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Volumn 8, Issue 11, 2012, Pages 4610-4623

Molecular dynamics simulations of a characteristic DPC micelle in water

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EID: 84869064697     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct3003207     Document Type: Article
Times cited : (64)

References (123)
  • 1
    • 55249113656 scopus 로고    scopus 로고
    • The use of detergents to purify membrane proteins
    • Chapter 4, Units
    • Arnold, T.; Linke, D. The use of detergents to purify membrane proteins. Current Protocols in Protein Science; 2008; Chapter 4, Units 53:4.8.1-4.8.30.
    • (2008) Current Protocols in Protein Science , pp. 53481-54830
    • Arnold, T.1    Linke, D.2
  • 2
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • Privé, G. Detergents for the stabilization and crystallization of membrane proteins Methods 2007, 41, 388-397
    • (2007) Methods , vol.41 , pp. 388-397
    • Privé, G.1
  • 5
  • 6
    • 0031920741 scopus 로고    scopus 로고
    • Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion
    • Gao, X. F.; Wong, T. C. Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion Biophys. J. 1998, 74, 1871-1888
    • (1998) Biophys. J. , vol.74 , pp. 1871-1888
    • Gao, X.F.1    Wong, T.C.2
  • 7
    • 82755198034 scopus 로고    scopus 로고
    • Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics
    • de Foresta, B.; Vincent, M.; Garrigos, M.; Gallay, J. Transverse and tangential orientation of predicted transmembrane fragments 4 and 10 from the human multidrug resistance protein (hMRP1/ABCC1) in membrane mimics Eur. Biophys. J. 2011, 40, 1043-1060
    • (2011) Eur. Biophys. J. , vol.40 , pp. 1043-1060
    • De Foresta, B.1    Vincent, M.2    Garrigos, M.3    Gallay, J.4
  • 8
    • 0037111207 scopus 로고    scopus 로고
    • Micelle-bound conformation of a hairpin-forming peptide: Combined NMR and molecular dynamics study
    • Dixon, A. M.; Venable, R. M.; Pastor, R. W.; Bull, T. E. Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study Biopolymers 2002, 65, 284-298
    • (2002) Biopolymers , vol.65 , pp. 284-298
    • Dixon, A.M.1    Venable, R.M.2    Pastor, R.W.3    Bull, T.E.4
  • 9
    • 70349745154 scopus 로고    scopus 로고
    • Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins
    • Kim, H. J.; Howell, S. C.; Van Horn, W. D.; Jeon, Y. H.; Sanders, C. R. Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins Prog. Nucl. Magn. Reson. Spectrosc. 2009, 55, 335-360
    • (2009) Prog. Nucl. Magn. Reson. Spectrosc. , vol.55 , pp. 335-360
    • Kim, H.J.1    Howell, S.C.2    Van Horn, W.D.3    Jeon, Y.H.4    Sanders, C.R.5
  • 10
    • 77950576779 scopus 로고    scopus 로고
    • Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape
    • Göbl, C.; Dulle, M.; Hohlweg, W.; Grossauer, J.; Falsone, S. F.; Glatter, O.; Zangger, K. Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape J. Phys. Chem. B 2010, 114, 4717-4724
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4717-4724
    • Göbl, C.1    Dulle, M.2    Hohlweg, W.3    Grossauer, J.4    Falsone, S.F.5    Glatter, O.6    Zangger, K.7
  • 11
    • 33751017943 scopus 로고    scopus 로고
    • Solution structure of amphibian tachykinin perolein bound to DPC micelles
    • Dike, A.; Cowsik, S. M. Solution structure of amphibian tachykinin perolein bound to DPC micelles J. Struct. Biol. 2006, 156, 442-452
    • (2006) J. Struct. Biol. , vol.156 , pp. 442-452
    • Dike, A.1    Cowsik, S.M.2
  • 12
    • 71649092717 scopus 로고    scopus 로고
    • α-Helical transmembrane peptides: A "divide and Conquer" approach to membrane proteins
    • Bordag, N.; Keller, S. α-Helical transmembrane peptides: A "Divide and Conquer" approach to membrane proteins Chem. Phys. Lipids 2010, 163, 1-26
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 1-26
    • Bordag, N.1    Keller, S.2
  • 13
    • 36849088540 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better
    • Poget, S. F.; Girvin, M. E. Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better Biochim. Biophys. Acta 2007, 1768, 3098-3106
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3098-3106
    • Poget, S.F.1    Girvin, M.E.2
  • 14
    • 0018798032 scopus 로고
    • Physicochemical studies of the protein-lipid interactions in melittin-containing micelles
    • Lauterwein, J.; Bösch, C.; Brown, L. R.; Wüthrich, K. Physicochemical studies of the protein-lipid interactions in melittin-containing micelles Biochim. Biophys. Acta: Biomembr. 1979, 556, 244-264
    • (1979) Biochim. Biophys. Acta: Biomembr. , vol.556 , pp. 244-264
    • Lauterwein, J.1    Bösch, C.2    Brown, L.R.3    Wüthrich, K.4
  • 15
    • 36049014994 scopus 로고    scopus 로고
    • Size and shape of detergent micelles determined by small-angle X-ray scattering
    • 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
    • (2007) J. Phys. Chem. B , vol.111 , pp. 12427-12438
    • Lipfert, J.1    Columbus, L.2    Chu, V.B.3    Lesley, S.A.4    Doniach, S.5
  • 16
