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Volumn 118, Issue 19, 2014, Pages 5119-5129

Lipid dynamics studied by calculation of 31P solid-state NMR spectra using ensembles from molecular dynamics simulations

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; LIPID BILAYERS; MOLECULAR DYNAMICS; PEPTIDES; SOLID STATE PHYSICS;

EID: 84900523942     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp5000304     Document Type: Article
Times cited : (15)

References (80)
  • 1
    • 80855133525 scopus 로고    scopus 로고
    • Cell Membranes: The Lipid Perspective
    • Coskun, U.; Simons, K. Cell Membranes: The Lipid Perspective Structure 2011, 19, 1543-1548
    • (2011) Structure , vol.19 , pp. 1543-1548
    • Coskun, U.1    Simons, K.2
  • 4
    • 80055067598 scopus 로고    scopus 로고
    • Unbiased Simulations Reveal the Inward-Facing Conformation of the Human Serotonin Transporter and Na+ Ion Release
    • Koldsø, H.; Noer, P.; Grouleff, J.; Autzen, H. E.; Sinning, S.; Schiøtt, B. Unbiased Simulations Reveal the Inward-Facing Conformation of the Human Serotonin Transporter and Na+ Ion Release PLOS Comput. Biol. 2011, 7, e1002246
    • (2011) PLOS Comput. Biol. , vol.7 , pp. 1002246
    • Koldsø, H.1    Noer, P.2    Grouleff, J.3    Autzen, H.E.4    Sinning, S.5    Schiøtt, B.6
  • 5
    • 84878940205 scopus 로고    scopus 로고
    • Ligand Induced Conformational Changes of the Human Serotonin Transporter Revealed by Molecular Dynamics Simulations
    • Koldsø, H.; Autzen, H. E.; Grouleff, J.; Schiøtt, B. Ligand Induced Conformational Changes of the Human Serotonin Transporter Revealed by Molecular Dynamics Simulations PLoS One 2013, 8, e63635
    • (2013) PLoS One , vol.8 , pp. 63635
    • Koldsø, H.1    Autzen, H.E.2    Grouleff, J.3    Schiøtt, B.4
  • 6
    • 33847114057 scopus 로고    scopus 로고
    • Conformational Dynamics of the Estrogen Receptor Alpha: Molecular Dynamics Simulations of the Influence of Binding Site Structure on Protein Dynamics
    • Celik, L.; Lund, J. D.; Schiøtt, B. Conformational Dynamics of the Estrogen Receptor Alpha: Molecular Dynamics Simulations of the Influence of Binding Site Structure on Protein Dynamics Biochemistry 2007, 46, 1743-1758
    • (2007) Biochemistry , vol.46 , pp. 1743-1758
    • Celik, L.1    Lund, J.D.2    Schiøtt, B.3
  • 7
    • 39549085136 scopus 로고    scopus 로고
    • Mechanism of Selectivity in Aquaporins and Aquaglyceroporins
    • Hub, J. S.; de Groot, B. L. Mechanism of Selectivity in Aquaporins and Aquaglyceroporins Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 1198-1203
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 1198-1203
    • Hub, J.S.1    De Groot, B.L.2
  • 8
    • 61449455404 scopus 로고    scopus 로고
    • Dynamics and Energetics of Permeation Through Aquaporins. What do We Learn from Molecular Dynamics Simulations?
