메뉴 건너뛰기




Volumn 53, Issue 17, 2008, Pages 2599-2606

Molecular dynamics simulation of a single polymer in hydrophilic nano-slits

Author keywords

Confined; Molecular dynamics simulation; Polymer

Indexed keywords


EID: 50849088025     PISSN: 10016538     EISSN: 18619541     Source Type: Journal    
DOI: 10.1007/s11434-008-0371-9     Document Type: Article
Times cited : (5)

References (33)
  • 1
    • 33748496359 scopus 로고
    • First observation of the coil-globule transition in a single polymer chain
    • Nishio I, Sun S T, Swislow G, et al. First observation of the coil-globule transition in a single polymer chain. Nature, 1979, 281: 208-209
    • (1979) Nature , vol.281 , pp. 208-209
    • Nishio, I.1    Sun, S.T.2    Swislow, G.3
  • 2
    • 0029733617 scopus 로고    scopus 로고
    • Polymer solutions in confining geometries
    • Teraoka I. Polymer solutions in confining geometries. Prog Polym Sci, 1996, 21: 89-149
    • (1996) Prog Polym Sci , vol.21 , pp. 89-149
    • Teraoka, I.1
  • 3
    • 0035913902 scopus 로고    scopus 로고
    • Dual function of protein confinement in chaperonin-assisted protein folding
    • Brinker A, Pfeifer G, Kerner M J, et al. Dual function of protein confinement in chaperonin-assisted protein folding. Cell, 2001, 107: 223-233
    • (2001) Cell , vol.107 , pp. 223-233
    • Brinker, A.1    Pfeifer, G.2    Kerner, M.J.3
  • 4
    • 35748958124 scopus 로고    scopus 로고
    • Dynamic control of protein folding pathway with a polymer of tunable hydrophobicity
    • Lu D, Wu J, Liu Z. Dynamic control of protein folding pathway with a polymer of tunable hydrophobicity. J Phys Chem B, 2007, 111: 12303-12309
    • (2007) J Phys Chem B , vol.111 , pp. 12303-12309
    • Lu, D.1    Wu, J.2    Liu, Z.3
  • 5
    • 33344465988 scopus 로고    scopus 로고
    • Influences of fracture orientation on oil recovery by water and polymer flooding processes: An experimental approach
    • Shedid S A. Influences of fracture orientation on oil recovery by water and polymer flooding processes: An experimental approach. J Pet Sci Eng, 2006, 50: 285-292
    • (2006) J Pet Sci Eng , vol.50 , pp. 285-292
    • Shedid, S.A.1
  • 6
    • 0021458355 scopus 로고
    • Concentration dependence of the effective viscosity of polymer solutions in small pores with repulsive or attractive walls
    • Chauveteau G, Tirrell M, Omari A. Concentration dependence of the effective viscosity of polymer solutions in small pores with repulsive or attractive walls. J Colloid Interface Sci, 1984, 100: 41-54
    • (1984) J Colloid Interface Sci , vol.100 , pp. 41-54
    • Chauveteau, G.1    Tirrell, M.2    Omari, A.3
  • 8
    • 0033362566 scopus 로고    scopus 로고
    • Confined polymer chains in poor solvent
    • Cordeiro C E. Confined polymer chains in poor solvent. J Phys Chem Solids, 1999, 60: 1645-1648
    • (1999) J Phys Chem Solids , vol.60 , pp. 1645-1648
    • Cordeiro, C.E.1
  • 9
  • 10
    • 0037156181 scopus 로고    scopus 로고
    • Simulation of short-chain polymer collapse with an explicit solvent
    • Polson J M, Zuckermann M J. Simulation of short-chain polymer collapse with an explicit solvent. J Chem Phys, 2002, 116: 7244-7254
    • (2002) J Chem Phys , vol.116 , pp. 7244-7254
    • Polson, J.M.1    Zuckermann, M.J.2
  • 12
    • 20444380056 scopus 로고    scopus 로고
    • From homogeneous dispersion to micelles-A molecular dynamics simulation on the compromise of the hydrophilic and hydrophobic effects of sodium dodecyl sulfate in aqueous solution
    • Gao J, Ge W, Hu G, et al. From homogeneous dispersion to micelles-A molecular dynamics simulation on the compromise of the hydrophilic and hydrophobic effects of sodium dodecyl sulfate in aqueous solution. Langmuir, 2005, 21: 5223-5229
    • (2005) Langmuir , vol.21 , pp. 5223-5229
    • Gao, J.1    Ge, W.2    Hu, G.3
  • 13
    • 0031207126 scopus 로고    scopus 로고
    • Molecular dynamics simulations of folding in cyclic alkanes
    • Sundararajan P R, Kavassalis T A. Molecular dynamics simulations of folding in cyclic alkanes. Macromolecules, 1997, 30: 5172-5174
    • (1997) Macromolecules , vol.30 , pp. 5172-5174
    • Sundararajan, P.R.1    Kavassalis, T.A.2
  • 15
    • 0027113827 scopus 로고
    • Scaling behavior of dilute polymer solutions confined between parallel plates
    • Vliet J H V, Luyten M C, Brinke G T. Scaling behavior of dilute polymer solutions confined between parallel plates. Macromolecules, 1992, 14: 3802-3806
    • (1992) Macromolecules , vol.14 , pp. 3802-3806
    • Vliet, J.H.V.1    Luyten, M.C.2    Brinke, G.T.3
  • 16
    • 0033742337 scopus 로고    scopus 로고
    • Structures and thermodynamics of nondilute polymer solutions confined between parallel plates
    • Wang Y, Teraoka I. Structures and thermodynamics of nondilute polymer solutions confined between parallel plates. Macromolecules, 2000, 33: 3478-3484
    • (2000) Macromolecules , vol.33 , pp. 3478-3484
    • Wang, Y.1    Teraoka, I.2
  • 17
    • 0001194138 scopus 로고
