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Volumn 117, Issue 39, 2013, Pages 11641-11653

Free energetics of arginine permeation into model DMPC lipid bilayers: Coupling of effective counterion concentration and lateral bilayer dimensions

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CELL MEMBRANES; ESTIMATION; FREE ENERGY; IONS; MOLECULAR DYNAMICS; PEPTIDES;

EID: 84885146622     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp404829y     Document Type: Article
Times cited : (47)

References (69)
  • 1
    • 0024209811 scopus 로고
    • Autonomous Functional Domains of Chemically Synthesized Human Immunodeficiency Virus TAT Trans-Activator Protein
    • Green, M.; Loewenstein, P. M. Autonomous Functional Domains of Chemically Synthesized Human Immunodeficiency Virus TAT Trans-Activator Protein Cell 1988, 55, 1179-1188
    • (1988) Cell , vol.55 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 2
    • 0024262589 scopus 로고
    • Cellular Uptake of the TAT Protein from Human Immunodeficiency Virus
    • Frankel, A. D.; Pabo, C. Cellular Uptake of the TAT Protein from Human Immunodeficiency Virus Cell 1988, 55, 1189-1193
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.2
  • 3
    • 77951902057 scopus 로고    scopus 로고
    • Arginine-Rich Cell-Penetrating Peptides
    • Schmidt, N.; Mishrab, A.; Laia, G. H.; Wong, G. C. Arginine-Rich Cell-Penetrating Peptides FEBS Lett. 2010, 584, 1806-1813
    • (2010) FEBS Lett. , vol.584 , pp. 1806-1813
    • Schmidt, N.1    Mishrab, A.2    Laia, G.H.3    Wong, G.C.4
  • 4
    • 84857771152 scopus 로고    scopus 로고
    • Potential Efficacy of Cell Penetrating Peptides for Nucleic Acid and Drug Delivery in Cancer
    • Bolhassani, A. Potential Efficacy of Cell Penetrating Peptides for Nucleic Acid and Drug Delivery in Cancer Biochim. Biophys. Acta 2011, 1816, 232-246
    • (2011) Biochim. Biophys. Acta , vol.1816 , pp. 232-246
    • Bolhassani, A.1
  • 6
    • 79955654072 scopus 로고    scopus 로고
    • Arginine in Membranes: The Connection between Molecular Dynamics Simulations and Translocon-Mediated Insertion Experiments
    • Schow, E. V.; Freites, J. A.; Cheng, P.; Bernsel, A.; von Heijne, G.; White, S. H.; Tobias, D. J. Arginine in Membranes: The Connection between Molecular Dynamics Simulations and Translocon-Mediated Insertion Experiments J. Membr. Biol. 2011, 239, 35-48
    • (2011) J. Membr. Biol. , vol.239 , pp. 35-48
    • Schow, E.V.1    Freites, J.A.2    Cheng, P.3    Bernsel, A.4    Von Heijne, G.5    White, S.H.6    Tobias, D.J.7
  • 7
    • 79955650131 scopus 로고    scopus 로고
    • A Look at Arginine in Membranes
    • Hristova, K.; Wimley, W. C. A Look at Arginine in Membranes J. Membr. Biol. 2011, 239, 49-56
    • (2011) J. Membr. Biol. , vol.239 , pp. 49-56
    • Hristova, K.1    Wimley, W.C.2
  • 8
    • 77958066477 scopus 로고    scopus 로고
    • Defect-Mediated Trafficking across Cell Membranes: Insights from in Silico Modeling
    • Gurtovenko, A. A.; Anwar, J.; Vattulainen, I. Defect-Mediated Trafficking across Cell Membranes: Insights from in Silico Modeling Chem. Rev. 2010, 110, 6077-6103
    • (2010) Chem. Rev. , vol.110 , pp. 6077-6103
    • Gurtovenko, A.A.1    Anwar, J.2    Vattulainen, I.3
  • 11
    • 45749120326 scopus 로고    scopus 로고
    • Cell-Penetrating Peptides as Delivery Vehicles for Biology and Medicine
    • Stewart, K. M.; Horton, K. L.; Kelley, S. O. Cell-Penetrating Peptides as Delivery Vehicles for Biology and Medicine Org. Biomol. Chem. 2008, 6, 2242-2255
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2242-2255
