메뉴 건너뛰기




Volumn 104, Issue 6, 2013, Pages

Conformational states of melittin at a bilayer interface

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84877086411     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.02.006     Document Type: Article
Times cited : (52)

References (27)
  • 1
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848. (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 3
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic -helices on membranes: Energetics of helix formation by melittin
    • DOI 10.1006/jmbi.1998.2346
    • Ladokhin, A. S., and S. H. White. 1999. Folding of amphipathic a-helices on membranes: energetics of helix formation by melittin. J. Mol. Biol. 285:1363-1369. (Pubitemid 29060439)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 4
    • 0035812599 scopus 로고    scopus 로고
    • Energetics, stability, and prediction of transmembrane helices
    • DOI 10.1006/jmbi.2001.5008
    • Jayasinghe, S., K. Hristova, and S. H. White. 2001. Energetics, stability, and prediction of transmembrane helices. J. Mol. Biol. 312:927-934. (Pubitemid 32980315)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.5 , pp. 927-934
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 5
    • 84855457273 scopus 로고    scopus 로고
    • Hydrogen-bond energetics drive helix formation in membrane interfaces
    • Almeida, P. F., A. S. Ladokhin, and S. H. White. 2012. Hydrogen-bond energetics drive helix formation in membrane interfaces. Biochim. Biophys. Acta. 1818:178-182.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 178-182
    • Almeida, P.F.1    Ladokhin, A.S.2    White, S.H.3
  • 6
    • 0019871670 scopus 로고
    • Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes
    • Vogel, H. 1981. Incorporation of melittin into phosphatidylcholine bilayers. Study of binding and conformational changes. FEBS Lett. 134:37-42.
    • (1981) FEBS Lett , vol.134 , pp. 37-42
    • Vogel, H.1
  • 7
    • 0024328774 scopus 로고
    • Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation
    • DOI 10.1021/bi00436a014
    • Kuchinka, E., and J. Seelig. 1989. Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation. Biochemistry. 28:4216-4221. (Pubitemid 19141622)
    • (1989) Biochemistry , vol.28 , Issue.10 , pp. 4216-4221
    • Kuchinka, E.1    Seelig, J.2
  • 8
    • 0025808271 scopus 로고
    • Effective charge of melittin upon interaction with POPC vesicles
    • Beschiaschvili, G., and H.-D. Baeuerle. 1991. Effective charge of melittin upon interaction with POPC vesicles. Biochim. Biophys. Acta. 1068:195-200.
    • (1991) Biochim. Biophys. Acta , vol.1068 , pp. 195-200
    • Beschiaschvili, G.1    Baeuerle, H.-D.2
  • 9
    • 33751230498 scopus 로고    scopus 로고
    • Diffraction-based density restraints for membrane and membrane-peptide molecular dynamics simulations
    • DOI 10.1529/biophysj.106.084483
    • Benz, R. W., H. Nanda,, D. J. Tobias. 2006. Diffraction-based density restraints for membrane and membrane-peptide molecular dynamics simulations. Biophys. J. 91:3617-3629. (Pubitemid 44788305)
    • (2006) Biophysical Journal , vol.91 , Issue.10 , pp. 3617-3629
    • Benz, R.W.1    Nanda, H.2    Castro-Roman, F.3    White, S.H.4    Tobias, D.J.5
  • 11
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • MacKerell, Jr., A. D., M. Feig, and C. L. Brooks, III. 2004. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25:1400-1415.
    • (2004) J. Comput. Chem , vol.25 , pp. 1400-1415
    • MacKerell Jr., A.D.1    Feig, M.2    Brooks III, C.L.3
  • 12
    • 77953377650 scopus 로고    scopus 로고
    • Update of the CHARMM all-atom additive force field for lipids: Validation on six lipid types
    • Klauda, J. B., R. M. Venable,, R. W. Pastor. 2010. Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types. J. Phys. Chem. B. 114:7830-7843.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 7830-7843
    • Klauda, J.B.1    Venable, R.M.2    Pastor, R.W.3
  • 13
