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Volumn 1838, Issue 1 PARTB, 2014, Pages 98-105

A thermodynamic approach to alamethicin pore formation

Author keywords

Barrel stave; Conductance; Implicit solvent; Ion channel; Membrane; Molecular dynamics simulations

Indexed keywords

ALAMETHICIN; OLIGOMER;

EID: 84887835850     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.09.012     Document Type: Article
Times cited : (16)

References (83)
  • 2
    • 0028226051 scopus 로고
    • Alamethicin: A peptide model for voltage gating and protein-membrane interactions
    • D.S. Cafiso Alamethicin: a peptide model for voltage gating and protein-membrane interactions Annu. Rev. Biophys. Biomol. Struct. 23 1994 141 165 (Pubitemid 24217365)
    • (1994) Annual Review of Biophysics and Biomolecular Structure , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 3
    • 0020360086 scopus 로고
    • A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution
    • DOI 10.1038/300325a0
    • R.O. Fox Jr., and F.M. Richards A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-A resolution Nature 300 1982 325 330 (Pubitemid 13196895)
    • (1982) Nature , vol.300 , Issue.5890 , pp. 325-330
    • Fox Jr., R.O.1    Richards, F.M.2
  • 4
    • 0015513556 scopus 로고
    • The unit conductance channel of alamethicin
    • L.G. Gordon, and D.A. Haydon The unit conductance channel of alamethicin Biochim. Biophys. Acta 255 1972 1014 1018
    • (1972) Biochim. Biophys. Acta , vol.255 , pp. 1014-1018
    • Gordon, L.G.1    Haydon, D.A.2
  • 5
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • G. Baumann, and P. Mueller A molecular model of membrane excitability J. Supramol. Struct. 2 1974 538 557
    • (1974) J. Supramol. Struct. , vol.2 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 6
    • 0016183539 scopus 로고
    • Statistical analysis of alamethicin channels in black lipid membranes
    • G. Boheim Statistical analysis of alamethicin channels in black lipid membranes J. Membr. Biol. 19 1974 277 303
    • (1974) J. Membr. Biol. , vol.19 , pp. 277-303
    • Boheim, G.1
  • 7
    • 0027817476 scopus 로고
    • Structure and function of channel-forming peptaibols
    • M.S. Sansom Structure and function of channel forming peptaibols Q. Rev. Biophys. 26 1993 365 421 (Pubitemid 24141019)
    • (1993) Quarterly Reviews of Biophysics , vol.26 , Issue.4 , pp. 365-421
    • Sansom, M.S.P.1
  • 8
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • DOI 10.1007/s00232-001-0077-2
    • H. Duclohier, and H. Wroblewski Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues J. Membr. Biol. 184 2001 1 12 (Pubitemid 33016166)
    • (2001) Journal of Membrane Biology , vol.184 , Issue.1 , pp. 1-12
    • Duclohier, H.1    Wroblewski, H.2
  • 9
    • 34447317806 scopus 로고    scopus 로고
    • Channel-forming activity of alamethicin: Effects of covalent tethering
    • DOI 10.1002/cbdv.200790113
    • G.A. Woolley Channel-forming activity of alamethicin: effects of covalent tethering Chem. Biodivers. 4 2007 1323 1337 (Pubitemid 47072878)
    • (2007) Chemistry and Biodiversity , vol.4 , Issue.6 , pp. 1323-1337
    • Woolley, G.A.1
  • 10
    • 0028841644 scopus 로고
    • Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15 N NMR
    • C.L. North, M. Barranger-Mathys, and D.S. Cafiso Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15 N NMR Biophys. J. 69 1995 2392 2397
    • (1995) Biophys. J. , vol.69 , pp. 2392-2397
    • North, C.L.1    Barranger-Mathys, M.2    Cafiso, D.S.3
  • 12
    • 84859590055 scopus 로고    scopus 로고
    • Observing a model ion channel gating action in model cell membranes in real time in situ: Membrane potential change induced alamethicin orientation change
