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Volumn 95, Issue 9, 2008, Pages 4241-4245

Hydrophobe-water interactions: Methane as a model

Author keywords

[No Author keywords available]

Indexed keywords

METHANE; WATER;

EID: 57849142600     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.137216     Document Type: Article
Times cited : (13)

References (47)
  • 1
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 2
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen, C. B. 1973. Principles that govern folding of protein chains. Science. 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. 1990. Dominant forces in protein folding. Biochemistry. 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 5
    • 0036840360 scopus 로고    scopus 로고
    • Extent of hydrogen-bond protection in folded proteins: A constraint on packing architectures
    • Fernandez, A., and R. S. Berry. 2002. Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures. Biophys. J. 83:2475-2481.
    • (2002) Biophys. J , vol.83 , pp. 2475-2481
    • Fernandez, A.1    Berry, R.S.2
  • 6
    • 0037058992 scopus 로고    scopus 로고
    • Shea, J. E., J. N. Onuchic, and C. L. Brooks 3rd. 2002. Probing the folding free energy landscape of the Src-SH3 protein domain. Proc. Natl. Acad. Sci. USA. 99:16064-16068.
    • Shea, J. E., J. N. Onuchic, and C. L. Brooks 3rd. 2002. Probing the folding free energy landscape of the Src-SH3 protein domain. Proc. Natl. Acad. Sci. USA. 99:16064-16068.
  • 7
    • 0345133287 scopus 로고    scopus 로고
    • Folding a protein in a computer: An atomic description of folding/unfolding of protein A
    • Garcia, A. E., and J. N. Onuchic. 2003. Folding a protein in a computer: an atomic description of folding/unfolding of protein A. Proc. Natl. Acad. Sci. USA. 100:13898-13903.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13898-13903
    • Garcia, A.E.1    Onuchic, J.N.2
  • 8
    • 0142027822 scopus 로고    scopus 로고
    • Dewetting-induced collapse of hydrophobic particles
    • Huang, X., C. J. Margulis, and B. J. Berne. 2003. Dewetting-induced collapse of hydrophobic particles. Proc. Natl. Acad. Sci. USA. 100:11953-11958.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11953-11958
    • Huang, X.1    Margulis, C.J.2    Berne, B.J.3
  • 9
    • 42749102158 scopus 로고    scopus 로고
    • Dielectric modulation of biological water
    • Despa, F., A. Fernandez, and R. S. Berry. 2004. Dielectric modulation of biological water. Phys. Rev. Lett. 93:228104.
    • (2004) Phys. Rev. Lett , vol.93 , pp. 228104
    • Despa, F.1    Fernandez, A.2    Berry, R.S.3
  • 11
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler, D. 2005. Interfaces and the driving force of hydrophobic assembly. Nature. 437:640-647.
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 12
    • 24344448662 scopus 로고    scopus 로고
    • Observation of a dewetting transition in the collapse of the melittin tetramer
    • Liu, P., X. Huang, R. Zhou, and B. J. Berne. 2005. Observation of a dewetting transition in the collapse of the melittin tetramer. Nature. 437:159-162.
    • (2005) Nature , vol.437 , pp. 159-162
    • Liu, P.1    Huang, X.2    Zhou, R.3    Berne, B.J.4
  • 13
    • 33646161965 scopus 로고    scopus 로고
    • Role of topology, nonadditivity, and water-mediated interactions in predicting the structures of α/β proteins
    • Zong, C., G. A. Papoian, J. Ulander, and P. G. Wolynes. 2006. Role of topology, nonadditivity, and water-mediated interactions in predicting the structures of α/β proteins. J. Am. Chem. Soc. 128:5168-5176.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 5168-5176