    • Hub, J. S.; Grubmuller, H.; de Groot, B. L. Dynamics and Energetics of Permeation Through Aquaporins. What do We Learn from Molecular Dynamics Simulations? Handb. Exp. Pharmacol. 2009, 57-76
    • (2009) Handb. Exp. Pharmacol. , pp. 57-76
    • Hub, J.S.1    Grubmuller, H.2    De Groot, B.L.3
  • 9
    • 58149164577 scopus 로고    scopus 로고
    • Peptide Aggregation and Pore Formation in a Lipid Bilayer: A Combined Coarse-Grained and All Atom Molecular Dynamics Study
    • Thøgersen, L.; Schiøtt, B.; Vosegaard, T.; Nielsen, N. C.; Tajkhorshid, E. Peptide Aggregation and Pore Formation in a Lipid Bilayer: A Combined Coarse-Grained and All Atom Molecular Dynamics Study Biophys. J. 2008, 95, 4337-4347
    • (2008) Biophys. J. , vol.95 , pp. 4337-4347
    • Thøgersen, L.1    Schiøtt, B.2    Vosegaard, T.3    Nielsen, N.C.4    Tajkhorshid, E.5
  • 10
    • 37549017736 scopus 로고    scopus 로고
    • Visualizing Spatially Correlated Dynamics that Directs RNA Conformational Transitions
    • Zhang, Q.; Stelzer, A. C.; Fisher, C. K.; Al-Hashimi, H. M. Visualizing Spatially Correlated Dynamics that Directs RNA Conformational Transitions Nature 2007, 450, 1263-1267
    • (2007) Nature , vol.450 , pp. 1263-1267
    • Zhang, Q.1    Stelzer, A.C.2    Fisher, C.K.3    Al-Hashimi, H.M.4
  • 12
    • 84867365389 scopus 로고    scopus 로고
    • Probing the Structure and Dynamics of Proteins by Combining Molecular Dynamics Simulations and Experimental NMR Data
    • Allison, J. R.; Hertig, S.; Missimer, J. H.; Smith, L. J.; Steinmetz, M. O.; Dolenc, J. Probing the Structure and Dynamics of Proteins by Combining Molecular Dynamics Simulations and Experimental NMR Data J. Chem. Theory Comput. 2012, 8, 3430-3444
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 3430-3444
    • Allison, J.R.1    Hertig, S.2    Missimer, J.H.3    Smith, L.J.4    Steinmetz, M.O.5    Dolenc, J.6
  • 13
    • 84863393269 scopus 로고    scopus 로고
    • Mechanism of Ion Permeation and Selectivity in a Voltage Gated Sodium Channel
    • Corry, B.; Thomas, M. Mechanism of Ion Permeation and Selectivity in a Voltage Gated Sodium Channel J. Am. Chem. Soc. 2012, 134, 1840-1846
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1840-1846
    • Corry, B.1    Thomas, M.2
  • 14
    • 33646719091 scopus 로고
    • Model-Free Approach to the Interpretation of Nuclear Magnetic-Resonance Relaxation in Macromolecules 1. Theory and Range of Validity
    • Lipari, G.; Szabo, A. Model-Free Approach to the Interpretation of Nuclear Magnetic-Resonance Relaxation in Macromolecules 1. Theory and Range of Validity J. Am. Chem. Soc. 1982, 104, 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 15
    • 33845553743 scopus 로고
    • Model-Free Approach to the Interpretation of Nuclear Magnetic-Resonance Relaxation in Macromolecules 2. Analysis of Experimental Results
    • Lipari, G.; Szabo, A. Model-Free Approach to the Interpretation of Nuclear Magnetic-Resonance Relaxation in Macromolecules 2. Analysis of Experimental Results J. Am. Chem. Soc. 1982, 104, 4559-4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 16
    • 0025046144 scopus 로고
    • Deviations from the Simple 2-Parameter Model-Free Approach to the Interpretation of N-15 Nuclear Magnetic-Relaxation of Proteins
    • Clore, G. M.; Szabo, A.; Bax, A.; Kay, L. E.; Driscoll, P. C.; Gronenborn, A. M. Deviations From the Simple 2-Parameter Model-Free Approach to the Interpretation of N-15 Nuclear Magnetic-Relaxation of Proteins J. Am. Chem. Soc. 1990, 112, 4989-4991
