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Volumn 104, Issue 2, 2013, Pages 412-420

Free energy of translocating an arginine-rich cell-penetrating peptide across a lipid bilayer suggests pore formation

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CELL PENETRATING PEPTIDE; WATER;

EID: 84872818385     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.10.027     Document Type: Article
Times cited : (88)

References (55)
  • 1
    • 33747038452 scopus 로고    scopus 로고
    • Cell-penetrating peptides - A brief introduction
    • P. Järver, and Ü. Langel Cell-penetrating peptides - a brief introduction Biochim. Biophys. Acta 1758 2006 260 263
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 260-263
    • Järver, P.1    Langel, Ü.2
  • 2
    • 0141942113 scopus 로고    scopus 로고
    • A brief introduction to cell-penetrating peptides
    • P. Lundberg, and Ü. Langel A brief introduction to cell-penetrating peptides J. Mol. Recognit. 16 2003 227 233
    • (2003) J. Mol. Recognit. , vol.16 , pp. 227-233
    • Lundberg, P.1    Langel, Ü.2
  • 3
    • 13844254266 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Mechanism and kinetics of cargo delivery
    • M. Zorko, and Ü. Langel Cell-penetrating peptides: mechanism and kinetics of cargo delivery Adv. Drug Deliv. Rev. 57 2005 529 545
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 529-545
    • Zorko, M.1    Langel, Ü.2
  • 4
    • 0346460957 scopus 로고    scopus 로고
    • Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake
    • J.P. Richard, and K. Melikov B. Lebleu Cell-penetrating peptides. A reevaluation of the mechanism of cellular uptake J. Biol. Chem. 278 2003 585 590
    • (2003) J. Biol. Chem. , vol.278 , pp. 585-590
    • Richard, J.P.1    Melikov, K.2    Lebleu, B.3
  • 5
    • 0038726020 scopus 로고    scopus 로고
    • Uptake of analogs of penetratin, Tat(48-60) and oligoarginine in live cells
    • P.E. Thorén, and D. Persson B. Nordén Uptake of analogs of penetratin, Tat(48-60) and oligoarginine in live cells Biochem. Biophys. Res. Commun. 307 2003 100 107
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 100-107
    • Thorén, P.E.1    Persson, D.2    Nordén, B.3
  • 6
    • 0038387344 scopus 로고    scopus 로고
    • TAT peptide internalization: Seeking the mechanism of entry
    • E. Vivès, and J.P. Richard B. Lebleu TAT peptide internalization: seeking the mechanism of entry Curr. Protein Pept. Sci. 4 2003 125 132
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 125-132
    • Vivès, E.1    Richard, J.P.2    Lebleu, B.3
  • 7
    • 0041698459 scopus 로고    scopus 로고
    • "Translocatory proteins" and "protein transduction domains": A critical analysis of their biological effects and the underlying mechanisms
    • J.A. Leifert, and J.L. Whitton "Translocatory proteins" and "protein transduction domains": a critical analysis of their biological effects and the underlying mechanisms Mol. Ther. 8 2003 13 20
    • (2003) Mol. Ther. , vol.8 , pp. 13-20
    • Leifert, J.A.1    Whitton, J.L.2
  • 8
    • 63649127300 scopus 로고    scopus 로고
    • Cell entry of arginine-rich peptides is independent of endocytosis
    • G. Ter-Avetisyan, and G. Tünnemann M.C. Cardoso Cell entry of arginine-rich peptides is independent of endocytosis J. Biol. Chem. 284 2009 3370 3378
    • (2009) J. Biol. Chem. , vol.284 , pp. 3370-3378
    • Ter-Avetisyan, G.1    Tünnemann, G.2    Cardoso, M.C.3
  • 9
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat
    • M. Silhol, and M. Tyagi E. Vivès Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat Eur. J. Biochem. 269 2002 494 501
    • (2002) Eur. J. Biochem. , vol.269 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Vivès, E.3
  • 11
    • 77951902057 scopus 로고    scopus 로고
    • Arginine-rich cell-penetrating peptides
    • N. Schmidt, and A. Mishra G.C. Wong Arginine-rich cell-penetrating peptides FEBS Lett. 584 2010 1806 1813
    • (2010) FEBS Lett. , vol.584 , pp. 1806-1813
    • Schmidt, N.1    Mishra, A.2    Wong, G.C.3
  • 12
    • 77958154973 scopus 로고    scopus 로고
    • Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells
    • I.D. Alves, and C.Y. Jiao S. Sagan Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells Biochim. Biophys. Acta 1798 2010 2231 2239
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 2231-2239
    • Alves, I.D.1    Jiao, C.Y.2    Sagan, S.3
  • 13
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • D.J. Mitchell, and D.T. Kim J.B. Rothbard Polyarginine enters cells more efficiently than other polycationic homopolymers J. Pept. Res. 56 2000 318 325
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Rothbard, J.B.3
  • 14
    • 28844454642 scopus 로고    scopus 로고
    • Arginine-rich cell penetrating peptides: From endosomal uptake to nuclear delivery
