메뉴 건너뛰기




Volumn 8, Issue 5, 2012, Pages 1556-1569

Modeling the self-assembly and stability of DHPC micelles using atomic resolution and coarse grained MD simulations

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84860731699     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct200921u     Document Type: Article
Times cited : (35)

References (60)
  • 1
    • 17844410935 scopus 로고    scopus 로고
    • Spontaneous formation of detergent micelles around the outer membrane protein OmpX
    • DOI 10.1529/biophysj.105.060426
    • Böckmann, R. A.; Caflisch, A. Spontaneous Formation of Detergent Micelles around the Outer Membrane Protein OmpX Biophys. J. 2005, 88, 3191-3204 (Pubitemid 40586572)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3191-3204
    • Bockmann, R.A.1    Caflisch, A.2
  • 5
    • 0034499269 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of the Kinetics of Spontaneous Micelle Formation
    • Marrink, S. J.; Tieleman, D. P.; Mark, A. E. Molecular Dynamics Simulation of the Kinetics of Spontaneous Micelle Formation J. Phys. Chem. B 2000, 104, 12165-12173
    • (2000) J. Phys. Chem. B , vol.104 , pp. 12165-12173
    • Marrink, S.J.1    Tieleman, D.P.2    Mark, A.E.3
  • 8
    • 77953810629 scopus 로고    scopus 로고
    • Spatial Structure of the Transmembrane Domain Heterodimer of ErbB1 and ErbB2 Receptor Tyrosine Kinases
    • Mineev, K. S.; Bocharov, E. V.; Pustovalova, Y. E.; Bocharova, O. V.; Chupin, V. V.; Arseniev, A. S. Spatial Structure of the Transmembrane Domain Heterodimer of ErbB1 and ErbB2 Receptor Tyrosine Kinases J. Mol. Biol. 2010, 400, 231-243
    • (2010) J. Mol. Biol. , vol.400 , pp. 231-243
    • Mineev, K.S.1    Bocharov, E.V.2    Pustovalova, Y.E.3    Bocharova, O.V.4    Chupin, V.V.5    Arseniev, A.S.6
  • 10
    • 77953547641 scopus 로고    scopus 로고
    • Atomistic Simulations of Bicelle Mixtures
    • Jiang, Y.; Wang, H.; Kindt, J. T. Atomistic Simulations of Bicelle Mixtures Biophys. J. 2010, 98, 2895-2903
    • (2010) Biophys. J. , vol.98 , pp. 2895-2903
    • Jiang, Y.1    Wang, H.2    Kindt, J.T.3
  • 11
    • 33847765026 scopus 로고    scopus 로고
    • Simulations of edge behavior in a mixed-lipid bilayer: Fluctuation analysis
    • Jiang, Y.; Kindt, J. T. Simulations of edge behavior in a mixed-lipid bilayer: Fluctuation analysis J. Chem. Phys. 2007, 126, 045105-1-045105-9
    • (2007) J. Chem. Phys. , vol.126 , pp. 0451051-0451059
    • Jiang, Y.1    Kindt, J.T.2
  • 12
    • 55549092456 scopus 로고    scopus 로고
    • Bilayer Edge and Curvature Effects on Partitioning of Lipids by Tail Length: Atomistic Simulations
    • Wang, H.; de Joannis, J.; Jiang, Y.; Gaulding, J. C.; Albrecht, B.; Yin, F.; Khanna, K.; Kindt, J. T. Bilayer Edge and Curvature Effects on Partitioning of Lipids by Tail Length: Atomistic Simulations Biophys. J. 2008, 95, 2647-2657
    • (2008) Biophys. J. , vol.95 , pp. 2647-2657
    • Wang, H.1    De Joannis, J.2    Jiang, Y.3    Gaulding, J.C.4    Albrecht, B.5    Yin, F.6    Khanna, K.7    Kindt, J.T.8
  • 13
    • 65249151900 scopus 로고    scopus 로고
    • Lipid Models for United-Atom Molecular Dynamics Simulations of Proteins
    • Kukol, A. Lipid Models for United-Atom Molecular Dynamics Simulations of Proteins J. Chem. Theory Comput. 2009, 5, 615-626
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 615-626
    • Kukol, A.1
  • 14
    • 3042767203 scopus 로고    scopus 로고
    • Characterization of phospholipid mixed micelles by translational diffusion
    • DOI 10.1023/B:JNMR.0000032560.43738.6a
    • Chou, J. J.; Baber, J. L.; Bax, A. Characterization of phospholipid mixed micelles by translational diffusion J. Biomol. NMR 2004, 29, 299-308 (Pubitemid 38864828)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.3 , pp. 299-308
    • Chou, J.J.1    Baber, J.L.2    Bax, A.3
  • 15