    • 0033543147 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure and dynamics of a dodecylphosphocholine micelle in aqueous solution
    • Wymore, T.; Gao, X. F.; Wong, T. C. Molecular dynamics simulation of the structure and dynamics of a dodecylphosphocholine micelle in aqueous solution THEOCHEM 1999, 485-486, 195-210
    • (1999) THEOCHEM , vol.485-486 , pp. 195-210
    • Wymore, T.1    Gao, X.F.2    Wong, T.C.3
  • 17
    • 0034499269 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of the Kinetics of Spontaneous Micelle Formation
    • Marrink, S.-J.; Tieleman, P. D.; 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, P.D.2    Mark, A.E.3
  • 18
    • 0034229640 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Dodecylphosphocholine Micelles at Three Different Aggregate Sizes: Micellar Structure and Chain Relaxation
    • Tieleman, D. P.; van der Spoel, D.; Berendsen, H. J. C. Molecular Dynamics Simulations of Dodecylphosphocholine Micelles at Three Different Aggregate Sizes: Micellar Structure and Chain Relaxation J. Phys. Chem. B 2000, 104, 6380-6388
    • (2000) J. Phys. Chem. B , vol.104 , pp. 6380-6388
    • Tieleman, D.P.1    Van Der Spoel, D.2    Berendsen, H.J.C.3
  • 19
    • 0035954988 scopus 로고    scopus 로고
    • Dynamics of Ganglioside Headgroup in Lipid Environment: Molecular Dynamics Simulations of GM1 Embedded in Dodecylphosphocholine Micelle
    • Vasudevan, S. V.; Balaji, P. V. Dynamics of Ganglioside Headgroup in Lipid Environment: Molecular Dynamics Simulations of GM1 Embedded in Dodecylphosphocholine Micelle J. Phys. Chem. B 2001, 105, 7033-7041
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7033-7041
    • Vasudevan, S.V.1    Balaji, P.V.2
  • 20
    • 33847010221 scopus 로고    scopus 로고
    • Quantifying the Hydrophobic Effect. 2. A Computer Simulation-Molecular- Thermodynamic Model for the Micellization of Nonionic Surfactants in Aqueous Solution
    • Stephenson, B. C.; Goldsipe, A.; Beers, K. J.; Blankschtein, D. Quantifying the Hydrophobic Effect. 2. A Computer Simulation-Molecular- Thermodynamic Model for the Micellization of Nonionic Surfactants in Aqueous Solution J. Phys. Chem. B 2007, 111, 1045-1062
    • (2007) J. Phys. Chem. B , vol.111 , pp. 1045-1062
    • Stephenson, B.C.1    Goldsipe, A.2    Beers, K.J.3    Blankschtein, D.4
  • 21
    • 1642485164 scopus 로고    scopus 로고
    • Coarse Grained Model for Semi quantitative Lipid Simulations
    • Marrink, S.-J.; de Vries, A. H.; Mark, A. E. Coarse Grained Model for Semi quantitative 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
  • 22
    • 56749177067 scopus 로고    scopus 로고
    • Study of the antimicrobial peptide indolicidin and a mutant in micelle medium by molecular dynamics simulation
    • Fuzo, C. A.; Castro, J. R. M.; Degreve, L. Study of the antimicrobial peptide indolicidin and a mutant in micelle medium by molecular dynamics simulation Genet. Mol. Res. 2008, 7, 986-999
    • (2008) Genet. Mol. Res. , vol.7 , pp. 986-999
    • Fuzo, C.A.1    Castro, J.R.M.2    Degreve, L.3
  • 23
    • 23844477976 scopus 로고    scopus 로고
    • Implicit Solvent Simulations of DPC Micelle Formation
    • Lazaridis, T.; Mallik, B.; Y., C.; Chen, Y. Implicit Solvent Simulations of DPC Micelle Formation J. Phys. Chem. B 2005, 109, 15098-15106
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15098-15106
    • Lazaridis, T.1    Mallik, B.2    Chen, Y.3
  • 24
    • 36649010822 scopus 로고    scopus 로고
    • Multi-Mannosides Based on a Carbohydrate Scaffold; Synthesis, Force Field Development, Molecular Dynamics Studies, and Binding Affinities for Lectin Con A
    • Gouin, S.; Vanquelef, E.; Garcia Fernandez, J. M.; Ortiz Mellet, C.; Dupradeau, F.-Y.; Kovensky, J. Multi-Mannosides Based on a Carbohydrate Scaffold; Synthesis, Force Field Development, Molecular Dynamics Studies, and Binding Affinities for Lectin Con A J. Org. Chem. 2007, 72, 9032-9045
    • (2007) J. Org. Chem. , vol.72 , pp. 9032-9045
    • Gouin, S.1    Vanquelef, E.2    Garcia Fernandez, J.M.3    Ortiz Mellet, C.4    Dupradeau, F.-Y.5    Kovensky, J.6
  • 27
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak, V.; Abel, R.; Okur, A.; Strockbine, B.; Roitberg, A.; Simmerling, C. Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins Struct. Funct. 2006, 65, 712-725
    • (2006) Proteins Struct. Funct. , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 28
    • 84858321169 scopus 로고    scopus 로고
    • Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids
    • Jämbeck, J. P. M.; Lyubartsev, A. P. Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids J. Phys. Chem. B 2012, 116, 3164-3179
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3164-3179
    • Jämbeck, J.P.M.1    Lyubartsev, A.P.2
  • 29
    • 84865101970 scopus 로고    scopus 로고
    • An Extension and Further Validation of an All-Atomistic Force Field for Biological Membranes
    • Jämbeck, J. P. M.; Lyubartsev, A. P. An Extension and Further Validation of an All-Atomistic Force Field for Biological Membranes J. Chem. Theory Comput. 2012, 8, 2938-2948
