structural Studies on a Membrane-Associated Cytochrome b5 by Solid-State MAS NMR Spectroscopy13
    • Xu, J.; Dürr, U. H.; Im, S.-C.; Gan, Z.; Waskell, L.; Ramamoorthy, A. Bicelle-Enabled Structural Studies on a Membrane-Associated Cytochrome b5 by Solid-State MAS NMR Spectroscopy13 Angew. Chem. 2008, 120, 7982-7985
    • (2008) Angew. Chem. , vol.120 , pp. 7982-7985
    • Xu, J.1    Dürr, U.H.2    Im, S.-C.3    Gan, Z.4    Waskell, L.5    Ramamoorthy, A.6
  • 28
    • 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.; Sligar, S. G. Direct solubilization of heterologously expressed membrane proteins by incorporation into nanoscale lipid bilayers BioTechniques 2003, 35, 562-3
    • (2003) BioTechniques , vol.35 , pp. 562-563
    • Civjan, N.R.1    Bayburt, T.H.2    Schuler, M.A.3    Sligar, S.G.4
  • 29
    • 36849083490 scopus 로고    scopus 로고
    • Magic-angle spinning solid-state NMR Spectroscopy of nanodisc-embedded human CYP3A4
    • Kijac, A. Z.; Li, Y.; Sligar, S. G.; Rienstra, C. M. Magic-angle spinning solid-state NMR Spectroscopy of nanodisc-embedded human CYP3A4 Biochemistry 2007, 46, 13696-13703
    • (2007) Biochemistry , vol.46 , pp. 13696-13703
    • Kijac, A.Z.1    Li, Y.2    Sligar, S.G.3    Rienstra, C.M.4
  • 30
    • 0030722243 scopus 로고    scopus 로고
    • Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium
    • Tjandra, N.; Bax, A. Direct Measurement of Distances and Angles in Biomolecules by NMR in a Dilute Liquid Crystalline Medium Science 1997, 278, 1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 31
    • 0030236298 scopus 로고    scopus 로고
    • Measurement of amide N-15-H-1 one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments
    • Tolman, J.; Prestegard, J. Measurement of amide N-15-H-1 one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments J. Magn. Reson., Ser. B 1996, 112, 269-274
    • (1996) J. Magn. Reson., Ser. B , vol.112 , pp. 269-274
    • Tolman, J.1    Prestegard, J.2
  • 32
    • 0001349394 scopus 로고    scopus 로고
    • An HNCO-based Pulse Scheme for the Measurement of 13CA-1HA
    • Yang, D.; Tolman, J. R.; Goto, N. K.; Kay, L. E. An HNCO-based Pulse Scheme for the Measurement of 13CA-1HA J. Biomol. NMR 1998, 12, 325-332
    • (1998) J. Biomol. NMR , vol.12 , pp. 325-332
    • Yang, D.1    Tolman, J.R.2    Goto, N.K.3    Kay, L.E.4
  • 33
    • 0030719460 scopus 로고    scopus 로고
    • Magnetic field dependent amide N-15 chemical shifts in a protein-DNA complex resulting from magnetic ordering in solution
    • Ottiger, M.; Tjandra, N.; Bax, A. Magnetic field dependent amide N-15 chemical shifts in a protein-DNA complex resulting from magnetic ordering in solution J. Am. Chem. Soc. 1997, 119, 9825-9830
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 9825-9830
    • Ottiger, M.1    Tjandra, N.2    Bax, A.3
  • 34
    • 0000471160 scopus 로고    scopus 로고
    • Magnetically aligned membrane model systems with positive order parameter: Switching the sign of S-zz with paramagnetic ions
    • Prosser, R. S.; Hunt, S. A.; DiNatale, J. A.; Vold, R. R. Magnetically aligned membrane model systems with positive order parameter: Switching the sign of S-zz with paramagnetic ions J. Am. Chem. Soc. 1996, 118, 269-270