    • S.J. Ye, H.C. Li, F. Wei, J. Jasensky, A.P. Boughton, P. Yang, and Z. Chen Observing a model ion channel gating action in model cell membranes in real time in situ: membrane potential change induced alamethicin orientation change J. Am. Chem. Soc. 134 2012 6237 6243
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6237-6243
    • Ye, S.J.1    Li, H.C.2    Wei, F.3    Jasensky, J.4    Boughton, A.P.5    Yang, P.6    Chen, Z.7
  • 13
    • 3042772810 scopus 로고    scopus 로고
    • Conformation of peptides in lipid membranes, studied by x-ray grazing incidence scattering
    • DOI 10.1529/biophysj.104.040667
    • A. Spaar, C. Munster, and T. Salditt Conformation of peptides in lipid membranes studied by X-ray grazing incidence scattering Biophys. J. 87 2004 396 407 (Pubitemid 38880094)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 396-407
    • Spaar, A.1    Munster, C.2    Salditt, T.3
  • 14
    • 0023248806 scopus 로고
    • Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes
    • H. Vogel Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes Biochemistry 26 1987 4562 4572 (Pubitemid 17131552)
    • (1987) Biochemistry , vol.26 , Issue.14 , pp. 4562-4572
    • Vogel, H.1
  • 15
    • 0025889072 scopus 로고
    • Lipid-alamethicin interactions influence alamethicin orientation
    • H.W. Huang, and Y. Wu Lipid-alamethicin interactions influence alamethicin orientation Biophys. J. 60 1991 1079 1087
    • (1991) Biophys. J. , vol.60 , pp. 1079-1087
    • Huang, H.W.1    Wu, Y.2
  • 16
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • K. He, S.J. Ludtke, W.T. Heller, and H.W. Huang Mechanism of alamethicin insertion into lipid bilayers Biophys. J. 71 1996 2669 2679 (Pubitemid 26367729)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 17
    • 0025832273 scopus 로고
    • Dynamics and aggregation of the peptide ion channel alamethicin - Measurements using spin-labeled peptides
    • S.J. Archer, J.F. Ellena, and D.S. Cafiso Dynamics and aggregation of the peptide ion channel alamethicin - measurements using spin-labeled peptides Biophys. J. 60 1991 389 398
    • (1991) Biophys. J. , vol.60 , pp. 389-398
    • Archer, S.J.1    Ellena, J.F.2    Cafiso, D.S.3
  • 18
    • 0028244098 scopus 로고
    • Collisions between helical peptides in membranes monitored using electron paramagnetic resonance: Evidence that alamethicin is monomeric in the absence of a membrane potential
    • M. Barranger-Mathys, and D.S. Cafiso Collisions between helical peptides in membranes monitored using electron-paramagnetic-resonance - evidence that alamethicin is monomeric in the absence of a membrane-potential Biophys. J. 67 1994 172 176 (Pubitemid 24197881)
    • (1994) Biophysical Journal , vol.67 , Issue.1 , pp. 172-176
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 19
    • 33846452163 scopus 로고    scopus 로고
    • TOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranes
    • DOI 10.1529/biophysj.106.092775
    • D. Marsh, M. Jost, C. Peggion, and C. Toniolo TOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranes Biophys. J. 92 2007 473 481 (Pubitemid 46145780)
    • (2007) Biophysical Journal , vol.92 , Issue.2 , pp. 473-481
    • Marsh, D.1    Jost, M.2    Peggion, C.3    Toniolo, C.4
  • 20
    • 0023056958 scopus 로고
    • Thermodynamic analysis of incorporation and aggregation in a membrane: Application to the pore-forming peptide alamethicin
    • G. Schwarz, S. Stankowski, and V. Rizzo Thermodynamic analysis of incorporation and aggregation in a membrane: application to the pore-forming peptide alamethicin Biochim. Biophys. Acta 861 1986 141 151
    • (1986) Biochim. Biophys. Acta , vol.861 , pp. 141-151
    • Schwarz, G.1    Stankowski, S.2    Rizzo, V.3
  • 21
    • 0023754246 scopus 로고
    • Conformation of alamethicin in phospholipid-vesicles - Implications for insertion models
    • M. Cascio, and B.A. Wallace Conformation of alamethicin in phospholipid-vesicles - implications for insertion models Proteins Struct. Funct. Genet. 4 1988 89 98