    • Stewart, K.M.1    Horton, K.L.2    Kelley, S.O.3
  • 12
    • 28844454642 scopus 로고    scopus 로고
    • Arginine-Rich Cell Penetrating Peptides: From Endosomal Uptake to Nuclear Delivery
    • Melikov, K.; Chernomordik, L. V. Arginine-Rich Cell Penetrating Peptides: From Endosomal Uptake to Nuclear Delivery Cell. Mol. Life Sci. 2005, 62, 2739-2749
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2739-2749
    • Melikov, K.1    Chernomordik, L.V.2
  • 13
    • 84877755819 scopus 로고    scopus 로고
    • Backbone Rigidity and Static Presentation of Guanidinium Groups Increases Cellular Uptake of Arginine-Rich Cell-Penetrating Peptides
    • Laettig-Tuennemann, G.; Prinz, M.; Hoffmann, D.; Behlke, J.; Palm-Apergi, C.; Morano, I.; Herce, H. D.; Cardoso, M. C. Backbone Rigidity and Static Presentation of Guanidinium Groups Increases Cellular Uptake of Arginine-Rich Cell-Penetrating Peptides Nat. Commun. 2011, 2, 1-6
    • (2011) Nat. Commun. , vol.2 , pp. 1-6
    • Laettig-Tuennemann, G.1    Prinz, M.2    Hoffmann, D.3    Behlke, J.4    Palm-Apergi, C.5    Morano, I.6    Herce, H.D.7    Cardoso, M.C.8
  • 14
    • 79960104118 scopus 로고    scopus 로고
    • Penetration without Cells: Membrane Translocation of Cell-Penetrating Peptides in the Model Giant Plasma Membrane Vesicles
    • Saalik, P.; Niinep, A.; Pae, J.; Hansen, M.; Lubenets, D.; Langel, U.; Pooga, M. Penetration without Cells: Membrane Translocation of Cell-Penetrating Peptides in the Model Giant Plasma Membrane Vesicles J. Controlled Release 2011, 153, 117-125
    • (2011) J. Controlled Release , vol.153 , pp. 117-125
    • Saalik, P.1    Niinep, A.2    Pae, J.3    Hansen, M.4    Lubenets, D.5    Langel, U.6    Pooga, M.7
  • 18
    • 70350040736 scopus 로고    scopus 로고
    • Cell Penetrating Peptides: How Do They Do It?
    • Herce, H. D.; Garcia, A. E. Cell Penetrating Peptides: How Do They Do It? J. Biol. Phys. 2007, 33, 345-356
    • (2007) J. Biol. Phys. , vol.33 , pp. 345-356
    • Herce, H.D.1    Garcia, A.E.2
  • 19
    • 79958796013 scopus 로고    scopus 로고
    • Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening
    • Marks, J.; Placone, J.; Hristova, K.; Wimley, W. C. Spontaneous Membrane-Translocating Peptides by Orthogonal High-Throughput Screening J. Am. Chem. Soc. 2011, 133, 8995-9004
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 8995-9004
    • Marks, J.1    Placone, J.2    Hristova, K.3    Wimley, W.C.4
  • 20
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-Rich Peptides Destabilize the Plasma Membrane, Consistent with a Pore Formation Translocation Mechanism of Cell-Penetrating Peptides
    • Herce, H. D.; Garcia, A. E.; Litt, J.; Kane, R. S.; Martin, P.; Enrique, N.; Rebolledo, A.; Milesi, V. Arginine-Rich Peptides Destabilize the Plasma Membrane, Consistent with a Pore Formation Translocation Mechanism of Cell-Penetrating Peptides Biohys. J. 2009, 97, 1917-1925
    • (2009) Biohys. J. , vol.97 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Litt, J.3    Kane, R.S.4    Martin, P.5    Enrique, N.6    Rebolledo, A.7    Milesi, V.8
  • 21
    • 33747038452 scopus 로고    scopus 로고
    • Cell-Penetrating Peptides: A Brief Introduction
    • Jarver, P.; Langel, U. Cell-Penetrating Peptides: A Brief Introduction Biochim. Biophys. Acta, Biomembr. 2006, 1758, 260-263
    • (2006) Biochim. Biophys. Acta, Biomembr. , vol.1758 , pp. 260-263
    • Jarver, P.1    Langel, U.2
  • 23
    • 33646236541 scopus 로고    scopus 로고
    • Oligorarginine Vectors for Intracelular Delivery: Design and Cellular - Uptake Mechanisms
