메뉴 건너뛰기




Volumn 89, Issue 6, 2005, Pages 3985-3996

Interfacial tryptophan residues: A role for the cation-π effect?

Author keywords

[No Author keywords available]

Indexed keywords

1 PALMITOYL 2 OLEOYLPHOSPHATIDYLETHANOLAMINE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; CARBONYL DERIVATIVE; GRAMICIDIN A; INDOLE; MEMBRANE PROTEIN; NITROGEN; PHOSPHATIDYLETHANOLAMINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 28444469286     PISSN: 00063495     EISSN: 00063495     Source Type: Journal    
DOI: 10.1529/biophysj.105.061804     Document Type: Article
Times cited : (101)

References (80)
  • 1
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane proteins
    • Schiffer, M., C.-H. Chang, and F. J. Stevens. 1992. The functions of tryptophan residues in membrane proteins. Protein Eng. 5:213-214.
    • (1992) Protein Eng. , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.-H.2    Stevens, F.J.3
  • 2
    • 0027499143 scopus 로고
    • Nonrandom distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena, C., K. A. Williams, C. M. Deber, and R. A. F. Reitmeier. 1993. Nonrandom distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol. 229:602-608.
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reitmeier, R.A.F.4
  • 3
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G. 1994. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:167-192.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 167-192
    • Von Heijne, G.1
  • 4
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and G. Heijne. 2000. How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25:429-434.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Heijne, G.2
  • 5
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R., and J. A. Killian. 2003. Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring. Mol. Membr. Biol. 20:271-284.
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 271-284
    • De Planque, M.R.1    Killian, J.A.2
  • 6
    • 0029103215 scopus 로고
    • Characterization and modeling of membrane proteins using sequence analysis
    • Reithmeier, R. A. 1995. Characterization and modeling of membrane proteins using sequence analysis. Curr. Opin. Struct. Biol. 5:491-500.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 491-500
    • Reithmeier, R.A.1
  • 7
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R. E., and S. H. White. 1989. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry. 28:3421-3437.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.E.1    White, S.H.2
  • 8
    • 2942750047 scopus 로고    scopus 로고
    • Simulations of a membrane-anchored peptide: Structure, dynamics, and influence on bilayer properties
    • Jensen, M. O., O. G. Mouritsen, and G. H. Peters. 2004. Simulations of a membrane-anchored peptide: structure, dynamics, and influence on bilayer properties. Biophys. J. 86:3556-3575.
    • (2004) Biophys. J. , vol.86 , pp. 3556-3575
    • Jensen, M.O.1    Mouritsen, O.G.2    Peters, G.H.3
  • 9
    • 0027170648 scopus 로고
    • Membrane partitioning: Distinguishing bilayer effects from the hydrophobic effect
    • Wimley, W. C., and S. H. White. 1993. Membrane partitioning: distinguishing bilayer effects from the hydrophobic effect. Biochemistry. 32:6307-6312.
    • (1993) Biochemistry , vol.32 , pp. 6307-6312
    • Wimley, W.C.1    White, S.H.2
  • 10
    • 0028790095 scopus 로고
    • Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: Parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids
    • Kachel, K., E. Asuncion-Punzalan, and E. London. 1995. Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids. Biochemistry. 34:15475-15479.
    • (1995) Biochemistry , vol.34 , pp. 15475-15479
    • Kachel, K.1    Asuncion-Punzalan, E.2    London, E.3
  • 11
    • 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
  • 12
    • 0030029091 scopus 로고    scopus 로고
    • Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
    • Killian, J. A., I. Salemink, M. R. de Planque, G. Lindblom, R. E. Koeppe II, and D. V. Greathouse. 1996. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry. 35:1037-1045.