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 269-270
    • Prosser, R.S.1    Hunt, S.A.2    Dinatale, J.A.3    Vold, R.R.4
  • 35
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza A M2 protein channel: Structural implications from helix tilt and orientation
    • Kovacs, F.; Cross, T. Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation Biophys. J. 1997, 73, 2511-2517
    • (1997) Biophys. J. , vol.73 , pp. 2511-2517
    • Kovacs, F.1    Cross, T.2
  • 36
    • 0026774489 scopus 로고
    • Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR
    • Sanders, C. R.; Schwonek, J. P. Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR Biochemistry 1992, 31, 8898-8905
    • (1992) Biochemistry , vol.31 , pp. 8898-8905
    • Sanders, C.R.1    Schwonek, J.P.2
  • 37
    • 54249086668 scopus 로고    scopus 로고
    • Bilayer in small bicelles revealed by lipid-protein interactions using NMR spectroscopy
    • Lee, D.; Walter, K.; Bruckner, A.-K.; Hilty, C.; Becker, S.; Griesinger, C. Bilayer in small bicelles revealed by lipid-protein interactions using NMR spectroscopy J. Am. Chem. Soc. 2008, 130, 13822-13823
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13822-13823
    • Lee, D.1    Walter, K.2    Bruckner, A.-K.3    Hilty, C.4    Becker, S.5    Griesinger, C.6
  • 38
    • 17444365826 scopus 로고    scopus 로고
    • Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins
    • Marcotte, I.; Auger, M. Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins Concepts Magn. Reson., Part A 2005, 24A, 17-37
    • (2005) Concepts Magn. Reson., Part A , vol.24 , pp. 17-37
    • Marcotte, I.1    Auger, M.2
  • 39
    • 4644372496 scopus 로고    scopus 로고
    • Magnetically alignable phase of phospholipid "bicelle" mixtures is a chiral nematic made up of wormlike micelles
    • Nieh, M.-P.; Raghunathan, V. A.; Glinka, C. J.; Harroun, T.; Pabst, G.; Katsaras, J. Magnetically alignable phase of phospholipid "bicelle" mixtures is a chiral nematic made up of wormlike micelles Langmuir 2004, 20, 7893-7897
    • (2004) Langmuir , vol.20 , pp. 7893-7897
    • Nieh, M.-P.1    Raghunathan, V.A.2    Glinka, C.J.3    Harroun, T.4    Pabst, G.5    Katsaras, J.6
  • 40
    • 0000578582 scopus 로고    scopus 로고
    • A liquid crystalline medium for measuring residual dipolar couplings over a wide range of temperatures
    • Wang, H.; Eberstadt, M.; Olejniczak, E. T.; Meadows, R. P.; Fesik, S. W. A liquid crystalline medium for measuring residual dipolar couplings over a wide range of temperatures J. Biomol. NMR 1998, 12, 443-446
    • (1998) J. Biomol. NMR , vol.12 , pp. 443-446
    • Wang, H.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesik, S.W.5
  • 41
    • 33746812736 scopus 로고    scopus 로고
    • Effects of lipid chain length and unsaturation on bicelles stability. A phosphorus NMR study
    • Triba, M. N.; Devaux, P. F.; Warschawski, D. E. Effects of lipid chain length and unsaturation on bicelles stability. A phosphorus NMR study Biophys. J. 2006, 91, 1357-1367
    • (2006) Biophys. J. , vol.91 , pp. 1357-1367
    • Triba, M.N.1    Devaux, P.F.2    Warschawski, D.E.3
  • 42
    • 77956448654 scopus 로고    scopus 로고
    • Triton X-100 as the "short-Chain Lipid" improves the magnetic alignment and stability of membrane proteins in phosphatidylcholine bilayers for oriented-sample solid-state NMR spectroscopy