    • Futaki, S. Oligorarginine Vectors for Intracelular Delivery: Design and Cellular-Uptake Mechanisms Biopolymers 2006, 84, 241-249
    • (2006) Biopolymers , vol.84 , pp. 241-249
    • Futaki, S.1
  • 24
    • 34247633528 scopus 로고    scopus 로고
    • On the Thermodynamic Stability of a Charged Arginine Sidechan in a Transmembrane Helix
    • S. Dorairaj, T. W. Au On the Thermodynamic Stability of a Charged Arginine Sidechan in a Transmembrane Helix Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 4943-4948
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 4943-4948
    • Dorairaj, S.1    Au, T.W.2
  • 26
    • 44349099863 scopus 로고    scopus 로고
    • A Continuum Method for Determining Membrane Protein Insertion Energies and the Problem of Charged Residues
    • Choe, S.; Hecht, K. A.; Grabe, M. A Continuum Method for Determining Membrane Protein Insertion Energies and the Problem of Charged Residues J. Gen. Physiol. 2009, 131, 563-573
    • (2009) J. Gen. Physiol. , vol.131 , pp. 563-573
    • Choe, S.1    Hecht, K.A.2    Grabe, M.3
  • 27
    • 50549085702 scopus 로고    scopus 로고
    • α Profile Calculation for the Lipid Membrane-Exposed Arginine Side Chain
    • α Profile Calculation for the Lipid Membrane-Exposed Arginine Side Chain J. Phys. Chem. B 2008, 112, 9574-9587
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9574-9587
    • Li, L.1    Vorobyov, I.2    Allen, T.W.3
  • 28
    • 80052468548 scopus 로고    scopus 로고
    • Transfer of Arginine into Lipid Bilayers Is Nonadditive
    • MacCallum, J. L.; Bennett, W. F. D.; Tieleman, D. P. Transfer of Arginine into Lipid Bilayers Is Nonadditive Biophys. J. 2011, 101, 110-117
    • (2011) Biophys. J. , vol.101 , pp. 110-117
    • Maccallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 29
    • 84872818385 scopus 로고    scopus 로고
    • Free Energy of Translocating an Arginine-Rich Cell-Penetrating Peptide across a Lipid Bilayer Suggests Pore Formation
    • Huang, K.; Garcia, A. E. Free Energy of Translocating an Arginine-Rich Cell-Penetrating Peptide across a Lipid Bilayer Suggests Pore Formation Biophys. J. 2013, 22, 412-420
    • (2013) Biophys. J. , vol.22 , pp. 412-420
    • Huang, K.1    Garcia, A.E.2
  • 30
    • 84871766912 scopus 로고    scopus 로고
    • Translocation of Polyarginines and Conjugated Nanoparticles across Symmetric Membranes
    • Li, Z.-L.; Ding, H.-M.; Ma, Y. Q. Translocation of Polyarginines and Conjugated Nanoparticles across Symmetric Membranes Soft Matter 2013, 9, 1281-1286
    • (2013) Soft Matter , vol.9 , pp. 1281-1286
    • Li, Z.-L.1    Ding, H.-M.2    Ma, Y.Q.3
  • 31
    • 79959928058 scopus 로고    scopus 로고
    • Side-Chain Hydrophobicity Scale Derived from Transmembrane Protein Folding into Lipid Bilayers
    • Moon, C. P.; Fleming, K. G. Side-Chain Hydrophobicity Scale Derived from Transmembrane Protein Folding into Lipid Bilayers Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 10174-10177
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2
  • 32
    • 84857333669 scopus 로고    scopus 로고
    • Determination of Membrane-Insertion Free Energies by Molecular Dynamics Simulations
    • Gumbart, J.; Roux, B. Determination of Membrane-Insertion Free Energies by Molecular Dynamics Simulations Biophys. J. 2012, 102, 795-801
    • (2012) Biophys. J. , vol.102 , pp. 795-801
    • Gumbart, J.1    Roux, B.2
  • 33
    • 84864008382 scopus 로고    scopus 로고
    • Membrane Bending is Critical for the Stability of Voltage Sensor Segments in the Membrane
    • Callenberg, K. M.; Latorraca, N. R.; Grabe, M. Membrane Bending is Critical for the Stability of Voltage Sensor Segments in the Membrane J. Gen. Physiol. 2012, 140, 55-68