    • (1988) Proteins Struct. Funct. Genet. , vol.4 , pp. 89-98
    • Cascio, M.1    Wallace, B.A.2
  • 22
    • 0023949690 scopus 로고
    • Alamethicin adsorption to a planar lipid bilayer
    • I. Vodyanoy, J.E. Hall, and V. Vodyanoy Alamethicin adsorption to a planar lipid bilayer Biophys. J. 53 1988 649 657
    • (1988) Biophys. J. , vol.53 , pp. 649-657
    • Vodyanoy, I.1    Hall, J.E.2    Vodyanoy, V.3
  • 23
    • 34547659143 scopus 로고    scopus 로고
    • Self-aggregation of spin-labeled alamethicin in ePC vesicles studied by pulsed electron-electron double resonance
    • A.D. Milov, R.I. Samoilova, Y.D. Tsvetkov, F. Formaggio, C. Toniolo, and J. Raap Self-aggregation of spin-labeled alamethicin in ePC vesicles studied by pulsed electron-electron double resonance J. Am. Chem. Soc. 129 2007 9260-+
    • (2007) J. Am. Chem. Soc. , vol.129
    • Milov, A.D.1    Samoilova, R.I.2    Tsvetkov, Y.D.3    Formaggio, F.4    Toniolo, C.5    Raap, J.6
  • 25
    • 0027376758 scopus 로고
    • Temperature dependence of the interaction of alamethicin helices in membranes
    • G.A. Woolley, and B.A. Wallace Temperature dependence of the interaction of alamethicin helices in membranes Biochemistry 32 1993 9819 9825 (Pubitemid 23296829)
    • (1993) Biochemistry , vol.32 , Issue.37 , pp. 9819-9825
    • Woolley, G.A.1    Wallace, B.A.2
  • 26
    • 0030028241 scopus 로고    scopus 로고
    • Neutron scattering in the plane of membranes: Structure of alamethicin pores
    • K. He, S.J. Ludtke, D.L. Worcester, and H.W. Huang Neutron scattering in the plane of membranes: structure of alamethicin pores Biophys. J. 70 1996 2659 2666 (Pubitemid 26000964)
    • (1996) Biophysical Journal , vol.70 , Issue.6 , pp. 2659-2666
    • He, K.1    Ludtke, S.J.2    Worcester, D.L.3    Huang, H.W.4
  • 27
    • 0027400112 scopus 로고
    • Probing alamethicin channels with water-soluble polymers. Effect on conductance of channel states
    • S.M. Bezrukov, and I. Vodyanoy Probing alamethicin channels with water-soluble polymers - effect on conductance of channel states Biophys. J. 64 1993 16 25 (Pubitemid 23063923)
    • (1993) Biophysical Journal , vol.64 , Issue.1 , pp. 16-25
    • Beznukov, S.M.1    Vodyanoy, I.2
  • 29
    • 0034043224 scopus 로고    scopus 로고
    • Asymmetrical ion-channel model inferred from two-dimensional crystallization of a peptide antibiotic
    • R. Ionov, A. El-Abed, A. Angelova, M. Goldmann, and P. Peretti Asymmetrical ion-channel model inferred from two-dimensional crystallization of a peptide antibiotic Biophys. J. 78 2000 3026 3035 (Pubitemid 30396933)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 3026-3035
    • Ionov, R.1    El-Abed, A.2    Angelova, A.3    Goldmann, M.4    Peretti, P.5
  • 30
    • 0031022167 scopus 로고    scopus 로고
    • Simulation studies of alamethicin-bilayer interactions
    • P.C. Biggin, J. Breed, H.S. Son, and M.S. Sansom Simulation studies of alamethicin-bilayer interactions Biophys. J. 72 1997 627 636 (Pubitemid 27044872)
    • (1997) Biophysical Journal , vol.72 , Issue.2 , pp. 627-636
    • Biggin, P.C.1    Breed, J.2    Son, H.S.3    Sansom, M.S.P.4
  • 31
    • 0031001316 scopus 로고    scopus 로고
    • Alamethicin channels - modelling via restrained molecular dynamics simulations
    • DOI 10.1016/S0005-2736(96)00262-3, PII S0005273696002623
    • J. Breed, P.C. Biggin, I.D. Kerr, O.S. Smart, and M.S.P. Sansom Alamethicin channels - modelling via restrained molecular dynamics simulations Biochim. Biophys. Acta Biomembr. 1325 1997 235 249 (Pubitemid 27193279)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1325 , Issue.2 , pp. 235-249
    • Breed, J.1    Biggin, P.C.2    Kerr, I.D.3    Smart, O.S.4    Sansom, M.S.P.5
  • 32
    • 0030916534 scopus 로고    scopus 로고
    • Helix bending in alamethicin: Molecular dynamics simulations and amide hydrogen exchange in methanol