    • 0009854860 scopus 로고
    • Monomer-to-micelle transition of dihexanoylphosphatidylcholine: Carbon-13 NMR and Raman studies
    • Burns, R. A.; Roberts, M. F.; Dluhy, R.; Mendelsohn, R. Monomer-to-micelle transition of dihexanoylphosphatidylcholine: carbon-13 NMR and Raman studies J. Am. Chem. Soc. 1982, 104, 430-438
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 430-438
    • Burns, R.A.1    Roberts, M.F.2    Dluhy, R.3    Mendelsohn, R.4
  • 16
    • 0015971059 scopus 로고
    • Physical chemical studies of short-chain lecithin homologues. II Micellar weights of dihexanoyl- and diheptanoyllecithin
    • Tausk, R. J. M.; Esch, J. v.; Karmiggelt, J.; Voordouw, G.; Overbeek, J. T. G. Physical chemical studies of short-chain lecithin homologues. II Micellar weights of dihexanoyl- and diheptanoyllecithin Biophys. Chem. 1974, 1, 184-203
    • (1974) Biophys. Chem. , vol.1 , pp. 184-203
    • Tausk, R.J.M.1    E, J.V.2    Karmiggelt, J.3    Voordouw, G.4    Overbeek, J.T.G.5
  • 17
    • 0016238907 scopus 로고
    • Physical chemical studies of short-chain lecithin homologues III. Phase separation and light scattering studies on aqueous dioctanoyllecithin solutions
    • Tausk, R. J. M.; Oudshoorn, C.; Overbeek, J. T. G. Physical chemical studies of short-chain lecithin homologues III. Phase separation and light scattering studies on aqueous dioctanoyllecithin solutions Biophys. Chem. 1974, 2, 53-63
    • (1974) Biophys. Chem. , vol.2 , pp. 53-63
    • Tausk, R.J.M.1    Oudshoorn, C.2    Overbeek, J.T.G.3
  • 18
    • 0034707098 scopus 로고    scopus 로고
    • Short-chain phospholipids as detergents
    • Helmut, H. Short-chain phospholipids as detergents Biochim. Biophys. Acta. Biomembr. 2000, 1508, 164-181
    • (2000) Biochim. Biophys. Acta. Biomembr. , vol.1508 , pp. 164-181
    • Helmut, H.1
  • 19
    • 0015222018 scopus 로고
    • Studies on Phospholipase A and its Zymogen from Porcine Pancreas: III. Action of the Enzyme on Short-chain Lecithins
    • De Haas, G. H.; Bonsen, P. P. M; Pieterson, W. A.; Van Deenen, L. L. M. Studies on Phospholipase A and its Zymogen from Porcine Pancreas: III. Action of the Enzyme on Short-chain Lecithins Biochim. Biophys. Acta 1971, 239, 252-266
    • (1971) Biochim. Biophys. Acta , vol.239 , pp. 252-266
    • De Haas, G.H.1    Bonsen, P.P.M.2    Pieterson, W.A.3    Van Deenen, L.L.M.4
  • 20
    • 0019451876 scopus 로고
    • Thermodynamics of dihexanoylphosphatidylcholine aggregation
    • DOI 10.1021/bi00517a044
    • Johnson, R. E.; Wells, M. A.; Rupley, J. A. Thermodynamics of dihexanoylphosphatidylcholine aggregation Biochemistry (N. Y.) 1981, 20, 4239-4242 (Pubitemid 11012535)
    • (1981) Biochemistry , vol.20 , Issue.14 , pp. 4239-4242
    • Johnson, R.E.1    Wells, M.A.2    Rupley, J.A.3
  • 21
    • 33845374873 scopus 로고
    • The use of small-angle neutron scattering to determine the structure and interaction of dihexanoylphosphatidylcholine micelles
    • Lin, T. L.; Chen, S. H.; Gabriel, N. E.; Roberts, M. F. The use of small-angle neutron scattering to determine the structure and interaction of dihexanoylphosphatidylcholine micelles J. Am. Chem. Soc. 1986, 108, 3499-3507
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 3499-3507
    • Lin, T.L.1    Chen, S.H.2    Gabriel, N.E.3    Roberts, M.F.4
  • 22
    • 0019330575 scopus 로고
    • Polar group conformation of phosphatidylcholine. Effect of solvent and aggregation
    • Hauser, H. Polar group conformation of phosphatidylcholine. Effect of solvent and aggregation Biochemistry 1980, 19, 366-373
    • (1980) Biochemistry , vol.19 , pp. 366-373
    • Hauser, H.1
  • 23
    • 0001723126 scopus 로고
    • Studies of the use of dihexanoyllecithin and other lecithins as substrates for phospholipase A: With addendum on aspects of micelle properties of dihexanoyllecithin