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 2938-2948
    • Jämbeck, J.P.M.1    Lyubartsev, A.P.2
  • 30
    • 84865722478 scopus 로고    scopus 로고
    • GAFFlipid: A General Amber Force Field for the accurate molecular dynamics simulation of phospholipid
    • Dickson, C. J.; Rosso, L.; Betz, R. M.; Walker, R. C.; Gould, I. R. GAFFlipid: a General Amber Force Field for the accurate molecular dynamics simulation of phospholipid Soft Matter 2012, 8, 9617-9627
    • (2012) Soft Matter , vol.8 , pp. 9617-9627
    • Dickson, C.J.1    Rosso, L.2    Betz, R.M.3    Walker, R.C.4    Gould, I.R.5
  • 31
    • 41549149586 scopus 로고    scopus 로고
    • Biomolecular simulations of membranes: Physical properties from different force fields
    • Siu, S. W. I.; Vácha, R.; Jungwirth, P.; Böckmann, R. A. Biomolecular simulations of membranes: physical properties from different force fields J. Chem. Phys. 2008, 128, 125103
    • (2008) J. Chem. Phys. , vol.128 , pp. 125103
    • Siu, S.W.I.1    Vácha, R.2    Jungwirth, P.3    Böckmann, R.A.4
  • 32
    • 34547372334 scopus 로고    scopus 로고
    • Performance of the general amber force field in modeling aqueous POPC membrane bilayers
    • Jójárt, B.; Martinek, T. A. Performance of the general amber force field in modeling aqueous POPC membrane bilayers J. Comput. Chem. 2007, 28, 2051-2058
    • (2007) J. Comput. Chem. , vol.28 , pp. 2051-2058
    • Jójárt, B.1    Martinek, T.A.2
  • 34
    • 78751664249 scopus 로고    scopus 로고
    • Molecular simulations of dodecyl-β-maltoside micelles in water: Influence of the headgroup conformation and force field parameters
    • Abel, S.; Dupradeau, F.-Y.; Raman, E. P.; MacKerell, A. D.; Marchi, M. Molecular simulations of dodecyl-β-maltoside micelles in water: influence of the headgroup conformation and force field parameters J. Phys. Chem. B 2011, 115, 487-499
    • (2011) J. Phys. Chem. B , vol.115 , pp. 487-499
    • Abel, S.1    Dupradeau, F.-Y.2    Raman, E.P.3    MacKerell, A.D.4    Marchi, M.5
  • 37
    • 0033654654 scopus 로고    scopus 로고
    • Molecular dynamics simulations of nucleic acids
    • Cheatham, T. E., III; Kollman, P. A. Molecular dynamics simulations of nucleic acids Annu. Rev. Phys. Chem. 2000, 51, 435-471
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 435-471
    • Cheatham Iii, T.E.1    Kollman, P.A.2
  • 39
    • 84934440741 scopus 로고    scopus 로고
    • Comparison of protein force fields for molecular dynamics simulations
    • Guvench, O.; MacKerell, A. D. Comparison of protein force fields for molecular dynamics simulations Methods Mol. Biol. 2008, 443, 63-88
    • (2008) Methods Mol. Biol. , vol.443 , pp. 63-88
    • Guvench, O.1    MacKerell, A.D.2
  • 40
    • 80051743238 scopus 로고    scopus 로고
    • Molecular dynamics studies of native and substituted cyclodextrins in different media: 1. Charge derivation and force field performances
    • Cézard, C.; Trivelli, X.; Aubry, F.; Djedaïni-Pilard, F.; Dupradeau, F.-Y. Molecular dynamics studies of native and substituted cyclodextrins in different media: 1. Charge derivation and force field performances Phys. Chem. Chem. Phys. 2011, 13, 15103-15121
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 15103-15121
    • Cézard, C.1    Trivelli, X.2    Aubry, F.3    Djedaïni-Pilard, F.4    Dupradeau, F.-Y.5
  • 41
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly, C. I.; Cieplak, P.; Cornell, W. D.; Kollman, P. A. A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model J. Phys. Chem. 1993, 97, 10269-10280
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 42
    • 84986516411 scopus 로고
    • Application of the multimolecule and multiconformational RESP methodology to biopolymers: Charge derivation for DNA, RNA, and proteins
    • Cieplak, P.; Cornell, W. D.; Bayly, C.; Kollman, P. A. Application of the multimolecule and multiconformational RESP methodology to biopolymers: Charge derivation for DNA, RNA, and proteins J. Comput. Chem. 1995, 16, 1357-1377
    • (1995) J. Comput. Chem. , vol.16 , pp. 1357-1377
    • Cieplak, P.1    Cornell, W.D.2    Bayly, C.3    Kollman, P.A.4
  • 46
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M. L. Analytical molecular surface calculation J. Appl. Crystallogr. 1983, 16, 548-558
    • (1983) J. Appl. Crystallogr. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 49
    • 77950590441 scopus 로고    scopus 로고
    • A new force field for simulating phosphatidylcholine bilayers
    • Poger, D.; Van Gunsteren, W. F.; Mark, A. E. A new force field for simulating phosphatidylcholine bilayers J. Comput. Chem. 2010, 31, 1117-1125
    • (2010) J. Comput. Chem. , vol.31 , pp. 1117-1125
    • Poger, D.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 51
    • 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
    • (1997) Biophys. J. , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jähnig, F.3
  • 52
    • 33645941402 scopus 로고