    • K. Melikov, and L.V. Chernomordik Arginine-rich cell penetrating peptides: from endosomal uptake to nuclear delivery Cell. Mol. Life Sci. 62 2005 2739 2749
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2739-2749
    • Melikov, K.1    Chernomordik, L.V.2
  • 15
    • 0034613057 scopus 로고    scopus 로고
    • The Antennapedia peptide penetratin translocates across lipid bilayers - The first direct observation
    • P.E. Thorén, and D. Persson B. Nordén The Antennapedia peptide penetratin translocates across lipid bilayers - the first direct observation FEBS Lett. 482 2000 265 268
    • (2000) FEBS Lett. , vol.482 , pp. 265-268
    • Thorén, P.E.1    Persson, D.2    Nordén, B.3
  • 16
    • 77954374712 scopus 로고    scopus 로고
    • Cell-penetrating HIV1 TAT peptides can generate pores in model membranes
    • C. Ciobanasu, J.P. Siebrasse, and U. Kubitscheck Cell-penetrating HIV1 TAT peptides can generate pores in model membranes Biophys. J. 99 2010 153 162
    • (2010) Biophys. J. , vol.99 , pp. 153-162
    • Ciobanasu, C.1    Siebrasse, J.P.2    Kubitscheck, U.3
  • 17
    • 79960104118 scopus 로고    scopus 로고
    • Penetration without cells: Membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles
    • P. Säälik, and A. Niinep M. Pooga Penetration without cells: membrane translocation of cell-penetrating peptides in the model giant plasma membrane vesicles J. Control. Release 153 2011 117 125
    • (2011) J. Control. Release , vol.153 , pp. 117-125
    • Säälik, P.1    Niinep, A.2    Pooga, M.3
  • 18
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides
    • H.D. Herce, and A.E. Garcia V. Milesi Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides Biophys. J. 97 2009 1917 1925
    • (2009) Biophys. J. , vol.97 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Milesi, V.3
  • 19
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • H.D. Herce, and A.E. Garcia Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes Proc. Natl. Acad. Sci. USA 104 2007 20805 20810
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 20
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • M. Tang, A.J. Waring, and M. Hong Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR J. Am. Chem. Soc. 129 2007 11438 11446
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 21
    • 77949795332 scopus 로고    scopus 로고
    • Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy
    • S. Li, and Y. Su M. Hong Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy J. Phys. Chem. B 114 2010 4063 4069
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4063-4069
    • Li, S.1    Su, Y.2    Hong, M.3
  • 22
    • 84864435306 scopus 로고    scopus 로고
    • Insertion mechanism of cell-penetrating peptides into supported phospholipid membranes revealed by x-ray and neutron reflection
    • D. Choi, and J.H. Moon K. Shin Insertion mechanism of cell-penetrating peptides into supported phospholipid membranes revealed by x-ray and neutron reflection Soft Matter 8 2012 8294 8297
    • (2012) Soft Matter , vol.8 , pp. 8294-8297
    • Choi, D.1    Moon, J.H.2    Shin, K.3
  • 23
    • 84877755819 scopus 로고    scopus 로고
    • Backbone rigidity and static presentation of guanidinium groups increases cellular uptake of arginine-rich cell-penetrating peptides
    • G. Lättig-Tünnemann, and M. Prinz M.C. Cardoso Backbone rigidity and static presentation of guanidinium groups increases cellular uptake of arginine-rich cell-penetrating peptides Nat Commun 2 2011 453
    • (2011) Nat Commun , vol.2 , pp. 453
    • Lättig-Tünnemann, G.1    Prinz, M.2    Cardoso, M.C.3
  • 24
    • 83455177932 scopus 로고    scopus 로고
    • Statistical convergence of equilibrium properties in simulations of molecular solutes embedded in lipid bilayers
    • C. Neale, and W.F.D. Bennett R. Pomès Statistical convergence of equilibrium properties in simulations of molecular solutes embedded in lipid bilayers J. Chem. Theory Comput. 7 2011 4175 4188
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 4175-4188
    • Neale, C.1    Bennett, W.F.D.2    Pomès, R.3
  • 25
    • 0037678992 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl
    • S.A. Pandit, D. Bostick, and M.L. Berkowitz Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl Biophys. J. 84 2003 3743 3750
    • (2003) Biophys. J. , vol.84 , pp. 3743-3750
    • Pandit, S.A.1    Bostick, D.2    Berkowitz, M.L.3
  • 26
    • 43649093151 scopus 로고    scopus 로고
    • +-lipid interactions and finite size effects
    • +-lipid interactions and finite size effects Biophys. J. 94 2008 3565 3576
    • (2008) Biophys. J. , vol.94 , pp. 3565-3576
    • Lee, S.J.1    Song, Y.2    Baker, N.A.3
  • 27
    • 43649094583 scopus 로고    scopus 로고