    • (2012) J. Gen. Physiol. , vol.140 , pp. 55-68
    • Callenberg, K.M.1    Latorraca, N.R.2    Grabe, M.3
  • 34
    • 50549097744 scopus 로고    scopus 로고
    • Assessing Atomistic and Coarse-Grained Force Fields for Protein-Lipid Interactions: The Formidable Challenge of an Ionizable Side Chain in a Membrane
    • Vorobyov, I.; Li, L.; Allen, T. W. Assessing Atomistic and Coarse-Grained Force Fields for Protein-Lipid Interactions: The Formidable Challenge of an Ionizable Side Chain in a Membrane J. Phys. Chem. B 2008, 112, 9588-9602
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9588-9602
    • Vorobyov, I.1    Li, L.2    Allen, T.W.3
  • 35
    • 45849126920 scopus 로고    scopus 로고
    • Charged Protein Side Chain Movement in Lipid Bilayers Explored with Free Energy Simulation
    • Li, L.; Vorobyov, I.; Dorairaj, S.; Allen, T. W. Charged Protein Side Chain Movement in Lipid Bilayers Explored with Free Energy Simulation Curr. Top. Membr. 2008, 60, 505-459
    • (2008) Curr. Top. Membr. , vol.60 , pp. 505-459
    • Li, L.1    Vorobyov, I.2    Dorairaj, S.3    Allen, T.W.4
  • 36
    • 84855437583 scopus 로고    scopus 로고
    • The Role of Membrane Thickness in Charged Protein-Lipid Interactions
    • Li, L. B.; Vorobyov, I.; Allen, T. W. The Role of Membrane Thickness in Charged Protein-Lipid Interactions Biochim. Biophys. Acta, Biomembr. 2012, 1818, 135-145
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 135-145
    • Li, L.B.1    Vorobyov, I.2    Allen, T.W.3
  • 37
    • 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
  • 40
    • 0030844208 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of Unsaturated Lipids at Low Hydration: Parametrization and Comparison with Diffraction Studies
    • Feller, S. E.; Yin, D.; Pastor, R. W.; MacKerell, J. A. D. Molecular Dynamics Simulation of Unsaturated Lipids at Low Hydration: Parametrization and Comparison with Diffraction Studies Biophys. J. 1997, 73, 2269-2279
    • (1997) Biophys. J. , vol.73 , pp. 2269-2279
    • Feller, S.E.1    Yin, D.2    Pastor, R.W.3    Mackerell, J.A.D.4
  • 43
    • 43149121350 scopus 로고    scopus 로고
    • Does Arginine Remain Protonated in the Lipid Membrane? Insights from Microscopic pKa Calculations
    • Yoo, J.; Cui, Q. Does Arginine Remain Protonated in the Lipid Membrane? Insights from Microscopic pKa Calculations Biophys. J. 2008, 94, L61-L63
    • (2008) Biophys. J. , vol.94
    • Yoo, J.1    Cui, Q.2
  • 45
    • 43649093151 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Asymmetric NaCl and KCl Solutions Separated by Phosphatidylcholine Bilayers: Potential Drops and Structural Changes Induced by Strong NA+-Lipid Interactions and Finite Size Effects
    • Lee, S.-J.; Song, Y.; Baker, N. A. Molecular Dynamics Simulations of Asymmetric NaCl and KCl Solutions Separated by Phosphatidylcholine Bilayers: Potential Drops and Structural Changes Induced by Strong NA+-Lipid Interactions and Finite Size Effects Biophys. J. 2008, 94, 3565-3576
    • (2008) Biophys. J. , vol.94 , pp. 3565-3576
    • Lee, S.-J.1    Song, Y.2    Baker, N.A.3
  • 46
    • 33646170214 scopus 로고    scopus 로고
    • Simulation-Based Methods for Interpreting X-ray Data from Lipid Bilayers
    • Klauda, J. B.; Kucerka, N.; Brooks, B. R.; Pastor, R. W.; Nagle, J. F. Simulation-Based Methods for Interpreting X-ray Data from Lipid Bilayers Biophys. J. 2006, 90, 2796-2807
    • (2006) Biophys. J. , vol.90 , pp. 2796-2807
    • Klauda, J.B.1    Kucerka, N.2    Brooks, B.R.3    Pastor, R.W.4    Nagle, J.F.5