    • The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen, W. L.; Tirado-Rives, J. The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin J. Am. Chem. Soc. 1988, 110, 1657-1666
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 53
    • 34547324134 scopus 로고    scopus 로고
    • Molecular dynamics simulations of rhodopsin in different one-component lipid bilayers
    • Cordomí, A.; Perez, J. J. Molecular dynamics simulations of rhodopsin in different one-component lipid bilayers J. Phys. Chem. B 2007, 111, 7052-7063
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7052-7063
    • Cordomí, A.1    Perez, J.J.2
  • 54
    • 33645310406 scopus 로고    scopus 로고
    • Assessing the influence of electrostatic schemes on molecular dynamics simulations of secondary structure forming peptides
    • Monticelli, L.; Simões, C.; Belvisi, L.; Colombo, G. Assessing the influence of electrostatic schemes on molecular dynamics simulations of secondary structure forming peptides J. Phys.: Condens. Matter 2006, 18, S329-S345
    • (2006) J. Phys.: Condens. Matter , vol.18
    • Monticelli, L.1    Simões, C.2    Belvisi, L.3    Colombo, G.4
  • 55
    • 77749320417 scopus 로고    scopus 로고
    • An iris-like mechanism of pore dilation in the CorA magnesium transport system
    • Chakrabarti, N.; Neale, C.; Payandeh, J.; Pai, E. F.; Pomès, R. An iris-like mechanism of pore dilation in the CorA magnesium transport system Biophys. J. 2010, 98, 784-792
    • (2010) Biophys. J. , vol.98 , pp. 784-792
    • Chakrabarti, N.1    Neale, C.2    Payandeh, J.3    Pai, E.F.4    Pomès, R.5
  • 56
    • 79954752757 scopus 로고    scopus 로고
    • Exploring the conformational dynamics and membrane interactions of PorB from C. glutamicum: A multi-scale molecular dynamics simulation study
    • Piñeiro, á.; Bond, P. J.; Khalid, S. Exploring the conformational dynamics and membrane interactions of PorB from C. glutamicum: a multi-scale molecular dynamics simulation study Biochim. Biophys. Acta 2011, 1808, 1746-1752
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1746-1752
    • Piñeiro, A.1    Bond, P.J.2    Khalid, S.3
  • 57
    • 79953898210 scopus 로고    scopus 로고
    • 3pi-helix conformation facilitates the transition of a voltage sensor S4 segment toward the down state
    • Schwaiger, C. S.; Bjelkmar, P.; Hess, B.; Lindahl, E. 3pi-helix conformation facilitates the transition of a voltage sensor S4 segment toward the down state Biophys. J. 2011, 100, 1446-1454
    • (2011) Biophys. J. , vol.100 , pp. 1446-1454
    • Schwaiger, C.S.1    Bjelkmar, P.2    Hess, B.3    Lindahl, E.4
  • 58
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the CHARMM Force Field in GROMACS: Analysis of Protein Stability Effects from Correction Maps, Virtual Interaction Sites, and Water Models
    • Bjelkmar, P.; Larsson, P.; Cuendet, M. A.; Hess, B.; Lindahl, E. Implementation of the CHARMM Force Field in GROMACS: Analysis of Protein Stability Effects from Correction Maps, Virtual Interaction Sites, and Water Models J. Chem. Theory Comput. 2010, 6, 459-466
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 459-466
    • Bjelkmar, P.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 59
    • 85047692291 scopus 로고    scopus 로고
    • Empirical force-field assessment: The interplay between backbone torsions and noncovalent term scaling
    • Sorin, E. J.; Pande, V. S. Empirical force-field assessment: The interplay between backbone torsions and noncovalent term scaling J. Comput. Chem. 2005, 26, 682-690
    • (2005) J. Comput. Chem. , vol.26 , pp. 682-690
    • Sorin, E.J.1    Pande, V.S.2
  • 60
    • 0029099308 scopus 로고
    • Incorporation of surface tension into molecular dynamics simulation of an interface: A fluid phase lipid bilayer membrane
    • Chiu, S. W.; Clark, M.; Balaji, V.; Subramaniam, S.; Scott, H. L.; Jakobsson, E. Incorporation of surface tension into molecular dynamics simulation of an interface: a fluid phase lipid bilayer membrane Biophys. J. 1995, 69, 1230-1245
    • (1995) Biophys. J. , vol.69 , pp. 1230-1245
    • Chiu, S.W.1    Clark, M.2    Balaji, V.3    Subramaniam, S.4    Scott, H.L.5    Jakobsson, E.6
  • 62
    • 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
  • 63
    • 0015222018 scopus 로고
    • Studies on phospholipase A and its zymogen from porcine pancreas. 3. Action of the enzyme on short-chain lecithins
    • de Haas, G. H.; Bonsen, P. P.; Pieterson, W. A.; van Deenen, L. L. Studies on phospholipase A and its zymogen from porcine pancreas. 3. 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.2    Pieterson, W.A.3    Van Deenen, L.L.4
  • 64
    • 33644644163 scopus 로고    scopus 로고
    • Insertion and Assembly of Membrane Proteins via Simulation
    • Bond, P. J.; Sansom, M. S. P. Insertion and Assembly of Membrane Proteins via Simulation J. Am. Chem. Soc. 2006, 128, 2697-2704
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2697-2704
    • Bond, P.J.1    Sansom, M.S.P.2
  • 65
    • 10344247720 scopus 로고    scopus 로고
