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Volumn 99, Issue 8, 2010, Pages 2534-2540

The energetics of transmembrane helix insertion into a lipid bilayer

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EID: 78049275424     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.08.002     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie, J. U. 2005. Solving the membrane protein folding problem. Nature. 438:581-589.
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 2
    • 23044510444 scopus 로고    scopus 로고
    • Transmembrane helices before, during, and after insertion
    • White, S. H., and G. von Heijne. 2005. Transmembrane helices before, during, and after insertion. Curr. Opin. Struct. Biol. 15: 378-386.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 378-386
    • White, S.H.1    Von Heijne, G.2
  • 3
    • 48249095616 scopus 로고    scopus 로고
    • How translocons select transmembrane helices
    • White, S. H., and G. von Heijne. 2008. How translocons select transmembrane helices. Annu. Rev. Biophys. 37:23-42.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 23-42
    • White, S.H.1    Von Heijne, G.2
  • 4
    • 67650869802 scopus 로고    scopus 로고
    • Insertion of short transmembrane helices by the Sec61 translocon
    • Jaud, S., M. Fernández-Vidal,., S. H. White. 2009. Insertion of short transmembrane helices by the Sec61 translocon. Proc. Natl. Acad. Sci. USA. 106:11588-11593.
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 11588-11593
    • Jaud, S.1    Fernández-Vidal, M.2    White, S.H.3
  • 5
    • 74649086575 scopus 로고    scopus 로고
    • Membrane insertion of marginally hydrophobic transmembrane helices depends on sequence context
    • Hedin, L. E., K. Ojemalm, ⋯, A. Elofsson. 2010. Membrane insertion of marginally hydrophobic transmembrane helices depends on sequence context. J. Mol. Biol. 396:221-229.
    • (2010) J. Mol. Biol. , vol.396 , pp. 221-229
    • Hedin, L.E.1    Ojemalm, K.2    Elofsson, A.3
  • 6
    • 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
  • 7
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa, T., H. Kim,., G. von Heijne. 2005. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature. 433:377-381.
    • (2005) Nature. , vol.433 , pp. 377-381
    • Hessa, T.1    Kim, H.2    Von Heijne, G.3
  • 8
    • 43649094583 scopus 로고    scopus 로고
    • Distribution of amino acids in a lipid bilayer from computer simulations
    • MacCallum, J. L., W. F. D. Bennett, and D. P. Tieleman. 2008. Distribution of amino acids in a lipid bilayer from computer simulations. Biophys. J. 94:3393-3404.
    • (2008) Biophys. J. , vol.94 , pp. 3393-3404
    • MacCallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 9
    • 70349436810 scopus 로고    scopus 로고
    • Protein contents in biological membranes can explain abnormal solvation of charged and polar residues
    • Johansson, A. C. V., and E. Lindahl. 2009. Protein contents in biological membranes can explain abnormal solvation of charged and polar residues. Proc. Natl. Acad. Sci. USA. 106:15684-15689.
    • (2009) Proc. Natl. Acad. Sci. USA. , vol.106 , pp. 15684-15689
    • Johansson, A.C.V.1    Lindahl, E.2
  • 10
    • 34247626293 scopus 로고    scopus 로고
    • Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment
    • MacCallum, J. L., W. F. D. Bennett, and D. P. Tieleman. 2007. Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment. J. Gen. Physiol. 129:371-377.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 371-377
    • MacCallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 11
    • 61749104028 scopus 로고    scopus 로고
    • Titratable amino acid solvation in lipid membranes as a function of protonation state
    • Johansson, A. C. V., and E. Lindahl. 2009. Titratable amino acid solvation in lipid membranes as a function of protonation state. J. Phys. Chem. B. 113:245-253.
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 245-253
    • Johansson, A.C.V.1    Lindahl, E.2
  • 12
    • 60849083215 scopus 로고    scopus 로고
    • Analysis of transmembrane helix integration in the endoplasmic reticulum in
    • Hessa, T., J. H. Reithinger, ⋯, H. Kim. 2009. Analysis of transmembrane helix integration in the endoplasmic reticulum in S. cerevisiae. J. Mol. Biol. 386:1222-1228.