    • (1996) Biochemistry , vol.35 , pp. 1037-1045
    • Killian, J.A.1    Salemink, I.2    De Planque, M.R.3    Lindblom, G.4    Koeppe II, R.E.5    Greathouse, D.V.6
  • 13
    • 0030835044 scopus 로고    scopus 로고
    • Influence of membrane-spanning alpha-helical peptides on the phase behavior of the dioleoylphosphatidylcholine/water system
    • Morein, S., E. Strandberg, J. A. Killian, S. Persson, G. Arvidson, R. E. Koeppe 2nd, and G. Lindblom. 1997. Influence of membrane-spanning alpha-helical peptides on the phase behavior of the dioleoylphosphatidylcholine/water system. Biophys. J. 73:3078-3088.
    • (1997) Biophys. J. , vol.73 , pp. 3078-3088
    • Morein, S.1    Strandberg, E.2    Killian, J.A.3    Persson, S.4    Arvidson, G.5    Koeppe II, R.E.6    Lindblom, G.7
  • 14
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W., W. C. Wimley, K. Gawrish, 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.1    Wimley, W.C.2    Gawrish, K.3    White, S.H.4
  • 15
    • 22344440794 scopus 로고    scopus 로고
    • Electrostatic contributions to indole-lipid interactions
    • Gaede, H. C., W.-M. Yau, and K. Gawrisch. 2005. Electrostatic contributions to indole-lipid interactions. J. Phys. Chem. B. 109:13014-13023.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 13014-13023
    • Gaede, H.C.1    Yau, W.-M.2    Gawrisch, K.3
  • 16
    • 0030033588 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A. 1996. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science. 271:163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 17
    • 0033544354 scopus 로고    scopus 로고
    • Cation-pi interactions in proteins: Can simple models provide an accurate description
    • Minoux, H., and C. Chipot. 1999. Cation-pi interactions in proteins: can simple models provide an accurate description. J. Am. Chem. Soc. 121:10366-10372.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10366-10372
    • Minoux, H.1    Chipot, C.2
  • 18
    • 0022450133 scopus 로고
    • Amino-aromatic interactions in proteins
    • Burley, S. K., and G. A. Petsko. 1986. Amino-aromatic interactions in proteins. FEBS Lett. 203:139-143.
    • (1986) FEBS Lett. , vol.203 , pp. 139-143
    • Burley, S.K.1    Petsko, G.A.2
  • 19
    • 4243468938 scopus 로고    scopus 로고
    • The cation-pi interaction
    • Ma, J. C., and D. A. Dougherty. 1997. The cation-pi interaction. Chem. Rev. 97:1303-1324.
    • (1997) Chem. Rev. , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 20
    • 0043167827 scopus 로고    scopus 로고
    • Molecular dynamics simulations of pentapeptides at interfaces: Salt bridge and cation-pi interactions
    • Aliste, M. P., J. L. MacCallum, and D. P. Tieleman. 2003. Molecular dynamics simulations of pentapeptides at interfaces: salt bridge and cation-pi interactions. Biochemistry. 42:8976-8987.
    • (2003) Biochemistry , vol.42 , pp. 8976-8987
    • Aliste, M.P.1    MacCallum, J.L.2    Tieleman, D.P.3
  • 21
    • 0032568609 scopus 로고    scopus 로고
    • Is polarization important in cation-pi interactions?
    • Cubero, E., F. J. Luque, and M. Orozco. 1998. Is polarization important in cation-pi interactions? Proc. Natl. Acad. Sci. USA. 95:5976-5980.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5976-5980
    • Cubero, E.1    Luque, F.J.2    Orozco, M.3
  • 23
    • 4143116650 scopus 로고    scopus 로고
    • Computational studies of membrane channels
    • Roux, B., and K. Schulten. 2004. Computational studies of membrane channels. Structure. 12:1343-1351.