    • MD Simulations of Spontaneous Membrane Protein/Detergent Micelle Formation
    • Bond, P. J.; Cuthbertson, J. M.; Deol, S. S.; Sansom, M. S. P. MD Simulations of Spontaneous Membrane Protein/Detergent Micelle Formation J. Am. Chem. Soc. 2004, 126, 15948-15949
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15948-15949
    • Bond, P.J.1    Cuthbertson, J.M.2    Deol, S.S.3    Sansom, M.S.P.4
  • 66
    • 22344445910 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of the Helical Antimicrobial Peptide Ovispirin-1 in a Zwitterionic Dodecylphosphocholine Micelle: Insights into Host-Cell Toxicity
    • Khandelia, H.; Kaznessis, Y. N. Molecular Dynamics Simulations of the Helical Antimicrobial Peptide Ovispirin-1 in a Zwitterionic Dodecylphosphocholine Micelle: Insights into Host-Cell Toxicity J. Phys. Chem. B 2005, 109, 12990-12996
    • (2005) J. Phys. Chem. B , vol.109 , pp. 12990-12996
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 67
    • 40549132558 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation and Thermodynamic Modeling of the Self-Assembly of the Triterpenoids Asiatic Acid and Madecassic Acid in Aqueous Solution
    • Stephenson, B. C.; Goldsipe, A.; Blankschtein, D. Molecular Dynamics Simulation and Thermodynamic Modeling of the Self-Assembly of the Triterpenoids Asiatic Acid and Madecassic Acid in Aqueous Solution J. Phys. Chem. B 2008, 112, 2357-2371
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2357-2371
    • Stephenson, B.C.1    Goldsipe, A.2    Blankschtein, D.3
  • 68
    • 79956028024 scopus 로고    scopus 로고
    • The effect of membrane curvature on the conformation of antimicrobial peptides: Implications for binding and the mechanism of action
    • Chen, R.; Mark, A. E. The effect of membrane curvature on the conformation of antimicrobial peptides: implications for binding and the mechanism of action Eur. Biophys. J. 2011, 40, 545-553
    • (2011) Eur. Biophys. J. , vol.40 , pp. 545-553
    • Chen, R.1    Mark, A.E.2
  • 71
    • 84986440341 scopus 로고
    • Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto, S.; Kollman, P. A. Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 1992, 13, 952-962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 72
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G.; Donadio, D.; Parrinello, M. Canonical sampling through velocity rescaling J. Chem. Phys. 2007, 126, 14101-14107
    • (2007) J. Chem. Phys. , vol.126 , pp. 14101-14107
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 73
    • 33845790250 scopus 로고
    • Molecular Dynamics Study of Liquid Water
    • Rahman, A.; Stillinger, F. H. Molecular Dynamics Study of Liquid Water J. Chem. Phys. 1971, 55, 3336-3359
    • (1971) J. Chem. Phys. , vol.55 , pp. 3336-3359
    • Rahman, A.1    Stillinger, F.H.2
  • 74
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M.; Rahman, A. Polymorphic transitions in single crystals: A new molecular dynamics method J. Appl. Phys. 1981, 52, 7182-7190
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 75
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nosé, S. A molecular dynamics method for simulations in the canonical ensemble Mol. Phys. 1984, 52, 255-268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nosé, S.1
  • 76
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. Canonical dynamics: Equilibrium phase-space distributions Phys. Rev. A 1985, 31, 1695-1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 78
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular dynamics simulations
    • Tironi, I. G.; Sperb, R.; Smith, P. E.; van Gunsteren, W. F. A generalized reaction field method for molecular dynamics simulations J. Chem. Phys. 1995, 102, 5451-5459
    • (1995) J. Chem. Phys. , vol.102 , pp. 5451-5459
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    Van Gunsteren, W.F.4
  • 79
    • 77955135754 scopus 로고    scopus 로고
    • Scrutinizing Molecular Mechanics Force Fields on the Submicrosecond Timescale with NMR Data
    • Lange, O. F.; van der Spoel, D.; de Groot, B. L. Scrutinizing Molecular Mechanics Force Fields on the Submicrosecond Timescale with NMR Data Biochem. J. 2010, 99, 647-655
    • (2010) Biochem. J. , vol.99 , pp. 647-655
    • Lange, O.F.1    Van Der Spoel, D.2    De Groot, B.L.3
  • 80
    • 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. 2007, 4, 116-122
    • (2007) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 81
    • 84857761247 scopus 로고    scopus 로고
    • Atomistic simulations of micellization of sodium hexyl, heptyl, octyl, and nonyl sulfates
    • Sanders, S. A.; Sammalkorpi, M.; Panagiotopoulos, A. Z. Atomistic simulations of micellization of sodium hexyl, heptyl, octyl, and nonyl sulfates J. Phys. Chem. B 2012, 116, 2430-2437
    • (2012) J. Phys. Chem. B , vol.116 , pp. 2430-2437
    • Sanders, S.A.1    Sammalkorpi, M.2    Panagiotopoulos, A.Z.3
  • 82
    • 0033485638 scopus 로고    scopus 로고
    • Large scale molecular dynamics simulation of self-assembly processes in short and long chain cationic surfactants
