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Volumn 129, Issue 5, 2007, Pages 371-377

Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYCLOHEXANE; ION CHANNEL; OCTANOL;

EID: 34247626293     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200709745     Document Type: Review
Times cited : (242)

References (20)
  • 1
    • 31544474881 scopus 로고    scopus 로고
    • Computer simulation of partitioning of ten pentapeptides Ace-WLXLL at the cyclohexane/water and phospholipid/water interfaces
    • Aliste, M.P., and D.P. Tieleman. 2005. Computer simulation of partitioning of ten pentapeptides Ace-WLXLL at the cyclohexane/water and phospholipid/water interfaces. BMC Biochem. 6:30.
    • (2005) BMC Biochem , vol.6 , pp. 30
    • Aliste, M.P.1    Tieleman, D.P.2
  • 2
    • 33847258823 scopus 로고    scopus 로고
    • Bilayer deformation by the Kv voltage sensor domain revealed by self-assembly simulations
    • Bond, P.J., and M.S.P. Sansom. 2007. Bilayer deformation by the Kv voltage sensor domain revealed by self-assembly simulations. Proc. Natl. Acad. Sci. USA. 104:2631-2636.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2631-2636
    • Bond, P.J.1    Sansom, M.S.P.2
  • 3
    • 34247633528 scopus 로고    scopus 로고
    • On the thermodynamic stability of a charged arginine sidechain in a transmembrane helix
    • In press
    • Dorairaj, S., and T.W. Allen. 2007. On the thermodynamic stability of a charged arginine sidechain in a transmembrane helix. Proc. Natl. Acad. Sci. USA. In press.
    • (2007) Proc. Natl. Acad. Sci. USA
    • Dorairaj, S.1    Allen, T.W.2
  • 5
    • 11144233948 scopus 로고    scopus 로고
    • A quantitative assessment of models for voltage-dependent gating of ion channels
    • Grabe, M., H. Lecar, Y.N. Jan, and L.Y. Jan. 2004. A quantitative assessment of models for voltage-dependent gating of ion channels. Proc. Natl. Acad. Sci. USA. 101:17640-17645.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17640-17645
    • Grabe, M.1    Lecar, H.2    Jan, Y.N.3    Jan, L.Y.4
  • 7
    • 20044389842 scopus 로고    scopus 로고
    • Membrane insertion of a potassium-channel voltage sensor
    • Hessa, T., S.H. White, and G. von Heijne. 2005b. Membrane insertion of a potassium-channel voltage sensor. Science. 307:1427.
    • (2005) Science , vol.307 , pp. 1427
    • Hessa, T.1    White, S.H.2    von Heijne, G.3
  • 10
    • 33845424528 scopus 로고    scopus 로고
    • Amino-acid solvation structure in transmembrane helices from molecular dynamics simulations
    • Johansson, A.C.V., and E. Lindahl. 2006. Amino-acid solvation structure in transmembrane helices from molecular dynamics simulations. Biophys. J. 91:4450-4463.
    • (2006) Biophys. J , vol.91 , pp. 4450-4463
    • Johansson, A.C.V.1    Lindahl, E.2
  • 12
    • 0037132616 scopus 로고    scopus 로고
    • Structure of neat and hydrated 1-octanol from computer simulations
    • MacCallum, J.L., and D.P. Tieleman. 2002. Structure of neat and hydrated 1-octanol from computer simulations. J. Am. Chem. Soc. 124:15085-15093.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 15085-15093
    • MacCallum, J.L.1    Tieleman, D.P.2
  • 13
    • 30744448428 scopus 로고    scopus 로고
    • Computer simulation of the distribution of hexane in a lipid bilayer: Spatially resolved free energy, entropy, and enthalpy profiles
    • MacCallum, J.L., and D.P. Tieleman. 2006. Computer simulation of the distribution of hexane in a lipid bilayer: spatially resolved free energy, entropy, and enthalpy profiles. J. Am. Chem. Soc. 128:125-130.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 125-130
    • MacCallum, J.L.1    Tieleman, D.P.2
  • 14
    • 33748493587 scopus 로고    scopus 로고
    • Indole localization in lipid membranes revealed by molecular simulation
    • Norman, K.E., and H. Nymeyer. 2006. Indole localization in lipid membranes revealed by molecular simulation. Biophys. J. 91:2046-2054.
    • (2006) Biophys. J , vol.91 , pp. 2046-2054
    • Norman, K.E.1    Nymeyer, H.2
  • 15
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
    • Radzicka, A., and R. Wolfenden. 1988. Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution. Biochemistry. 27:1664-1670.
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 16
    • 3142747401 scopus 로고    scopus 로고
    • Direct simulation of transmembrane helix association: Role of asparagines
    • Stockner, T., W.L. Ash, J.L. MacCallum, and D.P. Tieleman. 2004. Direct simulation of transmembrane helix association: role of asparagines. Biophys. J. 87:1650-1656.
    • (2004) Biophys. J , vol.87 , pp. 1650-1656
    • Stockner, T.1    Ash, W.L.2    MacCallum, J.L.3    Tieleman, D.P.4
  • 17
    • 33645470254 scopus 로고    scopus 로고
    • Polar networks control oligomeric assembly in membranes
    • Tatko, C.D., V. Nanda, J.D. Lear, and W.F. DeGrado. 2006. Polar networks control oligomeric assembly in membranes. J. Am. Chem. Soc. 128:4170-4171.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4170-4171
    • Tatko, C.D.1    Nanda, V.2    Lear, J.D.3    DeGrado, W.F.4
  • 18
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley, W.C., T.P. Creamer, and S.H. White. 1996. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry. 35:5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 19
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W.C., and S.H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 20
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W.-M., W.C. Wimley, K. Gawrisch, and S.H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37:14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.