    • Roholt, O. A.; Schlamowitz, M. Studies of the use of dihexanoyllecithin and other lecithins as substrates for phospholipase A: With addendum on aspects of micelle properties of dihexanoyllecithin Arch. Biochem. Biophys. 1961, 94, 364-379
    • (1961) Arch. Biochem. Biophys. , vol.94 , pp. 364-379
    • Roholt, O.A.1    Schlamowitz, M.2
  • 24
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B.; Kutzner, C.; van, d. S.; 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, D.S.3    Lindahl, E.4
  • 27
    • 1642485164 scopus 로고    scopus 로고
    • Coarse Grained Model for Semiquantitative Lipid Simulations
    • Marrink, S. J.; de Vries, A. H.; Mark, A. E. Coarse Grained Model for Semiquantitative Lipid Simulations J. Phys. Chem. B 2004, 108, 750-760
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 28
    • 0001283690 scopus 로고
    • The structure of a highly concentrated aqueous solution of lithium chloride
    • Copestake, A. P.; Neilson, G. W.; Enderby, J. E. The structure of a highly concentrated aqueous solution of lithium chloride J. Phys. C 1985, 18, 4211-4216
    • (1985) J. Phys. C , vol.18 , pp. 4211-4216
    • Copestake, A.P.1    Neilson, G.W.2    Enderby, J.E.3
  • 30
    • 70350238527 scopus 로고    scopus 로고
    • Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions
    • Rzepiela, A. J.; Sengupta, D.; Goga, N.; Marrink, S. J. Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions Faraday Discuss. 2010, 144, 431-443
    • (2010) Faraday Discuss. , vol.144 , pp. 431-443
    • Rzepiela, A.J.1    Sengupta, D.2    Goga, N.3    Marrink, S.J.4
  • 31
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; Van Gunsteren, W. F. A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6 J. Comput. Chem. 2004, 25, 1656-1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 32
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger, O.; Edholm, O.; Jähnig, F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature Biophys. J. 1997, 72, 2002-2013 (Pubitemid 27184429)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 34
    • 0002775934 scopus 로고
    • Interaction Models for Water in Relation to Protein Hydration
    • Pullman, B. D. Reidel Publishing
    • Berendsen, H. J. C.; Postma, J. P.; van Gunsteren, W. F.; Hermans, J. Interaction Models for Water in Relation to Protein Hydration. In Intermolecular Forces; Pullman, B., Ed.; D. Reidel Publishing: 1981; pp 331-342.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 36
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation
    • Hess, B. P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation J. Chem. Theory Comput. 2008, 4, 116-122
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 38
    • 33644893631 scopus 로고    scopus 로고
    • Coarse Grained Protein -Lipid Model with Application to Lipoprotein Particles
    • Shih, A. Y.; Arkhipov, A.; Freddolino, P. L.; Schulten, K. Coarse Grained Protein -Lipid Model with Application to Lipoprotein Particles J. Phys. Chem. B 2006, 110, 3674-3684
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3674-3684
    • Shih, A.Y.1    Arkhipov, A.2    Freddolino, P.L.3    Schulten, K.4
  • 39
    • 33847193915 scopus 로고    scopus 로고
    • Assembly of lipoprotein particles revealed by coarse-grained molecular dynamics simulations
    • Shih, A. Y.; Freddolino, P. L.; Arkhipov, A.; Schulten, K. Assembly of lipoprotein particles revealed by coarse-grained molecular dynamics simulations J. Struct. Biol. 2007, 157, 579-592
    • (2007) J. Struct. Biol. , vol.157 , pp. 579-592
    • Shih, A.Y.1    Freddolino, P.L.2    Arkhipov, A.3    Schulten, K.4
  • 43
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S. E.; Zhang, Y.; Pastor, R. W.; Brooks, B. R. Constant pressure molecular dynamics simulation: The Langevin piston method J. Chem. Phys. 1995, 103, 4613-4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 44