    • Maillet, J.-B.; Lachet, V.; Coveney, P. V. Large scale molecular dynamics simulation of self-assembly processes in short and long chain cationic surfactants Phys. Chem. Chem. Phys. 1999, 1, 5277-5290
    • (1999) Phys. Chem. Chem. Phys. , vol.1 , pp. 5277-5290
    • Maillet, J.-B.1    Lachet, V.2    Coveney, P.V.3
  • 83
    • 72149123675 scopus 로고    scopus 로고
    • Atomistic simulations of spontaneous formation and structural properties of linoleic acid micelles in water
    • Abel, S.; Attia, J.; Rémita, S.; Marchi, M.; Urbach, W.; Goldmann, M. Atomistic simulations of spontaneous formation and structural properties of linoleic acid micelles in water Chem. Phys. Lett. 2009, 481, 124-129
    • (2009) Chem. Phys. Lett. , vol.481 , pp. 124-129
    • Abel, S.1    Attia, J.2    Rémita, S.3    Marchi, M.4    Urbach, W.5    Goldmann, M.6
  • 84
    • 77950552018 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Glycocholate-Oleic Acid Mixed Micelle Assembly
    • Turner, D. C.; Yin, F.; Kindt, J. T.; Zhang, H. Molecular Dynamics Simulations of Glycocholate-Oleic Acid Mixed Micelle Assembly Langmuir 2010, 26, 4687-4692
    • (2010) Langmuir , vol.26 , pp. 4687-4692
    • Turner, D.C.1    Yin, F.2    Kindt, J.T.3    Zhang, H.4
  • 85
    • 56349083191 scopus 로고    scopus 로고
    • Implicit Solvent Models for Micellization of Ionic Surfactants
    • Jusufi, A.; Hynninen, A.-P.; Panagiotopoulos, A. Z. Implicit Solvent Models for Micellization of Ionic Surfactants J. Phys. Chem. B 2008, 112, 13783-13792
    • (2008) J. Phys. Chem. B , vol.112 , pp. 13783-13792
    • Jusufi, A.1    Hynninen, A.-P.2    Panagiotopoulos, A.Z.3
  • 86
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen, W. L.; Maxwell, D. S.; Tirado-Rives, J. Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids J. Am. Chem. Soc. 1996, 118, 11225-11236
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 87
    • 45749157286 scopus 로고    scopus 로고
    • Molecular dynamics simulation of self-assembly of n- decyltrimethylammonium bromide micelles
    • Jorge, M. Molecular dynamics simulation of self-assembly of n-decyltrimethylammonium bromide micelles Langmuir 2008, 24, 5714-25
    • (2008) Langmuir , vol.24 , pp. 5714-5725
    • Jorge, M.1
  • 89
    • 79960807978 scopus 로고    scopus 로고
    • Kinetics of thermo-induced micelle-to-vesicle transitions in a catanionic surfactant system investigated by stopped-flow temperature jump
    • Zhang, J.; Liu, S. Kinetics of thermo-induced micelle-to-vesicle transitions in a catanionic surfactant system investigated by stopped-flow temperature jump Phys. Chem. Chem. Phys. 2011, 13, 12545-12553
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 12545-12553
    • Zhang, J.1    Liu, S.2
  • 91
    • 74349095210 scopus 로고    scopus 로고
    • VORO++: A three-dimensional voronoi cell library in C++
    • Rycroft, C. H. VORO++: a three-dimensional voronoi cell library in C++ Chaos 2009, 19, 041111
    • (2009) Chaos , vol.19 , pp. 041111
    • Rycroft, C.H.1
  • 92
    • 84927514013 scopus 로고
    • Nouvelles applications des paramètres continus à la théorie des formes quadratiques
    • Voronoi, G. F. Nouvelles applications des paramètres continus à la théorie des formes quadratiques J. Reine Angew. Math. 1908, 134, 198-287
    • (1908) J. Reine Angew. Math. , vol.134 , pp. 198-287
    • Voronoi, G.F.1
  • 93
    • 80052614322 scopus 로고    scopus 로고
    • Volumetric properties of hydrated peptides: Voronoi-Delaunay analysis of molecular simulation runs
    • Voloshin, V. P.; Medvedev, N. N.; Andrews, M. N.; Burri, R. R.; Winter, R.; Geiger, A. Volumetric properties of hydrated peptides: Voronoi-Delaunay analysis of molecular simulation runs J. Phys. Chem. B 2011, 115, 14217-14228
    • (2011) J. Phys. Chem. B , vol.115 , pp. 14217-14228
    • Voloshin, V.P.1    Medvedev, N.N.2    Andrews, M.N.3    Burri, R.R.4    Winter, R.5    Geiger, A.6
  • 94
    • 0029859688 scopus 로고    scopus 로고
    • Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure
    • Paci, E.; Marchi, M. Intrinsic compressibility and volume compression in solvated proteins by molecular dynamics simulation at high pressure Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 11609-11614
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 11609-11614
    • Paci, E.1    Marchi, M.2
  • 95
    • 0037129516 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of Sodium Dodecyl Sulfate Micelle in Water: Micellar Structural Characteristics and Counterion Distribution
    • Bruce, C. D.; Berkowitz, M. L.; Perera, L.; Forbes, M. D. E. Molecular Dynamics Simulation of Sodium Dodecyl Sulfate Micelle in Water: Micellar Structural Characteristics and Counterion Distribution J. Phys. Chem. B 2002, 106, 3788-3793
    • (2002) J. Phys. Chem. B , vol.106 , pp. 3788-3793
    • Bruce, C.D.1    Berkowitz, M.L.2    Perera, L.3    Forbes, M.D.E.4
  • 96
    • 0002566769 scopus 로고