    • Park, S. H.; Opella, S. J. Triton X-100 as the "Short-Chain Lipid" improves the magnetic alignment and stability of membrane proteins in phosphatidylcholine bilayers for oriented-sample solid-state NMR spectroscopy J. Am. Chem. Soc. 2010, 132, 12552-12553
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12552-12553
    • Park, S.H.1    Opella, S.J.2
  • 44
    • 1842783195 scopus 로고    scopus 로고
    • The effects of cholesterol on magnetically aligned phospholipid bilayers: A solid-state NMR and EPR spectroscopy study
    • Lu, J. X.; Caporini, M. A.; Lorigan, G. A. The effects of cholesterol on magnetically aligned phospholipid bilayers: a solid-state NMR and EPR spectroscopy study J. Magn. Reson. 2004, 168, 18-30
    • (2004) J. Magn. Reson. , vol.168 , pp. 18-30
    • Lu, J.X.1    Caporini, M.A.2    Lorigan, G.A.3
  • 45
    • 0032177257 scopus 로고    scopus 로고
    • Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules
    • Losonczi, J. A.; Prestegard, J. H. Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules J. Biomol. NMR 1998, 12, 447-451
    • (1998) J. Biomol. NMR , vol.12 , pp. 447-451
    • Losonczi, J.A.1    Prestegard, J.H.2
  • 46
    • 77955820270 scopus 로고    scopus 로고
    • Thermal Stabilization of DMPC/DHPC Bicelles by Addition of Cholesterol Sulfate
    • Shapiro, R. A.; Brindley, A. J.; Martin, R. W. Thermal Stabilization of DMPC/DHPC Bicelles by Addition of Cholesterol Sulfate J. Am. Chem. Soc. 2010, 132, 11406-11407
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 11406-11407
    • Shapiro, R.A.1    Brindley, A.J.2    Martin, R.W.3
  • 47
    • 5444228437 scopus 로고    scopus 로고
    • Effects of small neutral molecules on phospholipid bicelle ordering
    • Li, X.; Goodson, B. M. Effects of small neutral molecules on phospholipid bicelle ordering Langmuir 2004, 20, 8437-8441
    • (2004) Langmuir , vol.20 , pp. 8437-8441
    • Li, X.1    Goodson, B.M.2
  • 48
    • 0036841870 scopus 로고    scopus 로고
    • Cation Modulation of Bicelle Size and Magnetic Alignment as Revealed by Solid-State NMR and Electron Microscopy
    • Arnold, A.; Labrot, T.; Oda, R.; Dufourc, E. J. Cation Modulation of Bicelle Size and Magnetic Alignment as Revealed by Solid-State NMR and Electron Microscopy Biophys. J. 2002, 83, 2667-80
    • (2002) Biophys. J. , vol.83 , pp. 2667-2680
    • Arnold, A.1    Labrot, T.2    Oda, R.3    Dufourc, E.J.4
  • 49
    • 2142676545 scopus 로고    scopus 로고
    • Verification of phylogenetic predictions in vivo and the importance of the tetraloop motif in a catalytic RNA
    • Krummel, D. A. P.; Altman, S. Verification of phylogenetic predictions in vivo and the importance of the tetraloop motif in a catalytic RNA Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 11200-11205
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11200-11205
    • Krummel, D.A.P.1    Altman, S.2
  • 50
    • 48749144559 scopus 로고
    • Evalutaion of a New Broadband Decoupling Sequence: WALTZ-16
    • Shaka, A.; Keeler, J.; Freeman, R. Evalutaion of a New Broadband Decoupling Sequence: WALTZ-16 J. Magn. Reson. 1983, 53, 313-340
    • (1983) J. Magn. Reson. , vol.53 , pp. 313-340