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4989-4991
    • Clore, G.M.1    Szabo, A.2    Bax, A.3    Kay, L.E.4    Driscoll, P.C.5    Gronenborn, A.M.6
  • 17
    • 4344704702 scopus 로고    scopus 로고
    • Structure Determination of Membrane Proteins by NMR Spectroscopy
    • Opella, S. J.; Marassi, F. M. Structure Determination of Membrane Proteins by NMR Spectroscopy Chem. Rev. 2004, 104, 3587-3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 18
    • 0842286074 scopus 로고    scopus 로고
    • Structure Determination of Aligned Samples of Membrane Proteins by NMR Spectroscopy
    • Nevzorov, A. A.; Mesleh, M. F.; Opella, S. J. Structure Determination of Aligned Samples of Membrane Proteins by NMR Spectroscopy Magn. Reson. Chem. 2004, 42, 162-171
    • (2004) Magn. Reson. Chem. , vol.42 , pp. 162-171
    • Nevzorov, A.A.1    Mesleh, M.F.2    Opella, S.J.3
  • 19
    • 33748344482 scopus 로고    scopus 로고
    • Conformational Flexibility of a Microcrystalline Globular Protein: Order Parameters by Solid-State NMR Spectroscopy
    • Lorieau, J. L.; McDermott, A. E. Conformational Flexibility of a Microcrystalline Globular Protein: Order Parameters by Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2006, 128, 11505-11512
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11505-11512
    • Lorieau, J.L.1    McDermott, A.E.2
  • 20
    • 44649085834 scopus 로고    scopus 로고
    • TROSY Effects in MAS Solid-State NMR
    • Chevelkov, V.; Reif, B. TROSY Effects in MAS Solid-State NMR Concepts Magn. Reson. A 2008, 32A, 143-156
    • (2008) Concepts Magn. Reson. A , vol.32 , pp. 143-156
    • Chevelkov, V.1    Reif, B.2
  • 21
    • 25144453329 scopus 로고    scopus 로고
    • Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy
    • Andronesi, O. C.; Becker, S.; Seidel, K.; Heise, H.; Young, H. S.; Baldus, M. Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2005, 127, 12965-12974
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12965-12974
    • Andronesi, O.C.1    Becker, S.2    Seidel, K.3    Heise, H.4    Young, H.S.5    Baldus, M.6
  • 22
    • 0006783466 scopus 로고
    • Nuclear Magnetic Resonance Measurements on a Macroscopically Ordered Smectic Liquid Crystalline Phase
    • De Vries, J. J.; Berendsen, H. J. C. Nuclear Magnetic Resonance Measurements on a Macroscopically Ordered Smectic Liquid Crystalline Phase Nature 1969, 221, 1239-1240
    • (1969) Nature , vol.221 , pp. 1239-1240
    • De Vries, J.J.1    Berendsen, H.J.C.2
  • 23
  • 24
    • 38449121914 scopus 로고    scopus 로고
    • Bicelle Samples for Solid-State NMR of Membrane Proteins
    • De Angelis, A. A.; Opella, S. J. Bicelle Samples for Solid-State NMR of Membrane Proteins Nat. Protoc. 2007, 2, 2332-2338
    • (2007) Nat. Protoc. , vol.2 , pp. 2332-2338
    • De Angelis, A.A.1    Opella, S.J.2
  • 26
    • 0031993272 scopus 로고    scopus 로고
    • Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach Toward Biomembrane Studies
    • Glaubitz, C.; Watts, A. Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach Toward Biomembrane Studies J. Magn. Reson. 1998, 130, 305-316
    • (1998) J. Magn. Reson. , vol.130 , pp. 305-316
    • Glaubitz, C.1    Watts, A.2
  • 27
    • 0037138669 scopus 로고    scopus 로고
    • Bilayer Sample for Fast or Slow Magic Angle Oriented Sample Spinning Solid-State NMR Spectroscopy