    • Isothermal compressibility of cyclohexane-n-decane, cyclohexane-n- dodecane, and cyclohexane-n-tetradecane
    • Aicart, E.; Tardajos, G.; Diaz Pena, M. Isothermal compressibility of cyclohexane-n-decane, cyclohexane-n-dodecane, and cyclohexane-n-tetradecane J. Chem. Eng. Data 1981, 26, 22-26
    • (1981) J. Chem. Eng. Data , vol.26 , pp. 22-26
    • Aicart, E.1    Tardajos, G.2    Diaz Pena, M.3
  • 98
    • 33745763431 scopus 로고    scopus 로고
    • The structure of zwitterionic phosphocholine surfactant monolayers
    • Yaseen, M.; Lu, J. R.; Webster, J. R. P.; Penfold, J. The structure of zwitterionic phosphocholine surfactant monolayers Langmuir 2006, 22, 5825-5832
    • (2006) Langmuir , vol.22 , pp. 5825-5832
    • Yaseen, M.1    Lu, J.R.2    Webster, J.R.P.3    Penfold, J.4
  • 100
    • 0026031974 scopus 로고
    • Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons
    • Johnson, S. J.; Bayerl, T. M.; McDermott, D. C.; Adam, G. W.; Rennie, A. R.; Thomas, R. K.; Sackmann, E. Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons Biophys. J. 1991, 59, 289-294
    • (1991) Biophys. J. , vol.59 , pp. 289-294
    • Johnson, S.J.1    Bayerl, T.M.2    McDermott, D.C.3    Adam, G.W.4    Rennie, A.R.5    Thomas, R.K.6    Sackmann, E.7
  • 101
    • 3142723209 scopus 로고    scopus 로고
    • Determination of bilayer thickness and lipid surface area in unilamellar dimyristoylphosphatidylcholine vesicles from small-angle neutron scattering curves: A comparison of evaluation methods
    • Kucerka, N.; Kiselev, M. A.; Balgavý, P. Determination of bilayer thickness and lipid surface area in unilamellar dimyristoylphosphatidylcholine vesicles from small-angle neutron scattering curves: a comparison of evaluation methods Eur. Biophys. J. 2004, 33, 328-334
    • (2004) Eur. Biophys. J. , vol.33 , pp. 328-334
    • Kucerka, N.1    Kiselev, M.A.2    Balgavý, P.3
  • 102
    • 79955574923 scopus 로고    scopus 로고
    • Schrodinger LLC. Version 1.3r1; DeLano Scientific: San Carlos, CA
    • Schrodinger LLC. The PyMOL Molecular Graphics System, Version 1.3r1; DeLano Scientific: San Carlos, CA, 2010.
    • (2010) The PyMOL Molecular Graphics System
  • 103
    • 0017372433 scopus 로고
    • Orientation and flexibility of the choline head group in phosphatidylcholine bilayers
    • Seelig, J.; Gally, H.-U.; Wohlgemuth, R. Orientation and flexibility of the choline head group in phosphatidylcholine bilayers Biochim. Biophys. Acta 1977, 467, 109-119
    • (1977) Biochim. Biophys. Acta , vol.467 , pp. 109-119
    • Seelig, J.1    Gally, H.-U.2    Wohlgemuth, R.3
  • 104
    • 84986483798 scopus 로고
    • The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies
    • Eisenhaber, F.; Lijnzaad, P.; Argos, P.; Sander, C.; Scharf, M. The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies J. Comput. Chem. 1995, 16, 273-284
    • (1995) J. Comput. Chem. , vol.16 , pp. 273-284
    • Eisenhaber, F.1    Lijnzaad, P.2    Argos, P.3    Sander, C.4    Scharf, M.5
  • 105
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • Tsai, J.; Taylor, R.; Chothia, C.; Gerstein, M. The packing density in proteins: standard radii and volumes J. Mol. Biol. 1999, 290, 253-266
    • (1999) J. Mol. Biol. , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 106
    • 77951251864 scopus 로고    scopus 로고
    • Turning the growth hormone receptor on: Evidence that hormone binding induces subunit rotation
    • Poger, D.; Mark, A. E. Turning the growth hormone receptor on: evidence that hormone binding induces subunit rotation Proteins 2010, 78, 1163-1174
    • (2010) Proteins , vol.78 , pp. 1163-1174
    • Poger, D.1    Mark, A.E.2
  • 107
    • 77958105722 scopus 로고    scopus 로고
    • On the hydration of the phosphocholine headgroup in aqueous solution
    • Foglia, F.; Lawrence, M. J.; Lorenz, C. D.; McLain, S. E. On the hydration of the phosphocholine headgroup in aqueous solution J. Chem. Phys. 2010, 133, 145103
    • (2010) J. Chem. Phys. , vol.133 , pp. 145103
    • Foglia, F.1    Lawrence, M.J.2    Lorenz, C.D.3    McLain, S.E.4
  • 108
    • 2942585239 scopus 로고    scopus 로고
    • Hydrogen Bonding Structure and Dynamics of Water at the Dimyristoylphosphatidylcholine Lipid Bilayer Surface from a Molecular Dynamics Simulation
    • Lopez, C. F.; Nielsen, S. O.; Klein, M. L.; Moore, P. B. Hydrogen Bonding Structure and Dynamics of Water at the Dimyristoylphosphatidylcholine Lipid Bilayer Surface from a Molecular Dynamics Simulation J. Phys. Chem. B 2004, 108, 6603-6610
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6603-6610
    • Lopez, C.F.1    Nielsen, S.O.2    Klein, M.L.3    Moore, P.B.4
  • 109
    • 0000112789 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fully hydrated dipalmitoylphosphatidylcholine bilayer with different macroscopic boundary conditions and parameters
    • Tieleman, P. D.; Berendsen, H. J. C. Molecular dynamics simulations of a fully hydrated dipalmitoylphosphatidylcholine bilayer with different macroscopic boundary conditions and parameters J. Chem. Phys. 1996, 105, 4871