    • N. Gibbs, R.B. Sessions, P.B. Williams, and C.E. Dempsey Helix bending in alamethicin: molecular dynamics simulations and amide hydrogen exchange in methanol Biophys. J. 72 1997 2490 2495 (Pubitemid 27227585)
    • (1997) Biophysical Journal , vol.72 , Issue.6 , pp. 2490-2495
    • Gibbs, N.1    Sessions, R.B.2    Williams, P.B.3    Dempsey, C.E.4
  • 33
    • 0032951553 scopus 로고    scopus 로고
    • Alamethicin helices in a bilayer and in solution: Molecular dynamics simulations
    • D.P. Tieleman, M.S. Sansom, and H.J. Berendsen Alamethicin helices in a bilayer and in solution: molecular dynamics simulations Biophys. J. 76 1999 40 49 (Pubitemid 29202436)
    • (1999) Biophysical Journal , vol.76 , Issue.1 , pp. 40-49
    • Tieleman, D.P.1    Sansom, M.S.P.2    Berendsen, H.J.C.3
  • 35
    • 0032998180 scopus 로고    scopus 로고
    • Surface binding of alamethicin stabilizes its helical structure: Molecular dynamics simulations
    • D.P. Tieleman, H.J. Berendsen, and M.S. Sansom Surface binding of alamethicin stabilizes its helical structure: molecular dynamics simulations Biophys. J. 76 1999 3186 3191 (Pubitemid 29269465)
    • (1999) Biophysical Journal , vol.76 , Issue.6 , pp. 3186-3191
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 36
    • 0035132984 scopus 로고    scopus 로고
    • Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces
    • D.P. Tieleman, H.J.C. Berendsen, and M.S.P. Sansom Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces Biophys. J. 80 2001 331 346
    • (2001) Biophys. J. , vol.80 , pp. 331-346
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 37
    • 0033035249 scopus 로고    scopus 로고
    • An alamethicin channel in a lipid bilayer: Molecular dynamics simulations
    • D.P. Tieleman, H.J. Berendsen, and M.S. Sansom An alamethicin channel in a lipid bilayer: molecular dynamics simulations Biophys. J. 76 1999 1757 1769 (Pubitemid 29266335)
    • (1999) Biophysical Journal , vol.76 , Issue.4 , pp. 1757-1769
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 38
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • D.P. Tieleman, B. Hess, and M.S. Sansom Analysis and evaluation of channel models: simulations of alamethicin Biophys. J. 83 2002 2393 2407 (Pubitemid 35265736)
    • (2002) Biophysical Journal , vol.83 , Issue.5 , pp. 2393-2407
    • Peter Tieleman, D.1    Hess, B.2    Sansom, M.S.P.3
  • 39
    • 0037341764 scopus 로고    scopus 로고
    • Understanding pH-dependent selectivity of alamethicin K18 channels by computer simulation
    • D.P. Tieleman, V. Borisenko, M.S.P. Sansom, and G.A. Woolley Understanding pH-dependent selectivity of alamethicin K18 channels by computer simulation Biophys. J. 84 2003 1464 1469 (Pubitemid 36322915)
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 1464-1469
    • Tieleman, D.P.1    Borisenko, V.2    Sansom, M.S.P.3    Woolley, G.A.4
  • 40
    • 58149164577 scopus 로고    scopus 로고
    • Peptide aggregation and pore formation in lipid bilayer: A combined coarse-grained and all atom model
    • L. Thogersen, B. Schiott, T. Vosegaard, N.C. Nielsen, and E. Tajkhorsid Peptide aggregation and pore formation in lipid bilayer: a combined coarse-grained and all atom model Biophys. J. 95 2008 4337 4347
    • (2008) Biophys. J. , vol.95 , pp. 4337-4347
    • Thogersen, L.1    Schiott, B.2    Vosegaard, T.3    Nielsen, N.C.4    Tajkhorsid, E.5
  • 41
    • 0034118188 scopus 로고    scopus 로고
    • Continuum solvent model calculations of alamethicin-membrane interactions: Thermodynamic aspects
    • A. Kessel, D.S. Cafiso, and N. Ben-Tal Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects Biophys. J. 78 2000 571 583 (Pubitemid 30211817)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 571-583
    • Kessel, A.1    Cafiso, D.S.2    Ben-Tal, N.3
  • 42