    • Sizun, C.; Bechinger, B. Bilayer Sample for Fast or Slow Magic Angle Oriented Sample Spinning Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2002, 124, 1146-1147
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1146-1147
    • Sizun, C.1    Bechinger, B.2
  • 29
    • 67649405180 scopus 로고    scopus 로고
    • Orientation and Dynamics of Peptides in Membranes Calculated from 2H-NMR Data
    • Strandberg, E.; Esteban-Martin, S.; Salgado, J.; Ulrich, A. S. Orientation and Dynamics of Peptides in Membranes Calculated from 2H-NMR Data Biophys. J. 2009, 96, 3223-3232
    • (2009) Biophys. J. , vol.96 , pp. 3223-3232
    • Strandberg, E.1    Esteban-Martin, S.2    Salgado, J.3    Ulrich, A.S.4
  • 30
    • 74549185814 scopus 로고    scopus 로고
    • Solid-State NMR Approaches to Measure Topological Equilibria and Dynamics of Membrane Polypeptides
    • Salnikov, E.; Aisenbrey, C.; Vidovic, V.; Bechinger, B. Solid-State NMR Approaches to Measure Topological Equilibria and Dynamics of Membrane Polypeptides Biochim. Biophys. Acta 2010, 1798, 258-265
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 258-265
    • Salnikov, E.1    Aisenbrey, C.2    Vidovic, V.3    Bechinger, B.4
  • 31
    • 0033637460 scopus 로고    scopus 로고
    • Area per Lipid and Acyl Length Distributions in Fluid Phosphatidylcholines Determined by 2H NMR Spectroscopy
    • Petrache, H. I.; Dodd, S. W.; Brown, M. F. Area per Lipid and Acyl Length Distributions in Fluid Phosphatidylcholines Determined by 2H NMR Spectroscopy Biophys. J. 2000, 79, 3172-3192
    • (2000) Biophys. J. , vol.79 , pp. 3172-3192
    • Petrache, H.I.1    Dodd, S.W.2    Brown, M.F.3
  • 32
    • 0037125502 scopus 로고    scopus 로고
    • Elastic Deformation of Membrane Bilayers Probed by Deuterium NMR Relaxation
    • Brown, M. F.; Thurmond, R. L.; Dodd, S. W.; Otten, D.; Beyer, K. Elastic Deformation of Membrane Bilayers Probed by Deuterium NMR Relaxation J. Am. Chem. Soc. 2002, 124, 8471-8484
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8471-8484
    • Brown, M.F.1    Thurmond, R.L.2    Dodd, S.W.3    Otten, D.4    Beyer, K.5
  • 33
    • 52349123671 scopus 로고    scopus 로고
    • Pore Structure, Thinning Effect, and Lateral Diffusive Dynamics of Oriented Lipid Membranes Interacting with Antimicrobial Peptide Protegrin-1:31P and 2H Solid-State NMR Study
    • Wi, S.; Kim, C. Pore Structure, Thinning Effect, and Lateral Diffusive Dynamics of Oriented Lipid Membranes Interacting with Antimicrobial Peptide Protegrin-1:31P and 2H Solid-State NMR Study J. Phys. Chem. B 2008, 112, 11402-11414
    • (2008) J. Phys. Chem. B , vol.112 , pp. 11402-11414
    • Wi, S.1    Kim, C.2
  • 34
    • 84867638118 scopus 로고    scopus 로고
    • Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented 31P Solid-State NMR Spectroscopy
    • Bertelsen, K.; Dorosz, J.; Hansen, S. K.; Nielsen, N. C.; Vosegaard, T. Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented 31P Solid-State NMR Spectroscopy PLoS One 2012, 7, e47745
    • (2012) PLoS One , vol.7 , pp. 47745
    • Bertelsen, K.1    Dorosz, J.2    Hansen, S.K.3    Nielsen, N.C.4    Vosegaard, T.5
  • 36
    • 0020360086 scopus 로고
    • A Voltage-Gated Ion Channel Model Inferred from the Crystal-Structure of Alamethicin at 1.5-a Resolution
    • Fox, R. O.; Richards, F. M. A Voltage-Gated Ion Channel Model Inferred from the Crystal-Structure of Alamethicin at 1.5-a Resolution Nature 1982, 300, 325-330