    • 36049014994 scopus 로고    scopus 로고
    • Size and shape of detergent micelles determined by small-angle X-ray scattering
    • DOI 10.1021/jp0730161
    • Lipfert, J.; Columbus, L.; Chu, V. B.; Lesley, S. A.; Doniach, S. Size and shape of detergent micelles determined by small-angle X-ray scattering J. Phys. Chem. B 2007, 111, 12427-12438 (Pubitemid 350097588)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.43 , pp. 12427-12438
    • Lipfert, J.1    Columbus, L.2    Chu, V.B.3    Lesley, S.A.4    Doniach, S.5
  • 45
    • 36849085363 scopus 로고    scopus 로고
    • The molecular mechanism of monolayer-bilayer transformations of lung surfactant from molecular dynamics simulations
    • DOI 10.1529/biophysj.107.113399
    • Baoukina, S.; Monticelli, L.; Amrein, M.; Tieleman, D. P. The Molecular Mechanism of Monolayer-Bilayer Transformations of Lung Surfactant from Molecular Dynamics Simulations Biophys. J. 2007, 93, 3775-3782 (Pubitemid 350223796)
    • (2007) Biophysical Journal , vol.93 , Issue.11 , pp. 3775-3782
    • Baoukina, S.1    Monticelli, L.2    Amrein, M.3    Tieleman, D.P.4
  • 46
    • 0035812426 scopus 로고    scopus 로고
    • Simulation of the spontaneous aggregation of phospholipids into bilayers [23]
    • DOI 10.1021/ja0159618
    • Marrink, S. J.; Lindahl, E.; Edholm, O.; Mark, A. E. Simulation of the Spontaneous Aggregation of Phospholipids into Bilayers J. Am. Chem. Soc. 2001, 123, 8638-8639 (Pubitemid 32808102)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.35 , pp. 8638-8639
    • Marrink, S.J.1    Lindahl, E.2    Edholm, O.3    Mark, A.E.4
  • 47
    • 77949700666 scopus 로고    scopus 로고
    • Micellization behavior of coarse grained surfactant models
    • Sanders, S. A.; Panagiotopoulos, A. Z. Micellization behavior of coarse grained surfactant models J. Chem. Phys. 2010, 132, 114902-1-114902-9
    • (2010) J. Chem. Phys. , vol.132 , pp. 1149021-1149029
    • Sanders, S.A.1    Panagiotopoulos, A.Z.2
  • 48
    • 79957998114 scopus 로고    scopus 로고
    • Coarse-Grained Molecular Dynamics Simulations of the Sphere to Rod Transition in Surfactant Micelles
    • Sangwai, A. V.; Sureshkumar, R. Coarse-Grained Molecular Dynamics Simulations of the Sphere to Rod Transition in Surfactant Micelles Langmuir 2011, 27, 6628-6638
    • (2011) Langmuir , vol.27 , pp. 6628-6638
    • Sangwai, A.V.1    Sureshkumar, R.2
  • 49
    • 0020905807 scopus 로고
    • Determination of micelle structure and charge by neutron small-angle scattering
    • Hayter, J. B.; Penfold, J. Determination of micelle structure and charge by neutron small-angle scattering Colloid Polym. Sci. 1983, 261, 1022-1030 (Pubitemid 14535080)
    • (1983) Colloid and Polymer Science , vol.261 , Issue.12 , pp. 1022-1030
    • Hayter, J.B.1    Penfold, J.2
  • 50
    • 34250108489 scopus 로고
    • Characteristics of rodlike micelles of cetyltrimethylammonium chloride in aqueous NaCl solutions: Their flexibility and the scaling laws in dilute and semidilute regimes
    • Imae, T.; Ikeda, S. Characteristics of rodlike micelles of cetyltrimethylammonium chloride in aqueous NaCl solutions: Their flexibility and the scaling laws in dilute and semidilute regimes Colloid Polym. Sci. 1987, 265, 1090-1098
    • (1987) Colloid Polym. Sci. , vol.265 , pp. 1090-1098
    • Imae, T.1    Ikeda, S.2
  • 51
    • 0025746488 scopus 로고
    • Stability of spherical and rod-like micelles of ionic surfactants, in relation to their counterion binding and modes of hydration
    • Ikeda, S. Stability of spherical and rod-like micelles of ionic surfactants, in relation to their counterion binding and modes of hydration Colloid Polym. Sci. 1991, 269, 49-61
    • (1991) Colloid Polym. Sci. , vol.269 , pp. 49-61
    • Ikeda, S.1
  • 52
    • 0031549595 scopus 로고    scopus 로고