  • 47
    • 0027375156 scopus 로고
    • The Use of Differential Scanning Calorimetry as a Tool to Characterize Liposome Preparations
    • Biltonen, R. L.; Lichtenberg, D. The Use of Differential Scanning Calorimetry as a Tool to Characterize Liposome Preparations Chem. Phys. Lipids 1993, 64, 129-142
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 129-142
    • Biltonen, R.L.1    Lichtenberg, D.2
  • 49
    • 0000035913 scopus 로고    scopus 로고
    • Temperature Dependence of TIP3P, SPC, and TIP4P Water from NPT Monte Carlo Simulations: Seeking Temperatures of Maximum Density
    • Jorgensen, W. L.; Jenson, C. Temperature Dependence of TIP3P, SPC, and TIP4P Water from NPT Monte Carlo Simulations: Seeking Temperatures of Maximum Density J. Comput. Chem. 1998, 19, 1179-1186
    • (1998) J. Comput. Chem. , vol.19 , pp. 1179-1186
    • Jorgensen, W.L.1    Jenson, C.2
  • 50
    • 33646940952 scopus 로고
    • Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n -Alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n -Alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 51
    • 33846823909 scopus 로고
    • Particle Mesh Ewald: An N log(N) Method for Ewald Sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald: An N log(N) Method for Ewald Sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 52
    • 84943502952 scopus 로고
    • A Molecular Dynamics Methods for Simulations in the Canonical Ensemble
    • Nosé, S. A Molecular Dynamics Methods for Simulations in the Canonical Ensemble Mol. Phys. 1984, 52, 255-268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nosé, S.1
  • 53
    • 0001082095 scopus 로고
    • Constant-Temperature Molecular Dynamics
    • Nosé, S. Constant-Temperature Molecular Dynamics J. Phys.: Condens. Matter 1990, 2, SA115-SA119
    • (1990) J. Phys.: Condens. Matter , vol.2
    • Nosé, S.1
  • 55
    • 4344660645 scopus 로고    scopus 로고
    • Overcoming Free Energy Barriers Using Unconstrained Molecular Dynamics Simulations
    • Hénin, J.; Chipot, C. Overcoming Free Energy Barriers Using Unconstrained Molecular Dynamics Simulations J. Chem. Phys. 2004, 121, 2904-2914
    • (2004) J. Chem. Phys. , vol.121 , pp. 2904-2914
    • Hénin, J.1    Chipot, C.2
  • 56
    • 29744459271 scopus 로고    scopus 로고
    • Exploring the Free-Energy Landscape of a Short Peptide Using an Average Force
    • Chipot, C.; Hénin, J. Exploring the Free-Energy Landscape of a Short Peptide Using an Average Force J. Chem. Phys. 2005, 123, 244906-6
    • (2005) J. Chem. Phys. , vol.123 , pp. 244906-244916
    • Chipot, C.1    Hénin, J.2
  • 58
    • 0035935802 scopus 로고    scopus 로고
    • Calculating Free Energies Using Average Force
    • Darve, E.; Pohorille, A. Calculating Free Energies Using Average Force J. Chem. Phys. 2001, 115, 9169-9183
    • (2001) J. Chem. Phys. , vol.115 , pp. 9169-9183
    • Darve, E.1    Pohorille, A.2
  • 59
    • 1642617408 scopus 로고    scopus 로고
    • Assessing the Efficiency of Free Energy Calculation Methods
    • Rodríguez-Gómez, D.; Darve, E.; Pohorille, A. Assessing the Efficiency of Free Energy Calculation Methods J. Chem. Phys. 2004, 120, 3563-3578
    • (2004) J. Chem. Phys. , vol.120 , pp. 3563-3578
    • Rodríguez-Gómez, D.1    Darve, E.2    Pohorille, A.3
  • 60
    • 42149194240 scopus 로고    scopus 로고
    • Adaptive Biasing Force Method for Scalar and Vector Free Energy Calculations
    • Darve, E.; Rodríguez-Gómez, D.; Pohorille, A. Adaptive Biasing Force Method for Scalar and Vector Free Energy Calculations J. Chem. Phys. 2008, 128, 144120-1-144120-13