    • (2004) Structure , vol.12 , pp. 1343-1351
    • Roux, B.1    Schulten, K.2
  • 24
    • 0036285985 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus, M. 2002. Molecular dynamics simulations of biomolecules. Acc. Chem. Res. 35:321-323.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 321-323
    • Karplus, M.1
  • 25
    • 0032738066 scopus 로고    scopus 로고
    • Simulation studies of the interaction of antimicrobial peptides and lipid bilayers
    • La Rocca, P., P. C. Biggin, D. P. Tieleman, and M. S. Sansom. 1999. Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. Biochim. Biophys. Acta. 1462:185-200.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 185-200
    • La Rocca, P.1    Biggin, P.C.2    Tieleman, D.P.3    Sansom, M.S.4
  • 26
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function-the hydrophobic matching hypothesis revisited
    • Jensen, M. O., and O. G. Mouritsen. 2004. Lipids do influence protein function-the hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta. 1666:205-226.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 29
    • 0028321565 scopus 로고
    • Molecular dynamics simulations of the gramicidin channel
    • Roux, B., and M. Karplus. 1994. Molecular dynamics simulations of the gramicidin channel. Annu. Rev. Biophys. Biomol. Struct. 23:731-761.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 731-761
    • Roux, B.1    Karplus, M.2
  • 31
    • 0037380854 scopus 로고    scopus 로고
    • Gramicidin a channel as a test ground for molecular dynamics force fields
    • Allen, T. W., T. Bastug, S. Kuyucak, and S. H. Chung. 2003. Gramicidin A channel as a test ground for molecular dynamics force fields. Biophys. J. 84:2159-2168.
    • (2003) Biophys. J. , vol.84 , pp. 2159-2168
    • Allen, T.W.1    Bastug, T.2    Kuyucak, S.3    Chung, S.H.4
  • 32
    • 4444351490 scopus 로고    scopus 로고
    • Empirical force fields for biological macromolecules: Overview and issues
    • Mackerell, A. D. Jr. 2004. Empirical force fields for biological macromolecules: overview and issues. J. Comput. Chem. 25:1584-1604.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1584-1604
    • Mackerell Jr., A.D.1
  • 33
    • 0008075262 scopus 로고    scopus 로고
    • Atomistic models and force fields
    • O. M. Becker, A. D. MacKerell, B. Roux, and M. Watanabe, editors. Marcel Dekker, New York
    • MacKerell, A. D. 2001. Atomistic models and force fields. In Computational Biochemistry and Biophysics. O. M. Becker, A. D. MacKerell, B. Roux, and M. Watanabe, editors. Marcel Dekker, New York. 7-38.
    • (2001) Computational Biochemistry and Biophysics , pp. 7-38
    • MacKerell, A.D.1
  • 34
    • 0007461231 scopus 로고    scopus 로고
    • Indoles at interfaces: Calculations of electrostatic effects with density functional and molecular dynamics methods
    • Woolf, T. B., A. Grossfield, and J. G. Pearson. 1999. Indoles at interfaces: calculations of electrostatic effects with density functional and molecular dynamics methods. Int. J. Quant. Chem. 75:197-206.
    • (1999) Int. J. Quant. Chem. , vol.75 , pp. 197-206
    • Woolf, T.B.1    Grossfield, A.2    Pearson, J.G.3
  • 35
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • MacKerell, A. D. Jr., N. Banavali, and N. Foloppe. 2000-2001. Development and current status of the CHARMM force field for nucleic acids. Biopolymers. 56:257-265.
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • MacKerell Jr., A.D.1    Banavali, N.2    Foloppe, N.3
  • 36
    • 0026471029 scopus 로고
    • Molecular determinants of channel function
    • Andersen, O. S., and R. E. Koeppe II. 1992. Molecular determinants of channel function. Physiol. Rev. 72:S89-S158.
    • (1992) Physiol. Rev. , vol.72
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 37
    • 0036280795 scopus 로고    scopus 로고
    • Computational studies of the gramicidin channel
    • Roux, B. 2002. Computational studies of the gramicidin channel. Acc. Chem. Res. 35:366-375.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 366-375
    • Roux, B.1
  • 39
    • 0033061633 scopus 로고    scopus 로고
    • Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex
    • Chiu, S.-W., S. Subramaniam, and E. Jakobsson. 1999. Simulation study of a gramicidin/lipid bilayer system in excess water and lipid. I. Structure of the molecular complex. Biophys. J. 76:1929-1938.