    • (2009) S. cerevisiae. J. Mol. Biol. , vol.386 , pp. 1222-1228
    • Hessa, T.1    Reithinger, J.H.2    Kim, H.3
  • 13
    • 63649153519 scopus 로고    scopus 로고
    • Membrane-integration characteristics of two ABC transporters, CFTR and P-glycoprotein
    • Enquist, K., M. Fransson, ⋯, I. Nilsson. 2009. Membrane-integration characteristics of two ABC transporters, CFTR and P-glycoprotein. J. Mol. Biol. 387:1153-1164.
    • (2009) J. Mol. Biol. , vol.387 , pp. 1153-1164
    • Enquist, K.1    Fransson, M.2    Nilsson, I.3
  • 14
    • 66549128460 scopus 로고    scopus 로고
    • The role of lipid composition for insertion and stabilization of amino acids in membranes
    • Johansson, A. C. V., and E. Lindahl. 2009. The role of lipid composition for insertion and stabilization of amino acids in membranes. J. Chem. Phys. 130:185101.
    • (2009) J. Chem. Phys. , vol.130 , pp. 185101
    • Johansson, A.C.V.1    Lindahl, E.2
  • 15
    • 34247633528 scopus 로고    scopus 로고
    • On the thermodynamic stability of a charged arginine side chain in a transmembrane helix
    • Dorairaj, S., and T. W. Allen. 2007. On the thermodynamic stability of a charged arginine side chain in a transmembrane helix. Proc. Natl. Acad. Sci. USA. 104:4943-4948.
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 4943-4948
    • Dorairaj, S.1    Allen, T.W.2
  • 16
    • 53249150686 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer
    • Bond, P. J., C. L. Wee, and M. S. P. Sansom. 2008. Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer. Biochemistry. 47:11321-11331.
    • (2008) Biochemistry , vol.47 , pp. 11321-11331
    • Bond, P.J.1    Wee, C.L.2    Sansom, M.S.P.3
  • 17
    • 75649151376 scopus 로고    scopus 로고
    • Interactions of phospholipid bilayers with several classes of amphiphilic α-helical peptides: Insights from coarse-grained molecular dynamics simulations
    • Gkeka, P., and L. Sarkisov. 2010. Interactions of phospholipid bilayers with several classes of amphiphilic α-helical peptides: Insights from coarse-grained molecular dynamics simulations. J. Phys. Chem. B. 114:826-839.
    • (2010) J. Phys. Chem. B. , vol.114 , pp. 826-839
    • Gkeka, P.1    Sarkisov, L.2
  • 18
    • 0035902367 scopus 로고    scopus 로고
    • A coarse grain model for phospholipid simulations
    • Shelley, J. C., M. Y. Shelley, ⋯, M. L. Klein. 2001. A coarse grain model for phospholipid simulations. J. Phys. Chem. B. 105:4464-4470.
    • (2001) J. Phys. Chem. B. , vol.105 , pp. 4464-4470
    • Shelley, J.C.1    Shelley, M.Y.2    Klein, M.L.3
  • 20
    • 2342473866 scopus 로고    scopus 로고
    • Coarse grain models and the computer simulation of soft materials
    • Nielsen, S. O., C. F. Lopez,., M. L. Klein. 2004. Coarse grain models and the computer simulation of soft materials. J. Phys. Condens. Matter. 16:R481-R512.
    • (2004) J. Phys. Condens. Matter. , vol.16
    • Nielsen, S.O.1    Lopez, C.F.2    Klein, M.L.3
  • 21
    • 17844379740 scopus 로고    scopus 로고
    • Structure and dynamics of model pore insertion into a membrane
    • Lopez, C. F., S. O. Nielsen, ⋯, M. L. Klein. 2005. Structure and dynamics of model pore insertion into a membrane. Biophys. J. 88:3083-3094.
    • (2005) Biophys. J. , vol.88 , pp. 3083-3094
    • Lopez, C.F.1    Nielsen, S.O.2    Klein, M.L.3
  • 22
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J., A. H. de Vries, and A. E. Mark. 2004. Coarse grained model for semiquantitative lipid simulations. J. Phys. Chem. B. 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
  • 23
    • 34547474332 scopus 로고    scopus 로고
    • The MARTINI force field: Coarse grained model for biomolecular simulations
    • Marrink, S. J., H. J. Risselada,., A. H. de Vries. 2007. The MARTINI force field: Coarse grained model for biomolecular simulations. J. Phys. Chem. B. 111:7812-7824.