    • Zong, C.1    Papoian, G.A.2    Ulander, J.3    Wolynes, P.G.4
  • 14
    • 33846450289 scopus 로고    scopus 로고
    • The origin of the long-range attraction of hydrophobes in water
    • Despa, F., and R. S. Berry. 2007. The origin of the long-range attraction of hydrophobes in water. Biophys. J. 92:373-378.
    • (2007) Biophys. J , vol.92 , pp. 373-378
    • Despa, F.1    Berry, R.S.2
  • 15
    • 34249892163 scopus 로고    scopus 로고
    • Hydrophobic potential of mean force as a salvation function for protein structure prediction
    • Lin, M. S., N. L. Fawzi, and T. Head-Gordon. 2007. Hydrophobic potential of mean force as a salvation function for protein structure prediction. Structure. 15:727-740.
    • (2007) Structure , vol.15 , pp. 727-740
    • Lin, M.S.1    Fawzi, N.L.2    Head-Gordon, T.3
  • 16
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by salvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung, M. S., A. E. Garcia, and J. N. Onuchic. 2002. Protein folding mediated by salvation: water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc. Natl. Acad. Sci. USA. 99:685-690.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 685-690
    • Cheung, M.S.1    Garcia, A.E.2    Onuchic, J.N.3
  • 17
    • 38849196324 scopus 로고    scopus 로고
    • Water as an active constituent in cell biology
    • Ball, P. 2008. Water as an active constituent in cell biology. Chem. Rev. 108:74-108.
    • (2008) Chem. Rev , vol.108 , pp. 74-108
    • Ball, P.1
  • 18
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solutions
    • Duan, Y., and P. A. Kollman. 1998. Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solutions. Science. 282:740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 19
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny, L., and E. Shakhnovich. 2001. Protein folding theory: from lattice to all-atom models. Annu. Rev. Biophys. Biomol. Struct. 30:361-396.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 361-396
    • Mirny, L.1    Shakhnovich, E.2
  • 20
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett, V., and A. Fersht. 2003. The present view of the mechanism of protein folding. Nat. Rev. Mol. Cell Biol. 4:497-502.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 21
    • 0030822464 scopus 로고    scopus 로고
    • Differences in hydration structure near hydrophobic and hydrophilic amino acids
    • Head-Gordon, T., J. M. Sorenson, A. Pertsemlidis, and R. M. Glaeser. 1997. Differences in hydration structure near hydrophobic and hydrophilic amino acids. Biophys. J. 73:2106-2115.
    • (1997) Biophys. J , vol.73 , pp. 2106-2115
    • Head-Gordon, T.1    Sorenson, J.M.2    Pertsemlidis, A.3    Glaeser, R.M.4
  • 22
    • 0033404370 scopus 로고    scopus 로고
    • Solution X-ray scattering as a probe of hydration-dependent structuring of aqueous solutions
    • Hura, G., J. M. Sorenson, R. M. Glaeser, and T. Head-Gordon. 1999. Solution X-ray scattering as a probe of hydration-dependent structuring of aqueous solutions. Perspect. Drug Discov. Des. 17:97-118.
    • (1999) Perspect. Drug Discov. Des , vol.17 , pp. 97-118
    • Hura, G.1    Sorenson, J.M.2    Glaeser, R.M.3    Head-Gordon, T.4
  • 23
    • 0029746155 scopus 로고    scopus 로고
    • Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid
    • Pertsemlidis, A., A. M. Saxena, A. K. Soper, T. Head-Gordon, and R. M. Glaeser. 1996. Direct evidence for modified solvent structure within the hydration shell of a hydrophobic amino acid. Proc. Natl. Acad. Sci. USA. 93:10769-10774.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10769-10774
    • Pertsemlidis, A.1    Saxena, A.M.2    Soper, A.K.3    Head-Gordon, T.4    Glaeser, R.M.5