    • (1982) Nature , vol.300 , pp. 325-330
    • Fox, R.O.1    Richards, F.M.2
  • 37
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: Molecular dynamics simulations
    • Tieleman, D. P.; Berendsen, H. J.; Sansom, M. S. An alamethicin channel in a lipid bilayer: molecular dynamics simulations Biophys. J. 1999, 76, 1757-69
    • (1999) Biophys. J. , vol.76 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.2    Sansom, M.S.3
  • 38
    • 0036280431 scopus 로고    scopus 로고
    • Modifications of Alamethicin Ion Channels by Substitution of Glu-7 for Gln-7
    • Asami, K.; Okazaki, T.; Nagai, Y.; Nagaoka, Y. Modifications of Alamethicin Ion Channels by Substitution of Glu-7 for Gln-7 Biophys. J. 2002, 83, 219-228
    • (2002) Biophys. J. , vol.83 , pp. 219-228
    • Asami, K.1    Okazaki, T.2    Nagai, Y.3    Nagaoka, Y.4
  • 40
    • 3142714765 scopus 로고    scopus 로고
    • Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-Phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations
    • Mackerell, A. D.; Feig, M.; Brooks, C. L. Extending the Treatment of Backbone Energetics in Protein Force Fields: Limitations of Gas-Phase Quantum Mechanics in Reproducing Protein Conformational Distributions in Molecular Dynamics Simulations J. Comput. Chem. 2004, 25, 1400-1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 43
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 2008, 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 46
    • 84860731699 scopus 로고    scopus 로고
    • Modeling the Self-Assembly and Stability of DHPC Micelles Using Atomic Resolution and Coarse Grained MD Simulations
    • Kraft, J. F.; Vestergaard, M.; Schiøtt, B.; Thøgersen, L. Modeling the Self-Assembly and Stability of DHPC Micelles Using Atomic Resolution and Coarse Grained MD Simulations J. Chem. Theory Comput. 2012, 8, 1556-1569
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1556-1569
    • Kraft, J.F.1    Vestergaard, M.2    Schiøtt, B.3    Thøgersen, L.4
  • 49
    • 0017841271 scopus 로고
    • Phosphorus-31 Chemical-Shift Tensors in Barium Diethyl Phosphate and Urea-Phosphoric Acid: Model Compounds for Phospholipid Head-Group Stuides
    • Herzfeld, J.; Griffin, R. G.; Haberkorn, R. A. Phosphorus-31 Chemical-Shift Tensors in Barium Diethyl Phosphate and Urea-Phosphoric Acid: Model Compounds for Phospholipid Head-Group Stuides Biochemistry 1978, 17, 8
    • (1978) Biochemistry , vol.17 , pp. 8
    • Herzfeld, J.1    Griffin, R.G.2    Haberkorn, R.A.3
  • 50
    • 0028841644 scopus 로고
    • Membrane Orientation of the N-Terminal Segment of Alamethicin Determined by Solid-State 15N NMR
    • North, C. L.; Barranger-Mathys, M.; Cafiso, D. S. Membrane Orientation of the N-Terminal Segment of Alamethicin Determined by Solid-State 15N NMR Biophys. J. 1995, 69, 2392-2397
    • (1995) Biophys. J. , vol.69 , pp. 2392-2397
    • North, C.L.1    Barranger-Mathys, M.2    Cafiso, D.S.3
  • 51
    • 11444256357 scopus 로고    scopus 로고
    • Investigations of Polypeptide Rotational Diffusion in Aligned Membranes by 2H and 15N Solid-State NMR Spectroscopy
    • Aisenbrey, C.; Bechinger, B. Investigations of Polypeptide Rotational Diffusion in Aligned Membranes by 2H and 15N Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2004, 126, 16676-16683
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16676-16683
    • Aisenbrey, C.1    Bechinger, B.2
  • 52