    • 1042267271 scopus 로고    scopus 로고
    • Implicit solvent model estimates of the stability of model structures of the alamethicin channel
    • DOI 10.1007/s00249-003-0345-4
    • A. Kessel, D.P. Tieleman, and N. Ben-Tal Implicit solvent model estimates of the stability of model structures of the alamethicin channel Eur. Biophys. J. 33 2004 16 28 (Pubitemid 38198715)
    • (2004) European Biophysics Journal , vol.33 , Issue.1 , pp. 16-28
    • Kessel, A.1    Tieleman, D.P.2    Ben-Tal, N.3
  • 43
    • 33745002504 scopus 로고    scopus 로고
    • Voltage-dependent energetics of alamethicin monomers in the membrane
    • DOI 10.1016/j.bpc.2006.02.005, PII S0301462206000469
    • M. Mottamal, and T. Lazaridis Voltage-dependent energetics of alamethicin monomers in the membrane Biophys. Chem. 122 2006 50 57 (Pubitemid 43867164)
    • (2006) Biophysical Chemistry , vol.122 , Issue.1 , pp. 50-57
    • Mottamal, M.1    Lazaridis, T.2
  • 44
    • 0030024628 scopus 로고    scopus 로고
    • Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling
    • M. Barranger-Mathys, and D.S. Cafiso Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling Biochemistry 35 1996 498 505
    • (1996) Biochemistry , vol.35 , pp. 498-505
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 45
    • 84855962625 scopus 로고    scopus 로고
    • Influence of membrane dipole potential on peptide binding to lipid bilayers
    • H. Zhan, and T. Lazaridis Influence of membrane dipole potential on peptide binding to lipid bilayers Biophys. Chem. 161 2012 1 7
    • (2012) Biophys. Chem. , vol.161 , pp. 1-7
    • Zhan, H.1    Lazaridis, T.2
  • 46
    • 84873383442 scopus 로고    scopus 로고
    • Inclusion of lateral pressure/curvature stress effects in implicit solvation models
    • (in press)
    • H. Zhan, and T. Lazaridis Inclusion of lateral pressure/curvature stress effects in implicit solvation models Biophys. J. 2013 (in press)
    • (2013) Biophys. J.
    • Zhan, H.1    Lazaridis, T.2
  • 47
    • 0038675609 scopus 로고    scopus 로고
    • Effective energy function for proteins in lipid membranes
    • DOI 10.1002/prot.10410
    • T. Lazaridis Effective energy function for proteins in lipid membranes Proteins Struct. Funct. Genet. 52 2003 176 192 (Pubitemid 36828942)
    • (2003) Proteins: Structure, Function and Genetics , vol.52 , Issue.2 , pp. 176-192
    • Lazaridis, T.1
  • 48
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • DOI 10.1002/(SICI)1097-0134(19990501)35:2<133::AID-PROT1>3.0.CO;2-N
    • T. Lazaridis, and M. Karplus Effective energy function for proteins in solution Proteins 35 1999 133 152 (Pubitemid 29165128)
    • (1999) Proteins: Structure, Function and Genetics , vol.35 , Issue.2 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 49
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • E. Neria, S. Fischer, and M. Karplus Simulation of activation free energies in molecular systems J. Chem. Phys. 105 1996 1902 1921 (Pubitemid 126612899)
    • (1996) Journal of Chemical Physics , vol.105 , Issue.5 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 50
    • 33744997947 scopus 로고    scopus 로고
    • Structural determinants of transmembrane beta-barrels
    • T. Lazaridis Structural determinants of transmembrane beta-barrels J. Chem. Theory Comput. 1 2005 716 722
    • (2005) J. Chem. Theory Comput. , vol.1 , pp. 716-722
    • Lazaridis, T.1
  • 51
    • 77953705223 scopus 로고    scopus 로고
    • Antimicrobial peptides bind more strongly to membrane pores
    • M. Mihajlovic, and T. Lazaridis Antimicrobial peptides bind more strongly to membrane pores Biochim. Biophys. Acta 1798 2010 1494 1502
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1494-1502
    • Mihajlovic, M.1    Lazaridis, T.2
  • 52
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • DOI 10.1006/jmbi.1998.2401