    • (2008) J. Chem. Phys. , vol.128 , pp. 1441201-14412013
    • Darve, E.1    Rodríguez-Gómez, D.2    Pohorille, A.3
  • 61
    • 77950102787 scopus 로고    scopus 로고
    • Exploring Multidimensional Free Energy Landscapes Using Time-Dependent Biases on Collective Variables
    • Hénin, J.; Fiorin, G.; Chipot, C.; Klein, M. L. Exploring Multidimensional Free Energy Landscapes Using Time-Dependent Biases on Collective Variables J. Chem. Theory Comput. 2010, 6, 35-47
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 35-47
    • Hénin, J.1    Fiorin, G.2    Chipot, C.3    Klein, M.L.4
  • 62
    • 84869020572 scopus 로고    scopus 로고
    • Exact Relation between Potential of Mean Force and Free-Energy Profile
    • Wong, K. Y.; York, D. M. Exact Relation between Potential of Mean Force and Free-Energy Profile J. Chem. Theory Comput. 2012, 8, 3998-4003
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 3998-4003
    • Wong, K.Y.1    York, D.M.2
  • 63
    • 36549102647 scopus 로고
    • Error Estimates on Averages of Correlated Data
    • Flyvbjerg, H.; Petersen, H. G. Error Estimates on Averages of Correlated Data J. Chem. Phys. 1989, 461-467
    • (1989) J. Chem. Phys. , pp. 461-467
    • Flyvbjerg, H.1    Petersen, H.G.2
  • 64
    • 84875803167 scopus 로고    scopus 로고
    • Free Energetics and the Role of Water in the Permeation of Methyl Guanidinium Across the Bilayer-Water Interface: Insights from Molecular Dynamics Simulations Using Charge Equilibration Potentials
    • Ou, S.; Lucas, T. R.; Zhong, Y.; Bauer, B. A.; Hu, Y.; Patel, S. Free Energetics and the Role of Water in the Permeation of Methyl Guanidinium Across the Bilayer-Water Interface: Insights from Molecular Dynamics Simulations Using Charge Equilibration Potentials J. Phys. Chem. B 2013, 117, 3578-92
    • (2013) J. Phys. Chem. B , vol.117 , pp. 3578-3592
    • Ou, S.1    Lucas, T.R.2    Zhong, Y.3    Bauer, B.A.4    Hu, Y.5    Patel, S.6
  • 66
    • 34247626293 scopus 로고    scopus 로고
    • Partitioning of Amino Acid Side Chains into Lipid Bilayers: Results from Computer Simulations and Comparison to Experiment
    • MacCallum, J. L.; Bennett, W. F. D.; Tieleman, D. P. Partitioning of Amino Acid Side Chains into Lipid Bilayers: Results from Computer Simulations and Comparison to Experiment J. Gen. Physiol. 2007, 129, 371-377
    • (2007) J. Gen. Physiol. , vol.129 , pp. 371-377
    • Maccallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 67
    • 0029941271 scopus 로고    scopus 로고
    • Energetics of Hydrogen Bonding in Proteins: A Model Compound Study
    • Habermann, S. M.; Murphy, K. P. Energetics of Hydrogen Bonding in Proteins: A Model Compound Study Protein Sci. 1996, 5, 1229-1239
    • (1996) Protein Sci. , vol.5 , pp. 1229-1239
    • Habermann, S.M.1    Murphy, K.P.2
  • 68
    • 43649094583 scopus 로고    scopus 로고
    • Distribution of Amino Acids in a Lipid Bilayer from Computer Simulations
    • MacCallum, J. L.; Bennett, W. F. D.; Tieleman, D. P. Distribution of Amino Acids in a Lipid Bilayer from Computer Simulations Biophys. J. 2008, 94, 3393-3404
    • (2008) Biophys. J. , vol.94 , pp. 3393-3404
    • Maccallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 69
    • 77953589882 scopus 로고    scopus 로고
    • Electrostatics of Deformable Lipid Membranes
    • Vorobyov, I.; Bekker, B.; Allen, T. W. Electrostatics of Deformable Lipid Membranes Biophys. J. 2010, 98, 2904-2913
    • (2010) Biophys. J. , vol.98 , pp. 2904-2913
    • Vorobyov, I.1    Bekker, B.2    Allen, T.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.