    • (1999) Biophys. J. , vol.76 , pp. 1929-1938
    • Chiu, S.-W.1    Subramaniam, S.2    Jakobsson, E.3
  • 40
    • 0042626159 scopus 로고    scopus 로고
    • Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data
    • Allen, T. W., O. S. Andersen, and B. Roux. 2003. Structure of gramicidin A in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data. J. Am. Chem. Soc. 125:9868-9877.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9868-9877
    • Allen, T.W.1    Andersen, O.S.2    Roux, B.3
  • 41
    • 0033638097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the gramicidin A- dimyristoylphosphatidylcholine system with an ion in the channel pore region
    • Tang, Y. Z., W. Z. Chen, and C. X. Wang. 2000. Molecular dynamics simulations of the gramicidin A-dimyristoylphosphatidylcholine system with an ion in the channel pore region. Eur. Biophys. J. 29:523-534.
    • (2000) Eur. Biophys. J. , vol.29 , pp. 523-534
    • Tang, Y.Z.1    Chen, W.Z.2    Wang, C.X.3
  • 42
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis, P. R., and B. deKruijff. 1979. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta. 559:399-420.
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    Dekruijff, B.2
  • 43
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner, S. M. 1985. Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl. Acad. Sci. USA. 82:3665-3669.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 44
    • 0022064483 scopus 로고
    • 11 lipid crystal phase transition: Hydrocarbon packing versus intrinsic curvature
    • 11 lipid crystal phase transition: hydrocarbon packing versus intrinsic curvature. J. Phys. [E]. 46:761-769.
    • (1985) J. Phys. [E] , vol.46 , pp. 761-769
    • Kirk, G.L.1    Gruner, S.M.2
  • 45
    • 0030992795 scopus 로고    scopus 로고
    • Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels
    • Lundbæk, J. A., A. M. Maer, and O. S. Andersen. 1997. Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels. Biochemistry. 36:5695-5701.
    • (1997) Biochemistry , vol.36 , pp. 5695-5701
    • Lundbæk, J.A.1    Maer, A.M.2    Andersen, O.S.3
  • 46
    • 0343434280 scopus 로고    scopus 로고
    • The effective size of lipid polare head groups and gramicidin channel function
    • Abstr.
    • Maer, A. M., L. L. Providence, and O. S. Andersen. 1997. The effective size of lipid polare head groups and gramicidin channel function. Biophys. J. 72:A191. (Abstr.)
    • (1997) Biophys. J. , vol.72
    • Maer, A.M.1    Providence, L.L.2    Andersen, O.S.3
  • 48
    • 4243997763 scopus 로고    scopus 로고
    • Grubmüller, H. 1996. Solvate 1.0. http://www.mpibpc.gwdg.de/ abteilungen/071/solvate/docu.html
    • (1996) Solvate 1.0
    • Grubmüller, H.1
  • 49
    • 0031895461 scopus 로고    scopus 로고
    • Energetics of inclusion-induced bilayer deformations
    • Nielsen, C., M. Goulian, and O. S. Andersen. 1998. Energetics of inclusion-induced bilayer deformations. Biophys. J. 74:1966-1983.
    • (1998) Biophys. J. , vol.74 , pp. 1966-1983
    • Nielsen, C.1    Goulian, M.2    Andersen, O.S.3
  • 51
    • 0002062192 scopus 로고    scopus 로고
    • An empirical potential energy function for phospholipids: Criteria for parameter optimization and applications
    • K. M. Merz and B. Roux, editors. Birkhäuser, Boston
    • Schlenkrich, M., J. Brickmann, A. MacKerell, and M. Karplus. 1996. An empirical potential energy function for phospholipids: criteria for parameter optimization and applications. In Biological Membranes: A Molecular Perspective from Computation and Experiment. K. M. Merz and B. Roux, editors. Birkhäuser, Boston. 31-81.