    • Liquid-vapor interfaces of alkane oligomers: Structure and thermodynamics from molecular dynamics simulations of chemically realistic models
    • Harris J G. Liquid-vapor interfaces of alkane oligomers: Structure and thermodynamics from molecular dynamics simulations of chemically realistic models. J Phys Chem, 1992, 12: 5077-5086
    • (1992) J Phys Chem , vol.12 , pp. 5077-5086
    • Harris, J.G.1
  • 19
    • 0029754167 scopus 로고    scopus 로고
    • Dynamics of confined polymer melts: Topology and entanglement
    • Shaffer J S. Dynamics of confined polymer melts: Topology and entanglement. Macromolecules, 1996, 29: 1010-1013
    • (1996) Macromolecules , vol.29 , pp. 1010-1013
    • Shaffer, J.S.1
  • 20
    • 0001351515 scopus 로고
    • Estimation of absolute and relative entropies of macromolecules using the covariance matrix
    • Schlitter J. Estimation of absolute and relative entropies of macromolecules using the covariance matrix. J Chem Phys Let, 1993, 215: 617-621
    • (1993) J Chem Phys Let , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 21
    • 0036467064 scopus 로고    scopus 로고
    • Entropy calculations on the molten globule state of a protein: Side-chain entropies of α-lactalbumin
    • Heiko S, Lorna. J S, Alan E M, et al. Entropy calculations on the molten globule state of a protein: side-chain entropies of α-lactalbumin. Proteins: Struct Funct Bioinf, 2002, 46, 215-224
    • (2002) Proteins: Struct Funct Bioinf , vol.46 , pp. 215-224
    • Heiko, S.1    Lorna, J.S.2    Alan, E.M.3
  • 22
    • 0034323089 scopus 로고    scopus 로고
    • Absolute entropies from molecular dynamics simulation trajectories
    • Heiko S, Alan E M, Wilfred F V G. Absolute entropies from molecular dynamics simulation trajectories. J Chem Phys, 2000, 113: 7809-7817
    • (2000) J Chem Phys , vol.113 , pp. 7809-7817
    • Heiko, S.1    Alan, E.M.2    Wilfred, F.V.G.3
  • 23
    • 0035828630 scopus 로고    scopus 로고
    • On the calculation of entropy from covariance matrices of the atomic fluctuations
    • Andricioaei I, Karplus M. On the calculation of entropy from covariance matrices of the atomic fluctuations. J Chem Phys, 2001, 115: 6289-6292
    • (2001) J Chem Phys , vol.115 , pp. 6289-6292
    • Andricioaei, I.1    Karplus, M.2
  • 24
    • 33646426637 scopus 로고    scopus 로고
    • Comparison of atomic-level and coarse-grained models for liquid hydrocarbons from molecular dynamics configurational entropy estimates
    • Baron R, deVries A H, Hunenberger P H, et al. Comparison of atomic-level and coarse-grained models for liquid hydrocarbons from molecular dynamics configurational entropy estimates. J Phys Chem B, 2006, 110: 8464-8473
    • (2006) J Phys Chem B , vol.110 , pp. 8464-8473
    • Baron, R.1    Devries, A.H.2    Hunenberger, P.H.3
  • 25
    • 33746837811 scopus 로고    scopus 로고
    • Configurational entropies of lipids in pure and mixed bilayers from atomic-level and coarse-grained molecular dynamics simulations
    • Baron R, deVries A H, Hunenberger P H, et al. Configurational entropies of lipids in pure and mixed bilayers from atomic-level and coarse-grained molecular dynamics simulations. J Phys Chem B, 2006, 110: 15602-15614
    • (2006) J Phys Chem B , vol.110 , pp. 15602-15614
    • Baron, R.1    Devries, A.H.2    Hunenberger, P.H.3
  • 26
    • 0035314075 scopus 로고    scopus 로고
    • Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior
    • Schaer H, Daura X, Mark A E, et al. Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior. Proteins: Struct Funct Bioinf, 2001, 43: 45-56
    • (2001) Proteins: Struct Funct Bioinf , vol.43 , pp. 45-56
    • Schaer, H.1    Daura, X.2    Mark, A.E.3
  • 27
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K A. Dominant forces in protein folding. Biochemistry, 1990, 29: 7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 29
    • 25844437141 scopus 로고    scopus 로고
    • Translational-entropy gain of solvent upon protein folding
    • Harano Y, Kinoshita M. Translational-entropy gain of solvent upon protein folding. Biophys J, 2005, 89: 2701-2710
    • (2005) Biophys J , vol.89 , pp. 2701-2710
    • Harano, Y.1    Kinoshita, M.2
  • 30
    • 20544433165 scopus 로고
    • Van der Waals volumes and radii
    • Bondi A. Van der Waals volumes and radii. J Phys Chem, 1964, 68: 441-451
    • (1964) J Phys Chem , vol.68 , pp. 441-451
    • Bondi, A.1
  • 31
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface: Calculated from simulation, using voronoi polyhedra
    • Gerstein M, Tsai J, Levitt M. The volume of atoms on the protein surface: Calculated from simulation, using voronoi polyhedra. J Mol, 1995, 249: 955-966
    • (1995) J Mol , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3
  • 32
    • 14844303856 scopus 로고    scopus 로고
    • Another face of entropy: Particles self-organize to make room for randomness
    • Weiss P. Another face of entropy: Particles self-organize to make room for randomness. SciNews, 1998, 154: 108-109
    • (1998) SciNews , vol.154 , pp. 108-109
    • Weiss, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.