    • J.M. Word, S.C. Lovell, J.S. Richardson, and D.C. Richardson Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation J. Mol. Biol. 285 1999 1735 1747 (Pubitemid 29060467)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 53
    • 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
    • A.D. MacKerell Jr., M. Feig, and I.C.L. Brooks 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 2004 1400 1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • Mackerell, Jr.A.D.1    Feig, M.2    Brooks, I.C.L.3
  • 55
    • 33845293800 scopus 로고    scopus 로고
    • Energetic determinants of oligomeric state specificity in coiled coils
    • DOI 10.1021/ja0655284
    • J. Ramos, and T. Lazaridis Energetic determinants of oligomeric state specificity in coiled coils J. Am. Chem. Soc. 128 2006 15499 15510 (Pubitemid 44876026)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.48 , pp. 15499-15510
    • Ramos, J.1    Lazaridis, T.2
  • 56
    • 77953724763 scopus 로고    scopus 로고
    • Antimicrobial peptides in toroidal and cylindrical pores
    • M. Mihajlovic, and T. Lazaridis Antimicrobial peptides in toroidal and cylindrical pores Biochim. Biophys. Acta 1798 2010 1485 1493
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1485-1493
    • Mihajlovic, M.1    Lazaridis, T.2
  • 57
    • 43649098591 scopus 로고    scopus 로고
    • Structure of the alamethicin pore reconstructed by X-ray diffraction analysis
    • S. Qian, W.C. Wang, L. Yang, and H.W. Huang Structure of the alamethicin pore reconstructed by X-ray diffraction analysis Biophys. J. 94 2008 3512 3522
    • (2008) Biophys. J. , vol.94 , pp. 3512-3522
    • Qian, S.1    Wang, W.C.2    Yang, L.3    Huang, H.W.4
  • 58
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring (Review)
    • DOI 10.1080/09687680310001605352
    • M.R.R. de Planque, and J.A. Killian Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring Review Mol. Membr. Biol. 20 2003 271 284 (Pubitemid 37406619)
    • (2003) Molecular Membrane Biology , vol.20 , Issue.4 , pp. 271-284
    • De Planque, M.R.R.1    Killian, J.A.2
  • 59
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • DOI 10.1146/annurev.biophys.36.040306.132643
    • O.S. Andersen, and R.E. Koeppe Bilayer thickness and membrane protein function: an energetic perspective Annu. Rev. Biophys. Biomol. Struct. 36 2007 107 130 (Pubitemid 46998112)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 60
    • 0028790410 scopus 로고
    • Antimicrobial peptide pores in membranes detected by neutron in-plane scattering
    • K. He, S.J. Ludtke, H.W. Huang, and D.L. Worcester Antimicrobial peptide pores in membranes detected by neutron in-plane scattering Biochemistry 34 1995 15614 15618
    • (1995) Biochemistry , vol.34 , pp. 15614-15618
    • He, K.1    Ludtke, S.J.2    Huang, H.W.3    Worcester, D.L.4
  • 61
    • 84871832622 scopus 로고    scopus 로고
    • Direct visualization of the alamethicin pore formed in a planar phospholipid matrix
    • P. Pieta, J. Mirza, and J. Lipkowski Direct visualization of the alamethicin pore formed in a planar phospholipid matrix Proc. Natl. Acad. Sci. U. S. A. 109 2012 21223 21227
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 21223-21227
    • Pieta, P.1    Mirza, J.2    Lipkowski, J.3
  • 62
    • 67649394753 scopus 로고    scopus 로고
    • Structure of self-aggregated alamethicin in ePC membranes detected by pulsed electron-electron double resonance and electron spin echo envelope modulation spectroscopies
    • A.D. Milov, R.I. Samoilova, Y.D. Tsvetkov, M. De Zotti, F. Formaggio, C. Toniolo, J.W. Handgraaf, and J. Raap Structure of self-aggregated alamethicin in ePC membranes detected by pulsed electron-electron double resonance and electron spin echo envelope modulation spectroscopies Biophys. J. 96 2009 3197 3209
    • (2009) Biophys. J. , vol.96 , pp. 3197-3209