    • 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. D.; DeGrado, W. F.; 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. 2007, 129, 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
  • 53
    • 33947586763 scopus 로고    scopus 로고
    • Selective Averaging for High-Resolution Solid-State NMR Spectroscopy of Aligned Samples
    • Nevzorov, A. A.; Opella, S. J. Selective Averaging for High-Resolution Solid-State NMR Spectroscopy of Aligned Samples J. Magn. Reson. 2007, 185, 59-70
    • (2007) J. Magn. Reson. , vol.185 , pp. 59-70
    • Nevzorov, A.A.1    Opella, S.J.2
  • 54
    • 36749003200 scopus 로고    scopus 로고
    • Membrane-Bound Conformation of Peptaibols with Methyl-Deuterated Alpha-Amino lsobutyric Acids by 2H Magic Angle Spinning Solid-State NMR Spectroscopy
    • Bertelsen, K.; Pedersen, J. M.; Rasmussen, B. S.; Skrydstrup, T.; Nielsen, N. C.; Vosegaard, T. Membrane-Bound Conformation of Peptaibols with Methyl-Deuterated Alpha-Amino lsobutyric Acids by 2H Magic Angle Spinning Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2007, 129, 14717-14723
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14717-14723
    • Bertelsen, K.1    Pedersen, J.M.2    Rasmussen, B.S.3    Skrydstrup, T.4    Nielsen, N.C.5    Vosegaard, T.6
  • 55
    • 0001552551 scopus 로고    scopus 로고
    • REPULSION, a Novel Approach to Efficient Powder Averaging in Solid-State NMR
    • Bak, M.; Nielsen, N. C. REPULSION, a Novel Approach to Efficient Powder Averaging in Solid-State NMR J. Magn. Reson. 1997, 125, 132-139
    • (1997) J. Magn. Reson. , vol.125 , pp. 132-139
    • Bak, M.1    Nielsen, N.C.2
  • 56
    • 37349104237 scopus 로고    scopus 로고
    • Alternative Mechanisms of Action of Cationic Antimicrobial Peptides on Bacteria
    • Hale, J. D.; Hancock, R. E. Alternative Mechanisms of Action of Cationic Antimicrobial Peptides on Bacteria Expert. Rev. Anti Infect. Ther. 2007, 5, 951-959
    • (2007) Expert. Rev. Anti Infect. Ther. , vol.5 , pp. 951-959
    • Hale, J.D.1    Hancock, R.E.2
  • 57
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial Peptides: Pore Formers or Metabolic Inhibitors in Bacteria?
    • Brogden, K. A. Antimicrobial Peptides: Pore Formers or Metabolic Inhibitors in Bacteria? Nat. Rev. Microbiol. 2005, 3, 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 58
    • 33745747109 scopus 로고    scopus 로고
    • Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin
    • Ramamoorthy, A.; Thennarasu, S.; Lee, D. K.; Tan, A.; Maloy, L. Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin Biophys. J. 2006, 91, 206-216
    • (2006) Biophys. J. , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.K.3    Tan, A.4    Maloy, L.5
  • 59
    • 0023815974 scopus 로고
    • Conformation and Orientation of Gramicidin a in Oriented Phospholipid Bilayers Measured by Solid State Carbon-13 NMR
    • Cornell, B. A.; Separovic, F.; Baldassi, A. J.; Smith, R. Conformation and Orientation of Gramicidin a in Oriented Phospholipid Bilayers Measured by Solid State Carbon-13 NMR Biophys. J. 1988, 53, 67-76
    • (1988) Biophys. J. , vol.53 , pp. 67-76
    • Cornell, B.A.1    Separovic, F.2    Baldassi, A.J.3    Smith, R.4
  • 60
    • 0034866022 scopus 로고    scopus 로고
    • Conformation of Alamethicin in Oriented Phospholipid Bilayers Determined by 15N Solid-State Nuclear Magnetic Resonance