    • (2007) J. Phys. Chem. B. , vol.111 , pp. 7812-7824
    • Marrink, S.J.1    Risselada, H.J.2    De Vries, A.H.3
  • 24
    • 34548146523 scopus 로고    scopus 로고
    • G protein-coupled receptors self-assemble in dynamics simulations of model bilayers
    • Periole, X., T. Huber,., T. P. Sakmar. 2007. G protein-coupled receptors self-assemble in dynamics simulations of model bilayers. J. Am. Chem. Soc. 129:10126-10132.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10126-10132
    • Periole, X.1    Huber, T.2    Sakmar, T.P.3
  • 25
  • 26
    • 56249119219 scopus 로고    scopus 로고
    • The molecular face of lipid rafts in model membranes
    • Risselada, H. J., and S. J. Marrink. 2008. The molecular face of lipid rafts in model membranes. Proc. Natl. Acad. Sci. USA. 105:17367-17372.
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 17367-17372
    • Risselada, H.J.1    Marrink, S.J.2
  • 27
    • 73349084983 scopus 로고    scopus 로고
    • Combining an elastic network with a coarse-grained molecular force field: Structure, dynamics, and intermolecular recognition
    • Periole, X., M. Cavalli, ⋯, M. A. Ceruso. 2009. Combining an elastic network with a coarse-grained molecular force field: Structure, dynamics, and intermolecular recognition. J. Chem. Theory Comput. 5:2531-2543.
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 2531-2543
    • Periole, X.1    Cavalli, M.2    Ceruso, M.A.3
  • 28
    • 62349108909 scopus 로고    scopus 로고
    • Curvature effects on lipid packing and dynamics in liposomes revealed by coarse grained molecular dynamics simulations
    • Risselada, H. J., and S. J. Marrink. 2009. Curvature effects on lipid packing and dynamics in liposomes revealed by coarse grained molecular dynamics simulations. Phys. Chem. Chem. Phys. 11:2056-2067.
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 2056-2067
    • Risselada, H.J.1    Marrink, S.J.2
  • 29
    • 33644644163 scopus 로고    scopus 로고
    • Insertion and assembly of membrane proteins via simulation
    • Bond, P. J., and M. S. P. Sansom. 2006. Insertion and assembly of membrane proteins via simulation. J. Am. Chem. Soc. 128:2697-2704.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2697-2704
    • Bond, P.J.1    Sansom, M.S.P.2
  • 30
    • 33847242278 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of membrane proteins and peptides
    • Bond, P. J., J. Holyoake, ⋯, M. S. Sansom. 2007. Coarse-grained molecular dynamics simulations of membrane proteins and peptides. J. Struct. Biol. 157:593-605.
    • (2007) J. Struct. Biol. , vol.157 , pp. 593-605
    • Bond, P.J.1    Holyoake, J.2    Sansom, M.S.3
  • 31
    • 41449119304 scopus 로고    scopus 로고
    • Coarse-grained MD simulations of membrane protein-bilayer self-assembly
    • Scott, K. A., P. J. Bond,., M. S. P. Sansom. 2008. Coarse-grained MD simulations of membrane protein-bilayer self-assembly. Structure. 16:621-630.
    • (2008) Structure , vol.16 , pp. 621-630
    • Scott, K.A.1    Bond, P.J.2    Sansom, M.S.P.3
  • 32
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 33
    • 0036430199 scopus 로고    scopus 로고
    • Proline-induced distortions of transmembrane helices
    • Cordes, F. S., J. N. Bright, and M. S. P. Sansom. 2002. Proline-induced distortions of transmembrane helices. J. Mol. Biol. 323:951-960.
    • (2002) J. Mol. Biol. , vol.323 , pp. 951-960
    • Cordes, F.S.1    Bright, J.N.2    Sansom, M.S.P.3
  • 34
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H. J. C., J. P. M. Postma, ⋯, J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81:3684-3690.
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 35
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., A. Dalke, and K. Schulten. 1996. VMD: Visual molecular dynamics. J. Mol. Graph. 14:33-38, 27-28.