    • Distribution of amino acids in a lipid bilayer from computer simulations
    • J. MacCallum, W. Bennett, and D. Tieleman Distribution of amino acids in a lipid bilayer from computer simulations Biophys. J. 94 2008 3393 3404
    • (2008) Biophys. J. , vol.94 , pp. 3393-3404
    • MacCallum, J.1    Bennett, W.2    Tieleman, D.3
  • 28
    • 81055154363 scopus 로고    scopus 로고
    • Arginine residues at internal positions in a protein are always charged
    • M.J. Harms, and J.L. Schlessman B. García-Moreno Arginine residues at internal positions in a protein are always charged Proc. Natl. Acad. Sci. USA 108 2011 18954 18959
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 18954-18959
    • Harms, M.J.1    Schlessman, J.L.2    García-Moreno, B.3
  • 29
    • 84986519238 scopus 로고
    • Weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • S. Kumar, and J. Rosenberg P. Kollman The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method J. Comput. Chem. 13 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.2    Kollman, P.3
  • 30
    • 0035277126 scopus 로고    scopus 로고
    • Extension to the weighted histogram analysis method: Combining umbrella sampling with free energy calculations
    • M. Souaille, and B. Roux Extension to the weighted histogram analysis method: combining umbrella sampling with free energy calculations Comput. Phys. Commun. 135 2001 40 57
    • (2001) Comput. Phys. Commun. , vol.135 , pp. 40-57
    • Souaille, M.1    Roux, B.2
  • 32
    • 80052468548 scopus 로고    scopus 로고
    • Transfer of arginine into lipid bilayers is nonadditive
    • J.L. MacCallum, W.F. Bennett, and D.P. Tieleman Transfer of arginine into lipid bilayers is nonadditive Biophys. J. 101 2011 110 117
    • (2011) Biophys. J. , vol.101 , pp. 110-117
    • MacCallum, J.L.1    Bennett, W.F.2    Tieleman, D.P.3
  • 33
    • 0035812110 scopus 로고    scopus 로고
    • Effect of undulations on surface tension in simulated bilayers
    • S. Marrink, and A. Mark Effect of undulations on surface tension in simulated bilayers J. Phys. Chem. B 105 2001 6122 6127
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6122-6127
    • Marrink, S.1    Mark, A.2
  • 34
    • 34247633528 scopus 로고    scopus 로고
    • On the thermodynamic stability of a charged arginine side chain in a transmembrane helix
    • S. Dorairaj, and T.W. Allen On the thermodynamic stability of a charged arginine side chain in a transmembrane helix Proc. Natl. Acad. Sci. USA 104 2007 4943 4948
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4943-4948
    • Dorairaj, S.1    Allen, T.W.2
  • 35
    • 80054729137 scopus 로고    scopus 로고
    • Outer membrane phospholipase A in phospholipid bilayers: A model system for concerted computational and experimental investigations of amino acid side chain partitioning into lipid bilayers
    • P.J. Fleming, and J.A. Freites K.G. Fleming Outer membrane phospholipase A in phospholipid bilayers: a model system for concerted computational and experimental investigations of amino acid side chain partitioning into lipid bilayers Biochim. Biophys. Acta 1818 2012 126 134
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 126-134
    • Fleming, P.J.1    Freites, J.A.2    Fleming, K.G.3
  • 36
    • 84855437583 scopus 로고    scopus 로고
    • The role of membrane thickness in charged protein-lipid interactions
    • L.B. Li, I. Vorobyov, and T.W. Allen The role of membrane thickness in charged protein-lipid interactions Biochim. Biophys. Acta 1818 2012 135 145
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 135-145
    • Li, L.B.1    Vorobyov, I.2    Allen, T.W.3
  • 37
    • 34547649222 scopus 로고    scopus 로고
    • Free energy of a trans-membrane pore calculated from atomistic molecular dynamics simulations
    • J. Wohlert, and W.K. den Otter W.J. Briels Free energy of a trans-membrane pore calculated from atomistic molecular dynamics simulations J. Chem. Phys. 124 2006 154905
    • (2006) J. Chem. Phys. , vol.124 , pp. 154905
    • Wohlert, J.1    Den Otter, W.K.2    Briels, W.J.3
  • 38
    • 33749182054 scopus 로고    scopus 로고
    • Lipids out of equilibrium: Energetics of desorption and pore mediated flip-flop
    • D.P. Tieleman, and S.J. Marrink Lipids out of equilibrium: energetics of desorption and pore mediated flip-flop J. Am. Chem. Soc. 128 2006 12462 12467
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12462-12467
    • Tieleman, D.P.1    Marrink, S.J.2
  • 39
    • 69349095310 scopus 로고    scopus 로고
    • Thermodynamics of flip-flop and desorption for a systematic series of phosphatidylcholine lipids
    • N. Sapay, W. Bennett, and D. Tieleman Thermodynamics of flip-flop and desorption for a systematic series of phosphatidylcholine lipids Soft Matter 5 2009 3295 3302