    • Milov, A.D.1    Samoilova, R.I.2    Tsvetkov, Y.D.3    De Zotti, M.4    Formaggio, F.5    Toniolo, C.6    Handgraaf, J.W.7    Raap, J.8
  • 63
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • S.L. Keller, S.M. Bezrukov, S.M. Gruner, M.W. Tate, I. Vodyanoy, and V.A. Parsegian Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids Biophys. J. 65 1993 23 27 (Pubitemid 23206034)
    • (1993) Biophysical Journal , vol.65 , Issue.1 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 64
    • 0031679215 scopus 로고    scopus 로고
    • Effect of lipid characteristics on the structure of transmembrane proteins
    • N. Dan, and S.A. Safran Effect of lipid characteristics on the structure of transmembrane proteins Biophys. J. 75 1998 1410 1414 (Pubitemid 28397610)
    • (1998) Biophysical Journal , vol.75 , Issue.3 , pp. 1410-1414
    • Dan, N.1    Safran, S.A.2
  • 65
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of Barrel-Stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile
    • R.S. Cantor Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile Biophys. J. 82 2002 2520 2525 (Pubitemid 34441291)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2520-2525
    • Cantor, R.S.1
  • 66
    • 0027293464 scopus 로고
    • Alamethicin and related peptaibols - Model ion channels
    • M.S.P. Sansom Alamethicin and related peptaibols - model ion channels Eur. Biophys. J. 22 1993 105 124 (Pubitemid 23275443)
    • (1993) European Biophysics Journal , vol.22 , Issue.2 , pp. 105-124
    • Sansom, M.S.P.1
  • 67
    • 84873383442 scopus 로고    scopus 로고
    • Inclusion of lateral pressure/curvature stress effects in implicit membrane models
    • H. Zhan, and T. Lazaridis Inclusion of lateral pressure/curvature stress effects in implicit membrane models Biophys. J. 104 2013 643 654
    • (2013) Biophys. J. , vol.104 , pp. 643-654
    • Zhan, H.1    Lazaridis, T.2
  • 68
    • 0036280431 scopus 로고    scopus 로고
    • Modifications of alamethicin ion channels by substitution of Glu-7 for Gln-7
    • K. Asami, T. Okazaki, Y. Nagai, and Y. Nagaoka Modifications of alamethicin ion channels by substitution of Glu-7 for Gln-7 Biophys. J. 83 2002 219 228 (Pubitemid 34694733)
    • (2002) Biophysical Journal , vol.83 , Issue.1 , pp. 219-228
    • Asami, K.1    Okazaki, T.2    Nagai, Y.3    Nagaoka, Y.4
  • 69
    • 34848857573 scopus 로고    scopus 로고
    • PH modulation of transport properties of alamethicin oligomers inserted in zwitterionic-based artificial lipid membranes
    • DOI 10.1016/j.bpc.2007.08.009, PII S0301462207002013
    • R. Chiriac, and T. Luchian pH modulation of transport properties of alamethicin oligomers inserted in zwitterionic-based artificial lipid membranes Biophys. Chem. 130 2007 139 147 (Pubitemid 47498711)
    • (2007) Biophysical Chemistry , vol.130 , Issue.3 , pp. 139-147
    • Chiriac, R.1    Luchian, T.2
  • 70
    • 84864456742 scopus 로고    scopus 로고
    • Gain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening
    • A.J. Krauson, J. He, and W.C. Wimley Gain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening J. Am. Chem. Soc. 134 2012 12732 12741
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 12732-12741
    • Krauson, A.J.1    He, J.2    Wimley, W.C.3
  • 71
    • 0017869782 scopus 로고
    • Analysis of the multi-pore system of alamethicin in a lipid membrane. I. Voltage-jump current-relaxation measurements
    • G. Boheim, and H.A. Kolb Analysis of multi-pore system of alamethicin in a lipid-membrane.1. Voltage jump current relaxation measurements J. Membr. Biol. 38 1978 99 150 (Pubitemid 8262768)
    • (1978) Journal of Membrane Biology , vol.38 , Issue.1-2 , pp. 99-150
    • Boheim, G.1    Kolb, H.A.2
  • 72
    • 0023251067 scopus 로고
    • Alamethicin incorporation in lipid bilayers: A thermodynamic study
    • DOI 10.1021/bi00384a015