    • Bak, M.; Bywater, R. P.; Hohwy, M.; Thomsen, J. K.; Adelhorst, K.; Jakobsen, H. J.; Sorensen, O. W.; Nielsen, N. C. Conformation of Alamethicin in Oriented Phospholipid Bilayers Determined by 15N Solid-State Nuclear Magnetic Resonance Biophys. J.. 2001, 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
  • 61
    • 58849139281 scopus 로고    scopus 로고
    • Structure and Alignment of the Membrane-Associated Peptaibols Ampullosporin A and Alamethicin by Oriented 15N and 31P Solid-State NMR Spectroscopy
    • Salnikov, E. S.; Friedrich, H.; Li, X.; Bertani, P.; Reissmann, S.; Hertweck, C.; O'Neil, J. D.; Raap, J.; Bechinger, B. Structure and Alignment of the Membrane-Associated Peptaibols Ampullosporin A and Alamethicin by Oriented 15N and 31P Solid-State NMR Spectroscopy Biophys. J. 2009, 96, 86-100
    • (2009) Biophys. J. , vol.96 , pp. 86-100
    • Salnikov, E.S.1    Friedrich, H.2    Li, X.3    Bertani, P.4    Reissmann, S.5    Hertweck, C.6    O'Neil, J.D.7    Raap, J.8    Bechinger, B.9
  • 62
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of Lipid Bilayer Disruption by the Human Antimicrobial Peptide, LL-37
    • Henzler Wildman, K. A.; Lee, D. K.; Ramamoorthy, A. Mechanism of Lipid Bilayer Disruption by the Human Antimicrobial Peptide, LL-37 Biochemistry 2003, 42, 6545-6558
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 63
    • 0037031254 scopus 로고    scopus 로고
    • Solid-State NMR Investigations of Peptide-Lipid Interaction and Orientation of a Beta-Sheet Antimicrobial Peptide, Protegrin
    • Yamaguchi, S.; Hong, T.; Waring, A.; Lehrer, R. I.; Hong, M. Solid-State NMR Investigations of Peptide-Lipid Interaction and Orientation of a Beta-Sheet Antimicrobial Peptide, Protegrin Biochemistry 2002, 41, 9852-9862
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 64
    • 33846595904 scopus 로고
    • High-Resolution Heteronuclear Dipolar Solid-State Nmr-Spectroscopy
    • Wu, C. H.; Ramamoorthy, A.; Opella, S. J. High-Resolution Heteronuclear Dipolar Solid-State Nmr-Spectroscopy J. Magn. Reson. A 1994, 109, 270-272
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 65
    • 30844466828 scopus 로고    scopus 로고
    • Probing Membrane Topology by High-Resolution 1H-13C Heteronuclear Dipolar Solid-State NMR Spectroscopy
    • Lu, J. X.; Damodaran, K.; Lorigan, G. A. Probing Membrane Topology by High-Resolution 1H-13C Heteronuclear Dipolar Solid-State NMR Spectroscopy J. Magn. Reson. 2006, 178, 283-287
    • (2006) J. Magn. Reson. , vol.178 , pp. 283-287
    • Lu, J.X.1    Damodaran, K.2    Lorigan, G.A.3
  • 67
    • 4143051192 scopus 로고    scopus 로고
    • Lessons of Slicing Membranes: Interplay of Packing, Free Area, and Lateral Diffusion in Phospholipid/Cholesterol Bilayers
    • Falck, E.; Patra, M.; Karttunen, M.; Hyvonen, M. T.; Vattulainen, I. Lessons of Slicing Membranes: Interplay of Packing, Free Area, and Lateral Diffusion in Phospholipid/Cholesterol Bilayers Biophys. J. 2004, 87, 1076-1091
    • (2004) Biophys. J. , vol.87 , pp. 1076-1091
    • Falck, E.1    Patra, M.2    Karttunen, M.3    Hyvonen, M.T.4    Vattulainen, I.5
  • 69
    • 84882398607 scopus 로고    scopus 로고
    • Perspective on the Martini Model
    • Marrink, S. J.; Tieleman, D. P. Perspective on the Martini Model Chem. Soc. Rev. 2013, 42, 6801-6822
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 6801-6822
    • Marrink, S.J.1    Tieleman, D.P.2
  • 70
    • 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.; 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. 2006, 128, 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