    • (2009) Soft Matter , vol.5 , pp. 3295-3302
    • Sapay, N.1    Bennett, W.2    Tieleman, D.3
  • 40
    • 0035812426 scopus 로고    scopus 로고
    • Simulation of the spontaneous aggregation of phospholipids into bilayers
    • S.J. Marrink, and E. Lindahl A.E. Mark Simulation of the spontaneous aggregation of phospholipids into bilayers J. Am. Chem. Soc. 123 2001 8638 8639
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8638-8639
    • Marrink, S.J.1    Lindahl, E.2    Mark, A.E.3
  • 41
    • 1842738717 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the spontaneous formation of a small DPPC vesicle in water in atomistic detail
    • A.H. de Vries, A.E. Mark, and S.J. Marrink Molecular dynamics simulation of the spontaneous formation of a small DPPC vesicle in water in atomistic detail J. Am. Chem. Soc. 126 2004 4488 4489
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4488-4489
    • De Vries, A.H.1    Mark, A.E.2    Marrink, S.J.3
  • 42
    • 68949116150 scopus 로고    scopus 로고
    • Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers
    • S. Yesylevskyy, S.J. Marrink, and A.E. Mark Alternative mechanisms for the interaction of the cell-penetrating peptides penetratin and the TAT peptide with lipid bilayers Biophys. J. 97 2009 40 49
    • (2009) Biophys. J. , vol.97 , pp. 40-49
    • Yesylevskyy, S.1    Marrink, S.J.2    Mark, A.E.3
  • 43
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • H. Berendsen, D. van der Spoel, and R. van Drunen GROMACS: a message-passing parallel molecular dynamics implementation Comput. Phys. Commun. 91 1995 43 56
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 43-56
    • Berendsen, H.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 44
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, and C. Kutzner E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 46
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • O. Berger, O. Edholm, and F. Jähnig Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys. J. 72 1997 2002 2013
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jähnig, F.3
  • 47
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Reidel Dordrecht, the Netherlands
    • H. Berendsen, and J. Postma J. Hermans Interaction models for water in relation to protein hydration Intermolecular Forces 1981 Reidel Dordrecht, the Netherlands 331 342
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.1    Postma, J.2    Hermans, J.3
  • 48
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • G. Bussi, D. Donadio, and M. Parrinello Canonical sampling through velocity rescaling J. Chem. Phys. 126 2007 014101
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 49
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • H. Berendsen, and J. Postma J. Haak Molecular dynamics with coupling to an external bath J. Chem. Phys. 81 1984 3684
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684
    • Berendsen, H.1    Postma, J.2    Haak, J.3
  • 50
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log (N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N log (N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 51
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • S. Miyamoto, and P. Kollman SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 13 1992 952 962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.2
  • 52
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • B. Hess, and H. Bekker J. Fraaije LINCS: a linear constraint solver for molecular simulations J. Comput. Chem. 18 1997 1463 1472
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Fraaije, J.3
  • 53
    • 78650186363 scopus 로고    scopus 로고
    • Lipidbook: A public repository for force-field parameters used in membrane simulations
    • J. Domański, and P.J. Stansfeld O. Beckstein Lipidbook: a public repository for force-field parameters used in membrane simulations J. Membr. Biol. 236 2010 255 258
    • (2010) J. Membr. Biol. , vol.236 , pp. 255-258
    • Domański, J.1    Stansfeld, P.J.2    Beckstein, O.3
  • 54
    • 69949118458 scopus 로고    scopus 로고
    • PACKMOL: A package for building initial configurations for molecular dynamics simulations
    • L. Martínez, and R. Andrade J.M. Martínez PACKMOL: a package for building initial configurations for molecular dynamics simulations J. Comput. Chem. 30 2009 2157 2164
    • (2009) J. Comput. Chem. , vol.30 , pp. 2157-2164
    • Martínez, L.1    Andrade, R.2    Martínez, J.M.3
  • 55
    • 0004313709 scopus 로고    scopus 로고
    • Ver. 2007-09 Chemical Computing Group, Montreal, Quebec, Canada
    • Molecular Operating Environment, Ver. 2007-09. 2007. Chemical Computing Group, Montreal, Quebec, Canada.
    • (2007) Molecular Operating Environment


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