    • (1996) Biological Membranes: A Molecular Perspective from Computation and Experiment , pp. 31-81
    • Schlenkrich, M.1    Brickmann, J.2    MacKerell, A.3    Karplus, M.4
  • 52
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy for molecular simulations of phospholipids
    • Feller, S. E., and A. MacKerell. 2000. An improved empirical potential energy for molecular simulations of phospholipids. J. Phys. Chem. B. 104:7510-7515.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, A.2
  • 53
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 55
    • 0032534843 scopus 로고    scopus 로고
    • Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: Molecular dynamics simulations
    • Tieleman, D. P., L. R. Forrest, M. S. Sansom, and H. J. Berendsen. 1998. Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: molecular dynamics simulations. Biochemistry. 37:17554-17561.
    • (1998) Biochemistry , vol.37 , pp. 17554-17561
    • Tieleman, D.P.1    Forrest, L.R.2    Sansom, M.S.3    Berendsen, H.J.4
  • 56
    • 0001439971 scopus 로고    scopus 로고
    • Molecular dynamics potential of mean force calculations: A study of the toluene-ammonium pi-cation interactions
    • Chipot, C., B. Maigret, D. A. Pearlman, and P. A. Kollman. 1996. Molecular dynamics potential of mean force calculations: a study of the toluene-ammonium pi-cation interactions. J. Am. Chem. Soc. 118:2998-3005.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2998-3005
    • Chipot, C.1    Maigret, B.2    Pearlman, D.A.3    Kollman, P.A.4
  • 57
    • 0028020035 scopus 로고
    • Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer
    • Woolf, T. B., and B. Roux. 1994. Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer. Proc. Natl. Acad. Sci. USA. 91:11631-11635.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11631-11635
    • Woolf, T.B.1    Roux, B.2
  • 58
    • 0036109653 scopus 로고    scopus 로고
    • Water permeation through gramicidin A: Desformylation and the double helix: A molecular dynamics study
    • de Groot, B. L., D. P. Tieleman, P. Pohl, and H. Grubmuller. 2002. Water permeation through gramicidin A: desformylation and the double helix: a molecular dynamics study. Biophys. J. 82:2934-2942.
    • (2002) Biophys. J. , vol.82 , pp. 2934-2942
    • De Groot, B.L.1    Tieleman, D.P.2    Pohl, P.3    Grubmuller, H.4
  • 59
    • 0028352135 scopus 로고
    • Motionally restricted tryptophan environments at the peptide-lipid interface of gramicidin channels
    • Mukherjee, S., and A, Chattopadhyay. 1994. Motionally restricted tryptophan environments at the peptide-lipid interface of gramicidin channels. Biochemistry. 33:5089-5097.
    • (1994) Biochemistry , vol.33 , pp. 5089-5097
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 60
    • 0042642646 scopus 로고    scopus 로고
    • Combined experimental/theoretical refinement of indole ring geometry using deuterium magnetic resonance and ab initio calculations
    • Koeppe 2nd, R. E., H. Sun, P. C. van der Wel, E. M. Scherer, P. Pulay, and D. V. Greathouse. 2003. Combined experimental/theoretical refinement of indole ring geometry using deuterium magnetic resonance and ab initio calculations. J. Am. Chem. Soc. 125:12268-12276.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12268-12276
    • Koeppe II, R.E.1    Sun, H.2    Van Der Wel, P.C.3    Scherer, E.M.4    Pulay, P.5    Greathouse, D.V.6
  • 61
    • 0038338832 scopus 로고    scopus 로고
    • Determination of chemical shielding tensor of an indole carbon and application to tryptophan orientation of a membrane peptide
    • Separovic, F., J. Ashida, T. Woolf, R. Smith, and T. Terao. 1999. Determination of chemical shielding tensor of an indole carbon and application to tryptophan orientation of a membrane peptide. Chem. Phys. Lett. 303:493-498.