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • Jorgensen, W. L., D. S. Maxwell, and J. Tirado-Rives. 1996. Development and testing of the OPLS all-atom forcefield on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236. (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 14
    • 0035144532 scopus 로고    scopus 로고
    • Structure, location, and lipid perturbations of melittin at the membrane interface
    • Hristova, K., C. E. Dempsey, and S. H. White. 2001. Structure, location, and lipid perturbations of melittin at the membrane interface. Biophys. J. 80:801-811. (Pubitemid 32128331)
    • (2001) Biophysical Journal , vol.80 , Issue.2 , pp. 801-811
    • Hristova, K.1    Dempsey, C.E.2    White, S.H.3
  • 15
    • 0026746013 scopus 로고
    • Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ
    • DOI 10.1021/bi00163a003
    • Dempsey, C. E., and G. S. Butler. 1992. Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ. Biochemistry. 31:11973-11977. (Pubitemid 23011338)
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 11973-11977
    • Dempsey, C.E.1    Butler, G.S.2
  • 16
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • Almeida, P. F., and A. Pokorny. 2009. Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics. Biochemistry. 48:8083-8093.
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 17
    • 78650191386 scopus 로고    scopus 로고
    • CD spectroscopy of peptides and proteins bound to large unilamellar vesicles
    • Ladokhin, A. S., M. Fernández-Vidal, and S. H. White. 2010. CD spectroscopy of peptides and proteins bound to large unilamellar vesicles. J. Membr. Biol. 236:247-253.
    • (2010) J. Membr. Biol , vol.236 , pp. 247-253
    • Ladokhin, A.S.1    Fernández-Vidal, M.2    White, S.H.3
  • 18
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • Vogel, H., and F. Jahnig. 1986. The structure of melittin in membranes. Biophys. J. 50:573-582.
    • (1986) Biophys. J , vol.50 , pp. 573-582
    • Vogel, H.1    Jahnig, F.2
  • 19
    • 84864660053 scopus 로고    scopus 로고
    • Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations
    • Ulmschneider, J. P., J. C. Smith, E. Strandberg. 2012. Reorientation and dimerization of the membrane-bound antimicrobial peptide PGLa from microsecond all-atom MD simulations. Biophys. J. 103:472-482.
    • (2012) Biophys. J. , vol.103 , pp. 472-482
    • Ulmschneider, J.P.1    Smith, J.C.2    Strandberg, E.3
  • 20
    • 22944460220 scopus 로고    scopus 로고
    • Gaussian split Ewald: A fast Ewald mesh method for molecular simulation
    • Shan, Y., J. L. Klepeis,, D. E. Shaw. 2005. Gaussian split Ewald: a fast Ewald mesh method for molecular simulation. J. Chem. Phys. 122:054101-054113.
    • (2005) J. Chem. Phys , vol.122 , pp. 054101-054113
    • Shan, Y.1    Klepeis, J.L.2    Shaw, D.E.3
  • 22
    • 0029633168 scopus 로고
    • GROMACS: A new message-passing parallel molecular dynamics implementation
    • Berendsen, H. J. C., D. van der Spoel, and R. van Drunen. 1995. GROMACS: a new message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 91:43-56.
    • (1995) Comput. Phys. Commun , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 23
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen,W. L., J. Chandrasekhar, M. L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935.
    • (1983) J. Chem. Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 24
    • 67949120080 scopus 로고    scopus 로고
    • United atom lipid parameters for combination with the optimized potentials for liquid simulations all-atom force fields
    • Ulmschneider, J. P., and M. B. Ulmschneider. 2009. United atom lipid parameters for combination with the optimized potentials for liquid simulations all-atom force fields. J. Chem. Theory Comput. 5:1803- 1813.
    • (2009) J. Chem. Theory Comput , vol.5 , pp. 1803-1813
    • Ulmschneider, J.P.1    Ulmschneider, M.B.2
  • 26
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., D. Donadio, and M. Parrinello. 2007. Canonical sampling through velocity rescaling. J. Chem. Phys. 126:014101.
    • (2007) J. Chem. Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 27
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.