  • 27
    • 0031553268 scopus 로고    scopus 로고
    • Free energy of the hydrophobic interaction from molecular dynamics simulations: The effect of solute and solvent polarizability
    • Rick, S. W., and B. J. Berne. 1997. Free energy of the hydrophobic interaction from molecular dynamics simulations: the effect of solute and solvent polarizability. J. Phys. Chem. B. 101:10488-10493.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 10488-10493
    • Rick, S.W.1    Berne, B.J.2
  • 29
    • 36849117971 scopus 로고
    • Free volume and entropy in condensed systems III. entropy in binary liquid mixtures; partial molal entropy in dilute solutions; structure and thermodynamics in aqueous electrolytes
    • Frank, H. S., and M. W. Evans. 1945. Free volume and entropy in condensed systems III. entropy in binary liquid mixtures; partial molal entropy in dilute solutions; structure and thermodynamics in aqueous electrolytes. J. Chem. Phys. 13:507-532.
    • (1945) J. Chem. Phys , vol.13 , pp. 507-532
    • Frank, H.S.1    Evans, M.W.2
  • 31
    • 2942560847 scopus 로고    scopus 로고
    • The hydrophobic effect: Molecular dynamics simulations of water confined between extended hydrophobic and hydrophilic surfaces
    • Jensen, M. Ø., O. G. Mouritsen, and G. H. Peters. 2004. The hydrophobic effect: molecular dynamics simulations of water confined between extended hydrophobic and hydrophilic surfaces. J. Chem. Phys. 120:9729-9744.
    • (2004) J. Chem. Phys , vol.120 , pp. 9729-9744
    • Jensen, M.Ø.1    Mouritsen, O.G.2    Peters, G.H.3
  • 32
    • 36749108636 scopus 로고
    • Monte-Carlo simulation of the hydrophobic interaction
    • Pangali, C., M. Rao, and B. J. Berne. 1979. Monte-Carlo simulation of the hydrophobic interaction. J. Chem. Phys. 71:2975-2980.
    • (1979) J. Chem. Phys , vol.71 , pp. 2975-2980
    • Pangali, C.1    Rao, M.2    Berne, B.J.3
  • 33
    • 0011960339 scopus 로고    scopus 로고
    • Hydrophobicity at small and large length scales
    • Lum, K., D. Chandler, and J. D. Weeks. 1999. Hydrophobicity at small and large length scales. J. Phys. Chem. B. 103:4570-4577.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 4570-4577
    • Lum, K.1    Chandler, D.2    Weeks, J.D.3
  • 34
    • 0037076337 scopus 로고    scopus 로고
    • Drying-induced hydrophobic polymer collapse
    • ten Wolde, P. R., and D. Chandler. 2002. Drying-induced hydrophobic polymer collapse. Proc. Natl. Acad. Sci. USA. 99:6539-6543.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6539-6543
    • ten Wolde, P.R.1    Chandler, D.2
  • 35
    • 33748634058 scopus 로고    scopus 로고
    • On the size dependence of hydrophobic hydration
    • Graziano, G. 1998. On the size dependence of hydrophobic hydration. J. Chem. Soc., Faraday Trans. 94:3345-3352.
    • (1998) J. Chem. Soc., Faraday Trans , vol.94 , pp. 3345-3352
    • Graziano, G.1
  • 36
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. 1959. Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14:1-63.
    • (1959) Adv. Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 37
    • 36448999850 scopus 로고
    • Dynamical fluctuating charge force fields: Application to liquid water
    • Rick, S. W., S. J. Stuart, and B. J. Berne. 1994. Dynamical fluctuating charge force fields: application to liquid water. J. Chem. Phys. 101:6141-6156.
    • (1994) J. Chem. Phys , vol.101 , pp. 6141-6156
    • Rick, S.W.1    Stuart, S.J.2    Berne, B.J.3
  • 38
    • 0013271660 scopus 로고
    • Determination of net atomic charges from ab initio self-consistent-field molecular electrostatic properties