    • Effect of counterion competition on micellar growth horizons for cetyltrimethylammonium micellar surfaces: Electrostatics and specific binding
    • Magid, L. J.; Han, Z.; Warr, G. G.; Cassidy, M. A.; Butler, P. D.; Hamilton, W. A. Effect of Counterion Competition on Micellar Growth Horizons for Cetyltrimethylammonium Micellar Surfaces: Electrostatics and Specific Binding J. Phys. Chem. B 1997, 101, 7919-7927 (Pubitemid 127576552)
    • (1997) Journal of Physical Chemistry B , vol.101 , Issue.40 , pp. 7919-7927
    • Magid, L.J.1    Han, Z.2    Warr, G.G.3    Cassidy, M.A.4    Butler, P.D.5    Hamilton, W.A.6
  • 53
    • 0015991171 scopus 로고
    • Physical chemical studies of short-chain lecithin homologues. I. Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle concentration
    • Tausk, R. J. M.; Karmiggelt, J.; Oudshoorn, C.; Overbeek, J. T. G. Physical chemical studies of short-chain lecithin homologues. I. Influence of the chain length of the fatty acid ester and of electrolytes on the critical micelle concentration Biophys. Chem. 1974, 1, 175-183
    • (1974) Biophys. Chem. , vol.1 , pp. 175-183
    • Tausk, R.J.M.1    Karmiggelt, J.2    Oudshoorn, C.3    Overbeek, J.T.G.4
  • 54
    • 0016198708 scopus 로고
    • Physical chemical studies of short-chain lecithin homologues IV. A simple model for the influence of salt and the alkyl chain length on the micellar size
    • Tausk, R. J. M.; Overbeek, J. T. G. Physical chemical studies of short-chain lecithin homologues IV. A simple model for the influence of salt and the alkyl chain length on the micellar size Biophys. Chem. 1974, 2, 175-179
    • (1974) Biophys. Chem. , vol.2 , pp. 175-179
    • Tausk, R.J.M.1    Overbeek, J.T.G.2
  • 55
    • 4344582879 scopus 로고    scopus 로고
    • Direct observation and characterization of DMPC/DHPC aggregates under conditions relevant for biological solution NMR
    • DOI 10.1016/j.bbamem.2004.06.005, PII S0005273604001506
    • van Dam, L.; Karlsson, G.; Edwards, K. Direct observation and characterization of DMPC/DHPC aggregates under conditions relevant for biological solution NMR Biochim. Biophys. Acta, Biomembr. 2004, 1664, 241-256 (Pubitemid 39140998)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1664 , Issue.2 , pp. 241-256
    • Van Dam, L.1    Karlsson, G.2    Edwards, K.3
  • 56
    • 0000530868 scopus 로고
    • Temperature dependence of the micelle aggregation number and rate of intramicellar excimer formation in aqueous surfactant solutions
    • Malliaris, A.; Le Moigne, J.; Sturm, J.; Zana, R. Temperature dependence of the micelle aggregation number and rate of intramicellar excimer formation in aqueous surfactant solutions J. Phys. Chem. 1985, 89, 2709-2713
    • (1985) J. Phys. Chem. , vol.89 , pp. 2709-2713
    • Malliaris, A.1    Le Moigne, J.2    Sturm, J.3    Zana, R.4
  • 57
  • 58
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins - Energyminimizations for crystals of cyclic-peptides and crambin
    • Jorgensen, W. L.; Tirado-Rives, J. The OPLS potential functions for proteins-energyminimizations for crystals of cyclic-peptides and crambin J. Am. Chem. Soc. 1988, 110, 1666-1671
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1666-1671
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 59
    • 82455184397 scopus 로고    scopus 로고
    • Sphere-to-Rod Transitions of Nonionic Surfactant Micelles in Aqueous Solution Modeled by Molecular Dynamics Simulations
    • Velinova, M.; Sengupta, D.; Tadjer, A. V.; Marrink, S. Sphere-to-Rod Transitions of Nonionic Surfactant Micelles in Aqueous Solution Modeled by Molecular Dynamics Simulations Langmuir 2011, 27, 14071-14077
    • (2011) Langmuir , vol.27 , pp. 14071-14077
    • Velinova, M.1    Sengupta, D.2    Tadjer, A.V.3    Marrink, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.