    • (1996) J. Chem. Phys. , vol.105 , pp. 4871
    • Tieleman, P.D.1    Berendsen, H.J.C.2
  • 110
    • 0034950798 scopus 로고    scopus 로고
    • Effects of phospholipid unsaturation on the membrane/water interface: A molecular simulation study
    • Murzyn, K.; Róg, T.; Jezierski, G.; Takaoka, Y.; Pasenkiewicz-Gierula, M. Effects of phospholipid unsaturation on the membrane/water interface: a molecular simulation study Biophys. J. 2001, 81, 170-183
    • (2001) Biophys. J. , vol.81 , pp. 170-183
    • Murzyn, K.1    Róg, T.2    Jezierski, G.3    Takaoka, Y.4    Pasenkiewicz-Gierula, M.5
  • 111
    • 0000065270 scopus 로고    scopus 로고
    • Hydrogen Bonding of Water to Phosphatidylcholine in the Membrane As Studied by a Molecular Dynamics Simulation: Location, Geometry, and Lipid-Lipid Bridging via Hydrogen-Bonded Water
    • Pasenkiewicz-Gierula, M.; Takaoka, Y.; Miyagawa, H.; Kitamura, K.; Kusumi, A. Hydrogen Bonding of Water to Phosphatidylcholine in the Membrane As Studied by a Molecular Dynamics Simulation: Location, Geometry, and Lipid-Lipid Bridging via Hydrogen-Bonded Water J. Phys. Chem. A 1997, 101, 3677-3691
    • (1997) J. Phys. Chem. A , vol.101 , pp. 3677-3691
    • Pasenkiewicz-Gierula, M.1    Takaoka, Y.2    Miyagawa, H.3    Kitamura, K.4    Kusumi, A.5
  • 112
    • 0019330575 scopus 로고
    • Polar group conformation of phosphatidylcholine. Effect of solvent and aggregation
    • Hauser, H.; Guyer, W.; Pascher, I.; Skrabal, P.; Sundell, S. 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    Guyer, W.2    Pascher, I.3    Skrabal, P.4    Sundell, S.5
  • 113
  • 114
    • 79953048721 scopus 로고    scopus 로고
    • Headgroup mediated water insertion into the DPPC bilayer: A molecular dynamics study
    • Pandey, P. R.; Roy, S. Headgroup mediated water insertion into the DPPC bilayer: a molecular dynamics study J. Phys. Chem. B 2011, 115, 3155-3163
    • (2011) J. Phys. Chem. B , vol.115 , pp. 3155-3163
    • Pandey, P.R.1    Roy, S.2
  • 115
    • 0025779595 scopus 로고
    • Conformational analysis of the polar head group in phosphatidylcholine bilayers: A structural change induced by cations
    • Akutsu, H.; Nagamori, T. Conformational analysis of the polar head group in phosphatidylcholine bilayers: a structural change induced by cations Biochemistry 1991, 30, 4510-4516
    • (1991) Biochemistry , vol.30 , pp. 4510-4516
    • Akutsu, H.1    Nagamori, T.2
  • 116
    • 0000545128 scopus 로고
    • Conformation of the hydrocarbon chains of sodium dodecyl sulfate molecules in micelles: An FTIR study
    • Holler, F.; Callis, J. B. Conformation of the hydrocarbon chains of sodium dodecyl sulfate molecules in micelles: an FTIR study J. Phys. Chem. 1989, 93, 2053-2058
    • (1989) J. Phys. Chem. , vol.93 , pp. 2053-2058
    • Holler, F.1    Callis, J.B.2
  • 117
    • 15744368593 scopus 로고    scopus 로고
    • An ab initio study on the torsional surface of alkanes and its effect on molecular simulations of alkanes and a DPPC bilayer
    • Klauda, J. B.; Brooks, B. R.; MacKerell, A. D.; Venable, R. M. R. M.; Pastor, R. W.; MacKerell, A. D., Jr. An ab initio study on the torsional surface of alkanes and its effect on molecular simulations of alkanes and a DPPC bilayer J. Phys. Chem. B 2005, 109, 5300-5311
    • (2005) J. Phys. Chem. B , vol.109 , pp. 5300-5311
    • Klauda, J.B.1    Brooks, B.R.2    MacKerell, A.D.3    Venable, R.M.R.M.4    Pastor, R.W.5    Mackerell Jr., A.D.6
  • 118
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S. E.; Zhang, Y.; 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    Brooks, B.R.3
  • 119
    • 0347963579 scopus 로고
    • Molecular Dynamics Simulation Analysis of a Sodium Dodecyl Sulfate Micelle in Aqueous Solution: Decreased Fluidity of the Micelle Hydrocarbon Interior
    • MacKerell, A. D., Jr. Molecular Dynamics Simulation Analysis of a Sodium Dodecyl Sulfate Micelle in Aqueous Solution: Decreased Fluidity of the Micelle Hydrocarbon Interior J. Phys. Chem. 1995, 99, 1846-1855
    • (1995) J. Phys. Chem. , vol.99 , pp. 1846-1855
    • Mackerell Jr., A.D.1
  • 120
    • 0033718963 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of Octyl Glucoside Micelles: Structural Properties
    • Bogusz, S.; Venable, R.; Pastor, R. W. Molecular Dynamics Simulations of Octyl Glucoside Micelles: Structural Properties J. Phys. Chem. B 2000, 104, 5462-5470
    • (2000) J. Phys. Chem. B , vol.104 , pp. 5462-5470
    • Bogusz, S.1    Venable, R.2    Pastor, R.W.3
  • 121
    • 0035822895 scopus 로고    scopus 로고
    • Molecular Dynamics Study of Spherical Aggregates of Chain Molecules at Different Degrees of Hydrophilicity in Water Solution
    • Sterpone, F.; Briganti, G.; Pierleoni, C. Molecular Dynamics Study of Spherical Aggregates of Chain Molecules at Different Degrees of Hydrophilicity in Water Solution Langmuir 2001, 17, 5103-5110
    • (2001) Langmuir , vol.17 , pp. 5103-5110
    • Sterpone, F.1    Briganti, G.2    Pierleoni, C.3


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