    • (1996) J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 36
    • 1642570286 scopus 로고    scopus 로고
    • Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol
    • Mitra, K., I. Ubarretxena-Belandia, ⋯, D. M. Engelman. 2004. Modulation of the bilayer thickness of exocytic pathway membranes by membrane proteins rather than cholesterol. Proc. Natl. Acad. Sci. USA. 101:4083-4088.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 4083-4088
    • Mitra, K.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 37
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method
    • Kumar, S., D. Bouzida,., J. M. Rosenberg. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. 1. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Rosenberg, J.M.3
  • 38
    • 33644849922 scopus 로고    scopus 로고
    • Measurement of thermodynamic parameters for hydrophobic mismatch 1: Self-association of a transmembrane helix
    • Yano, Y., and K. Matsuzaki. 2006. Measurement of thermodynamic parameters for hydrophobic mismatch 1: Self-association of a transmembrane helix. Biochemistry. 45:3370-3378.
    • (2006) Biochemistry , vol.45 , pp. 3370-3378
    • Yano, Y.1    Matsuzaki, K.2
  • 39
    • 69249143221 scopus 로고    scopus 로고
    • Transmembrane vs. non-transmembrane hydrophobic helix topography in model and natural membranes
    • London, E., and K. Shahidullah. 2009. Transmembrane vs. non-transmembrane hydrophobic helix topography in model and natural membranes. Curr. Opin. Struct. Biol. 19:464-472.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 464-472
    • London, E.1    Shahidullah, K.2
  • 40
    • 44349099863 scopus 로고    scopus 로고
    • A continuum method for determining membrane protein insertion energies and the problem of charged residues
    • Choe, S., K. A. Hecht, and M. Grabe. 2008. A continuum method for determining membrane protein insertion energies and the problem of charged residues. J. Gen. Physiol. 131:563-573.
    • (2008) J. Gen. Physiol. , vol.131 , pp. 563-573
    • Choe, S.1    Hecht, K.A.2    Grabe, M.3
  • 41
    • 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
  • 42
    • 77953598334 scopus 로고    scopus 로고
    • Peptide partitioning properties from direct insertion studies
    • Ulmschneider, M. B., J. C. Smith, and J. P. Ulmschneider. 2010. Peptide partitioning properties from direct insertion studies. Biophys. J. 98:L60-L62.
    • (2010) Biophys. J. , vol.98
    • Ulmschneider, M.B.1    Smith, J.C.2    Ulmschneider, J.P.3
  • 43
    • 77950448361 scopus 로고    scopus 로고
    • 3rd. Hydrophobically stabilized open state for the lateral gate of the Sec translocon
    • Zhang, B., and T. F. Miller, 3rd. 2010. Hydrophobically stabilized open state for the lateral gate of the Sec translocon. Proc. Natl. Acad. Sci. USA. 107:5399-5404.
    • (2010) Proc. Natl. Acad. Sci. USA. , vol.107 , pp. 5399-5404
    • Zhang, B.1    Miller, T.F.2
  • 44
    • 77249173166 scopus 로고    scopus 로고
    • Repositioning of transmembrane α-helices during membrane protein folding
    • Kauko, A., L. E. Hedin, ⋯, G. von Heijne. 2010. Repositioning of transmembrane α-helices during membrane protein folding. J. Mol. Biol. 397:190-201.
    • (2010) J. Mol. Biol. , vol.397 , pp. 190-201
    • Kauko, A.1    Hedin, L.E.2    Von Heijne, G.3
  • 45
    • 77952569092 scopus 로고    scopus 로고
    • Changes in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations
    • Vostrikov, V. V., B. A. Hall,., M. S. Sansom. 2010. Changes in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations. J. Am. Chem. Soc. 132:5803-5811.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5803-5811
    • Vostrikov, V.V.1    Hall, B.A.2    Sansom, M.S.3
  • 46
    • 70350774221 scopus 로고    scopus 로고
    • Simulations of the c-subunit of ATP-synthase reveal helix rearrangements
    • Sengupta, D., A. Rampioni, and S. J. Marrink. 2009. Simulations of the c-subunit of ATP-synthase reveal helix rearrangements. Mol. Membr. Biol. 26:422-434.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 422-434
    • Sengupta, D.1    Rampioni, A.2    Marrink, S.J.3
  • 47
    • 70350238527 scopus 로고    scopus 로고
    • Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions
    • discussion
    • Rzepiela, A. J., D. Sengupta, ⋯, S. J. Marrink. 2010. Membrane poration by antimicrobial peptides combining atomistic and coarse-grained descriptions. Faraday Discuss. 144:431-443, discussion 445-481
    • (2010) Faraday Discuss. , vol.144 , Issue.431-443 , pp. 445-481
    • Rzepiela, A.J.1    Sengupta, D.2    Marrink, S.J.3


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