  • 73
    • 33749511249 scopus 로고    scopus 로고
    • Three-Dimensional Structure of the Transmembrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles
    • Park, S. H.; De Angelis, A. A.; Nevzorov, A. A.; Wu, C. H.; Opella, S. J. Three-Dimensional Structure of the Transmembrane Domain of Vpu from HIV-1 in Aligned Phospholipid Bicelles Biophys. J. 2006, 91, 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
  • 74
    • 79952000948 scopus 로고    scopus 로고
    • Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides
    • Bertelsen, K.; Vad, B.; Nielsen, E. H.; Hansen, S. K.; Skrydstrup, T.; Otzen, D. E.; Vosegaard, T.; Nielsen, N. C. Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides J. Phys. Chem. B 2011, 115, 1767-1774
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1767-1774
    • Bertelsen, K.1    Vad, B.2    Nielsen, E.H.3    Hansen, S.K.4    Skrydstrup, T.5    Otzen, D.E.6    Vosegaard, T.7    Nielsen, N.C.8
  • 75
    • 0026774489 scopus 로고
    • Characterization of Magnetically Orientable Bilayers in Mixtures of Dihexanoylphosphatidylcholine and Dimyristoylphosphatidylcholine by Solid-State NMR
    • Sanders, C. R., 2nd; 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 II, C.R.1    Schwonek, J.P.2
  • 76
    • 0032586679 scopus 로고    scopus 로고
    • 31P NMR First Spectral Moment Study of the Partial Magnetic Orientation of Phospholipid Membranes
    • Picard, F.; Paquet, M. J.; Levesque, J.; Belanger, A.; Auger, M. 31P NMR First Spectral Moment Study of the Partial Magnetic Orientation of Phospholipid Membranes Biophys. J. 1999, 77, 888-902
    • (1999) Biophys. J. , vol.77 , pp. 888-902
    • Picard, F.1    Paquet, M.J.2    Levesque, J.3    Belanger, A.4    Auger, M.5
  • 77
    • 33747570634 scopus 로고    scopus 로고
    • Magnetically Oriented Phospholipid Bilayered Micelles for Structural Studies of Polypeptides. Does the Ideal Bicelle Exist?
    • Vold, R. R.; Prosser, R. S. Magnetically Oriented Phospholipid Bilayered Micelles for Structural Studies of Polypeptides. Does the Ideal Bicelle Exist? J. Magn. Reson. B 1996, 113, 267-271
    • (1996) J. Magn. Reson. B , vol.113 , pp. 267-271
    • Vold, R.R.1    Prosser, R.S.2
  • 78
    • 0031969085 scopus 로고    scopus 로고
    • Magnetically Aligned Phospholipid Bilayers with Positive Ordering: A New Model Membrane System
    • Prosser, R. S.; Hwang, J. S.; Vold, R. R. Magnetically Aligned Phospholipid Bilayers with Positive Ordering: A New Model Membrane System Biophys. J. 1998, 74, 2405-2418
    • (1998) Biophys. J. , vol.74 , pp. 2405-2418
    • Prosser, R.S.1    Hwang, J.S.2    Vold, R.R.3
  • 79
    • 0032174883 scopus 로고    scopus 로고
    • Characterization of Magnetically Oriented Phospholipid Micelles for Measurement of Dipolar Couplings in Macromolecules
    • Ottiger, M.; Bax, A. Characterization of Magnetically Oriented Phospholipid Micelles for Measurement of Dipolar Couplings in Macromolecules J. Biomol. NMR 1998, 12, 361-372
    • (1998) J. Biomol. NMR , vol.12 , pp. 361-372
    • Ottiger, M.1    Bax, A.2
  • 80
    • 21244486782 scopus 로고    scopus 로고
    • Reinvestigation by Phosphorus NMR of Lipid Distribution in Bicelles
    • Triba, M. 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, M.N.1    Warschawski, D.E.2    Devaux, P.F.3


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