    • (1999) Chem. Phys. Lett. , vol.303 , pp. 493-498
    • Separovic, F.1    Ashida, J.2    Woolf, T.3    Smith, R.4    Terao, T.5
  • 62
    • 0028882402 scopus 로고
    • Tryptophan dynamics and structural refinement in a lipid bilayer environment: Solid state NMR of the gramicidin channels
    • Hu, W., N. D. Lazo, and T. A. Cross. 1995. Tryptophan dynamics and structural refinement in a lipid bilayer environment: solid state NMR of the gramicidin channels. Biochemistry. 34:14138-14146.
    • (1995) Biochemistry , vol.34 , pp. 14138-14146
    • Hu, W.1    Lazo, N.D.2    Cross, T.A.3
  • 63
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin a channel in a DMPC bilayer
    • Woolf, T. B., and B. Roux. 1996. Structure, energetics, and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins. 24:92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 64
    • 0028045061 scopus 로고
    • Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy
    • Koeppe II, R. E., J. A. Killian, and D. V. Greathouse. 1994. Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy. Biophys. J. 66:14-24.
    • (1994) Biophys. J. , vol.66 , pp. 14-24
    • Koeppe II, R.E.1    Killian, J.A.2    Greathouse, D.V.3
  • 65
    • 0035797933 scopus 로고    scopus 로고
    • Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles
    • Townsley, L. E., W. A. Tucker, S. Sham, and J. F. Hinton. 2001. Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. Biochemistry. 40:11676-11686.
    • (2001) Biochemistry , vol.40 , pp. 11676-11686
    • Townsley, L.E.1    Tucker, W.A.2    Sham, S.3    Hinton, J.F.4
  • 66
    • 0000346708 scopus 로고
    • Gramicidin a transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR spectroscopy and energy refinement
    • Arseniev, A. S., A. L. Lomize, I. L. Barsukov, and V. F. Bystrov. 1986. Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR spectroscopy and energy refinement. Biol. Membr. (USSR). 3:1077-1104.
    • (1986) Biol. Membr. (USSR) , vol.3 , pp. 1077-1104
    • Arseniev, A.S.1    Lomize, A.L.2    Barsukov, I.L.3    Bystrov, V.F.4
  • 67
    • 0031574382 scopus 로고    scopus 로고
    • High-resolution polypeptide structure in a lamellar phase lipid environment form solid state NMR derived orientational constraints
    • Ketchem, R. R., B. Roux, and T. A. Cross. 1997. High-resolution polypeptide structure in a lamellar phase lipid environment form solid state NMR derived orientational constraints. Structure. 5:1655-1669.
    • (1997) Structure , vol.5 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 68
  • 69
    • 0029991865 scopus 로고    scopus 로고
    • Conformation of the acylation site of palmitoylgramicidin in lipid bilayers of dimyristoylphosphatidylcholine
    • Koeppe 2nd, R. E., T. C. Vogt, D. V. Greathouse, J. A. Killian, and B. de Kruijff. 1996. Conformation of the acylation site of palmitoylgramicidin in lipid bilayers of dimyristoylphosphatidylcholine. Biochemistry. 35:3641-3648.
    • (1996) Biochemistry , vol.35 , pp. 3641-3648
    • Koeppe II, R.E.1    Vogt, T.C.2    Greathouse, D.V.3    Killian, J.A.4    De Kruijff, B.5
  • 70
    • 0041878923 scopus 로고    scopus 로고
    • Modeling induced polarization with classical Drude oscillators: Theory and molecular dynamics simulation
    • Lamoureux, G., and B. Roux. 2003. Modeling induced polarization with classical Drude oscillators: theory and molecular dynamics simulation. J. Chem. Phys. 119:3025-3039.