    • Chipot, C., B. Maigret, J. L. Rivail, and H. A. Scheraga. 1992. Determination of net atomic charges from ab initio self-consistent-field molecular electrostatic properties. J. Phys. Chem. 96:10276-10284.
    • (1992) J. Phys. Chem , vol.96 , pp. 10276-10284
    • Chipot, C.1    Maigret, B.2    Rivail, J.L.3    Scheraga, H.A.4
  • 39
    • 36549099780 scopus 로고
    • The structure of liquid water at an extended hydrophobic surface
    • Lee, C. Y., J. A. McCammon, and P. J. Rossky. 1984. The structure of liquid water at an extended hydrophobic surface. J. Chem. Phys. 80:4448-4455.
    • (1984) J. Chem. Phys , vol.80 , pp. 4448-4455
    • Lee, C.Y.1    McCammon, J.A.2    Rossky, P.J.3
  • 40
    • 2342655841 scopus 로고    scopus 로고
    • Temperature dependence of the hydrophobic hydration and interaction of simple solutes: An examination of five popular water models
    • Paschek, D. 2004. Temperature dependence of the hydrophobic hydration and interaction of simple solutes: an examination of five popular water models. J. Chem. Phys. 120:6674-6690.
    • (2004) J. Chem. Phys , vol.120 , pp. 6674-6690
    • Paschek, D.1
  • 41
    • 33847704540 scopus 로고    scopus 로고
    • On the influence of solute polarizability on the hydrophobic interaction
    • Bresme, F., and A. Wynveen. 2007. On the influence of solute polarizability on the hydrophobic interaction. J. Chem. Phys. 126:044501.
    • (2007) J. Chem. Phys , vol.126 , pp. 044501
    • Bresme, F.1    Wynveen, A.2
  • 42
    • 49649108879 scopus 로고    scopus 로고
    • Influence of nonlinear electrostatics on transfer energies between liquid phases: Charge burial is far less expensive than Born model
    • In press
    • Gong, H., G. Hocky, and K. F. Freed. 2008. Influence of nonlinear electrostatics on transfer energies between liquid phases: charge burial is far less expensive than Born model. Proc. Natl. Acad. Sci. USA. In press.
    • (2008) Proc. Natl. Acad. Sci. USA
    • Gong, H.1    Hocky, G.2    Freed, K.F.3
  • 43
    • 0022424655 scopus 로고
    • Attractive forces between uncharged hydrophobic surfaces: Direct measurements in aqueous solution
    • Pashley, R. M., P. M. McGuiggan, B. Ninham, and D. F. Evans. 1985. Attractive forces between uncharged hydrophobic surfaces: direct measurements in aqueous solution. Science. 229:1088-1089.
    • (1985) Science , vol.229 , pp. 1088-1089
    • Pashley, R.M.1    McGuiggan, P.M.2    Ninham, B.3    Evans, D.F.4
  • 44
    • 0027922464 scopus 로고
    • Long-range attractive force between hydrophobic surfaces observed by atomic force microscope
    • Tsao, Y.-H., D. F. Evans, and H. Wennerström. 1993. Long-range attractive force between hydrophobic surfaces observed by atomic force microscope. Science. 262:547-550.
    • (1993) Science , vol.262 , pp. 547-550
    • Tsao, Y.-H.1    Evans, D.F.2    Wennerström, H.3
  • 46
    • 33947669512 scopus 로고
    • The potential of mean force surface for the alanine dipeptide in aqueous solution: A theoretical approach
    • Pettitt, B. M., and M. Karplus. 1985. The potential of mean force surface for the alanine dipeptide in aqueous solution: a theoretical approach. Chem. Phys. Lett. 121:194-201.
    • (1985) Chem. Phys. Lett , vol.121 , pp. 194-201
    • Pettitt, B.M.1    Karplus, M.2
  • 47
    • 34247496760 scopus 로고    scopus 로고
    • The dewetting transition and the hydrophobic effect
    • Choudhury, N., and B. M. Pettitt. 2007. The dewetting transition and the hydrophobic effect. J. Am. Chem. Soc. 129:4847-4852.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 4847-4852
    • Choudhury, N.1    Pettitt, B.M.2


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