    • V. Rizzo, S. Stankowski, and G. Schwarz Alamethicin incorporation in lipid bilayers - a thermodynamic study Biochemistry 26 1987 2751 2759 (Pubitemid 17084646)
    • (1987) Biochemistry , vol.26 , Issue.10 , pp. 2751-2759
    • Rizzo, V.1    Stankowski, S.2    Schwarz, G.3
  • 74
    • 70350660660 scopus 로고    scopus 로고
    • Chemical labeling strategy with (R)- and (S)-trifluoromethylaianine for solid state F-19 NMR analysis of peptaibols in membranes
    • D. Maisch, P. Wadhwani, S. Afonin, C. Bottcher, B. Koksch, and A.S. Ulrich Chemical labeling strategy with (R)- and (S)-trifluoromethylaianine for solid state F-19 NMR analysis of peptaibols in membranes J. Am. Chem. Soc. 131 2009 15596-+
    • (2009) J. Am. Chem. Soc. , vol.131
    • Maisch, D.1    Wadhwani, P.2    Afonin, S.3    Bottcher, C.4    Koksch, B.5    Ulrich, A.S.6
  • 75
    • 60749131043 scopus 로고    scopus 로고
    • Orientation and peptide-lipid interactions of alamethicin incorporated in phospholipid membranes: Polarized infrared and spin-label EPR spectroscopy
    • D. Marsh Orientation and peptide-lipid interactions of alamethicin incorporated in phospholipid membranes: polarized infrared and spin-label EPR spectroscopy Biochemistry 48 2009 729 737
    • (2009) Biochemistry , vol.48 , pp. 729-737
    • Marsh, D.1
  • 76
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • DOI 10.1038/72440
    • C. Choma, H. Gratkowski, J.D. Lear, and W.F. DeGrado Asn-mediated self-association of a model transmembrane helix Nat. Struct. Biol. 7 2000 161 166 (Pubitemid 30082515)
    • (2000) Nature Structural Biology , vol.7 , Issue.2 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 77
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • DOI 10.1006/jmbi.2001.5353
    • J.P. Dawson, J.S. Weinger, and D.M. Engelman Motifs of Ser and Thr can drive association of transmembrane helices J. Mol. Biol. 316 2002 799 805 (Pubitemid 34729255)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.3 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 78
    • 33748446964 scopus 로고    scopus 로고
    • Calculating the free energy of association of transmembrane helices
    • DOI 10.1529/biophysj.106.081224
    • J.M. Zhang, and T. Lazaridis Calculating the free energy of association of transmembrane helices Biophys. J. 91 2006 1710 1723 (Pubitemid 44352436)
    • (2006) Biophysical Journal , vol.91 , Issue.5 , pp. 1710-1723
    • Zhang, J.1    Lazaridis, T.2
  • 79
    • 68949142901 scopus 로고    scopus 로고
    • Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues
    • J.M. Zhang, and T. Lazaridis Transmembrane helix association affinity can be modulated by flanking and noninterfacial residues Biophys. J. 96 2009 4418 4427
    • (2009) Biophys. J. , vol.96 , pp. 4418-4427
    • Zhang, J.M.1    Lazaridis, T.2
  • 80
    • 68749100896 scopus 로고    scopus 로고
    • Non-equilibrium thermodynamic potential and flux fluctuation theorem
    • M. Criado-Sancho, J. Casas-Vazquez, and D. Jou Non-equilibrium thermodynamic potential and flux fluctuation theorem Phys. Lett. A 373 2009 3301 3303
    • (2009) Phys. Lett. A , vol.373 , pp. 3301-3303
    • Criado-Sancho, M.1    Casas-Vazquez, J.2    Jou, D.3
  • 81
    • 0025897469 scopus 로고
    • Reversed alamethicin conductance in lipid bilayers
    • R.J. Taylor, and R. Delevie Reversed alamethicin conductance in lipid bilayers Biophys. J. 59 1991 873 879
    • (1991) Biophys. J. , vol.59 , pp. 873-879
    • Taylor, R.J.1    Delevie, R.2
  • 83
    • 4344584311 scopus 로고    scopus 로고
    • Helical kink and channel behaviour: A comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin
    • H. Duclohier Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin Eur. Biophys. J. 33 2004 169 174 (Pubitemid 39118293)
    • (2004) European Biophysics Journal , vol.33 , Issue.3 , pp. 169-174
    • Duclohier, H.1


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