    • (2003) J. Chem. Phys. , vol.119 , pp. 3025-3039
    • Lamoureux, G.1    Roux, B.2
  • 71
    • 0141704114 scopus 로고    scopus 로고
    • A simple polarizable model of water based on classical Drude oscillators
    • Lamoureux, G., A. D. MacKerell, and B. Roux. 2003. A simple polarizable model of water based on classical Drude oscillators. J. Chem. Phys. 119:5185-5197.
    • (2003) J. Chem. Phys. , vol.119 , pp. 5185-5197
    • Lamoureux, G.1    MacKerell, A.D.2    Roux, B.3
  • 72
    • 0037039619 scopus 로고    scopus 로고
    • Interaction of tryptophan analogs with POPC lipid bilayers investigated by molecular dynamics calculations
    • Grossfield, A., and T. B. Woolf. 2002. Interaction of tryptophan analogs with POPC lipid bilayers investigated by molecular dynamics calculations. Langmuir. 18:198-210.
    • (2002) Langmuir , vol.18 , pp. 198-210
    • Grossfield, A.1    Woolf, T.B.2
  • 73
    • 0002940760 scopus 로고
    • Ionization and ion binding
    • G. Cevc, editor. Marcel Dekker, New York
    • Tatulian, S. A. 1993. Ionization and ion binding. In Phospholipids Handbook. G. Cevc, editor. Marcel Dekker, New York. 511-552.
    • (1993) Phospholipids Handbook , pp. 511-552
    • Tatulian, S.A.1
  • 75
    • 0037678992 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl
    • Pandit, S. A., D. Bostick, and M. L. Berkowitz. 2003. Molecular dynamics simulation of a dipalmitoylphosphatidylcholine bilayer with NaCl. Biophys. J. 84:3743-3750.
    • (2003) Biophys. J. , vol.84 , pp. 3743-3750
    • Pandit, S.A.1    Bostick, D.2    Berkowitz, M.L.3
  • 76
    • 0023018907 scopus 로고
    • Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime
    • Huang, H. W. 1986. Deformation free energy of bilayer membrane and its effect on gramicidin channel lifetime. Biophys. J. 50:1061-1070.
    • (1986) Biophys. J. , vol.50 , pp. 1061-1070
    • Huang, H.W.1
  • 77
    • 0001182731 scopus 로고    scopus 로고
    • Hydration, curvature, and bending elasticity of phospholipid monolayers
    • R. Epand, editor. Academic Press, San Diego
    • Rand, R. P., and V. A. Parsegian. 1997. Hydration, curvature, and bending elasticity of phospholipid monolayers. In Lipid Polymorphism and Membrane Properties. R. Epand, editor. Academic Press, San Diego. 167-189.
    • (1997) Lipid Polymorphism and Membrane Properties , pp. 167-189
    • Rand, R.P.1    Parsegian, V.A.2
  • 78
    • 0033737385 scopus 로고    scopus 로고
    • Inclusion-induced bilayer deformations: Effects of monolayer equilibrium curvature
    • Nielsen, C., and O. S. Andersen. 2000. Inclusion-induced bilayer deformations: effects of monolayer equilibrium curvature. Biophys. J. 79:2583-2604.
    • (2000) Biophys. J. , vol.79 , pp. 2583-2604
    • Nielsen, C.1    Andersen, O.S.2
  • 80
    • 0037881905 scopus 로고    scopus 로고
    • Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
    • de Planque, M. R., B. B. Bonev, J. A. Demmers, D. V. Greathouse, R. E. Koeppe 2nd, F. Separovic, A. Watts, and J. A. Killian. 2003. Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions. Biochemistry. 42:5341-5348.
    • (2003) Biochemistry , vol.42 , pp. 5341-5348
    • De Planque, M.R.1    Bonev, B.B.2    Demmers, J.A.3    Greathouse, D.V.4    Koeppe II, R.E.5    Separovic, F.6    Watts, A.7    Killian, J.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.