    • Shaka, A.1    Keeler, J.2    Freeman, R.3
  • 52
    • 27644528605 scopus 로고    scopus 로고
    • Bicellar" lipid mixtures as used in biochemical and biophysical studies
    • Katsaras, J.; Harroun, T.; Pencer, J.; Nieh, M.-P. Bicellar" lipid mixtures as used in biochemical and biophysical studies Naturwissenschaften 2005, 92, 355-366
    • (2005) Naturwissenschaften , vol.92 , pp. 355-366
    • Katsaras, J.1    Harroun, T.2    Pencer, J.3    Nieh, M.-P.4
  • 54
    • 21244486782 scopus 로고    scopus 로고
    • Reinvestigation by Phosphorus NMR of Lipid Distribution in Bicelles
    • Triba, N. N.; Warschawski, D. E.; Devaux, P. F. Reinvestigation by Phosphorus NMR of Lipid Distribution in Bicelles Biophys. J. 2005, 88, 1887-1901
    • (2005) Biophys. J. , vol.88 , pp. 1887-1901
    • Triba, N.N.1    Warschawski, D.E.2    Devaux, P.F.3
  • 55
    • 0018908116 scopus 로고
    • 31P Nuclear magenetic resonance and freeze-fracture electron microscopy studies on Escherichia coli. II. Lipopolysaccharide and lipopolysaccharide- phospholipid complexes
    • Alphen, L. V.; Verkleij, A.; Burnell, E.; Lugtenberg, B. 31P Nuclear magenetic resonance and freeze-fracture electron microscopy studies on Escherichia coli. II. Lipopolysaccharide and lipopolysaccharide-phospholipid complexes Biochim. Biophys. Acta 1980, 597, 502-527
    • (1980) Biochim. Biophys. Acta , vol.597 , pp. 502-527
    • Alphen, L.V.1    Verkleij, A.2    Burnell, E.3    Lugtenberg, B.4
  • 56
    • 0019315509 scopus 로고
    • Effects of tumbling and lateral diffusion on phosphatidylcholine model membrane 31P-NMR lineshapes
    • Burnell, E.; Cullis, P.; Kruijff, B. D. Effects of tumbling and lateral diffusion on phosphatidylcholine model membrane 31P-NMR lineshapes Biochim. Biophys. Acta 1980, 603, 63-69
    • (1980) Biochim. Biophys. Acta , vol.603 , pp. 63-69
    • Burnell, E.1    Cullis, P.2    Kruijff, B.D.3
  • 57
    • 77952096752 scopus 로고    scopus 로고
    • Lamellar phase coexistence induced by electrostatic interactions
    • Jho, Y. S.; Kim, M. W.; Safran, S. A.; Pincus, P. A. Lamellar phase coexistence induced by electrostatic interactions Eur. Phys. J. E 2010, 31, 201-214
    • (2010) Eur. Phys. J. e , vol.31 , pp. 201-214
    • Jho, Y.S.1    Kim, M.W.2    Safran, S.A.3    Pincus, P.A.4
  • 58
    • 77952566893 scopus 로고    scopus 로고
    • Use of a Copper-Chelated Lipid Sppeds Up NMR Measurements from Membrane Proteins
    • Yamamoto, K.; Xu, J.; Kawulka, K. E.; Vederas, J. C.; Ramamoorthy, A. Use of a Copper-Chelated Lipid Sppeds Up NMR Measurements from Membrane Proteins J. Am. Chem. Soc. 2010, 123, 6929-6931
    • (2010) J. Am. Chem. Soc. , vol.123 , pp. 6929-6931
    • Yamamoto, K.1    Xu, J.2    Kawulka, K.E.3    Vederas, J.C.4    Ramamoorthy, A.5
  • 59
    • 80054974914 scopus 로고    scopus 로고
    • Fast NMR Data Acquisition from Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance
    • Yamamoto, K.; Vivekanandan, S.; Ramamoorthy, A. Fast NMR Data Acquisition From Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance J. Phys. Chem. B 2011, 115, 12448-12455
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12448-12455
    • Yamamoto, K.1    Vivekanandan, S.2    Ramamoorthy, A.3


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