메뉴 건너뛰기




Volumn 32, Issue 3-4, 2006, Pages 193-201

Effects of mutations on the C-terminus of protegrin-1: A molecular dynamics simulation study

Author keywords

Antimicrobial peptides; DPC micelles; Molecular dynamics simulations; Protegrin; SDS micelles

Indexed keywords

BACTERIA; COMPUTER SIMULATION; MICELLES; MUTAGENESIS; PROTEINS; TOXICITY;

EID: 33746592900     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927020600612205     Document Type: Conference Paper
Times cited : (14)

References (53)
  • 1
    • 0346494748 scopus 로고    scopus 로고
    • ANTIMIC: A database of antimicrobial sequences
    • M. Brahmachary, et al. ANTIMIC: a database of antimicrobial sequences. Nucleic Acids Res., 32(Datebase issue), D586 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , Issue.DATEBASE ISSUE
    • Brahmachary, M.1
  • 2
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff. Antimicrobial peptides of multicellular organisms. Nature, 415(6870), 389 (2002).
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389
    • Zasloff, M.1
  • 3
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de novo designed diastereomeric cell-selective antimicrobial peptides
    • Y. Shai, Z. Oren. From "carpet" mechanism to de novo designed diastereomeric cell-selective antimicrobial peptides. Peptides, 22(10), 1629 (2001).
    • (2001) Peptides , vol.22 , Issue.10 , pp. 1629
    • Shai, Y.1    Oren, Z.2
  • 4
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • R.M. Epand, H.J. Vogel. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta, 1462(1/2), 11 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , Issue.1-2 , pp. 11
    • Epand, R.M.1    Vogel, H.J.2
  • 5
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • M. Dathe, et al. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett., 501(2/3), 146 (2001).
    • (2001) FEBS Lett. , vol.501 , Issue.2-3 , pp. 146
    • Dathe, M.1
  • 6
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • K.J. Hallock, D.K. Lee, A. Ramamoorthy. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain. Biophys. J., 84(5), 3052 (2003).
    • (2003) Biophys. J. , vol.84 , Issue.5 , pp. 3052
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 7
    • 0037183527 scopus 로고    scopus 로고
    • Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity
    • T. Tachi, et al. Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry, 41(34), 10723 (2002).
    • (2002) Biochemistry , vol.41 , Issue.34 , pp. 10723
    • Tachi, T.1
  • 8
    • 0037083922 scopus 로고    scopus 로고
    • Translocation of protegrin i through phospholipid membranes: Role of peptide folding
    • G. Drin, J. Temsamani. Translocation of protegrin I through phospholipid membranes: role of peptide folding. Biochim. Biophys. Acta, 1559(2), 160 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1559 , Issue.2 , pp. 160
    • Drin, G.1    Temsamani, J.2
  • 9
    • 0027169823 scopus 로고
    • Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • V.N. Kokryakov, et al. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett., 327(2), 231 (1993).
    • (1993) FEBS Lett. , vol.327 , Issue.2 , pp. 231
    • Kokryakov, V.N.1
  • 10
    • 0029964525 scopus 로고    scopus 로고
    • Susceptibility of Neisseria gonorrhoeas to protegrins
    • X.D. Qu, et al. Susceptibility of Neisseria gonorrhoeas to protegrins. Infect. Immun., 64(4), 1240 (1996).
    • (1996) Infect. Immun. , vol.64 , Issue.4 , pp. 1240
    • Qu, X.D.1
  • 11
    • 0031034573 scopus 로고    scopus 로고
    • Protegrin structure and activity against Neisseria gonorrhoeas
    • X.D. Qu, et al. Protegrin structure and activity against Neisseria gonorrhoeas. Infect. Immun., 65(2), 636 (1997).
    • (1997) Infect. Immun. , vol.65 , Issue.2 , pp. 636
    • Qu, X.D.1
  • 12
    • 0032497922 scopus 로고    scopus 로고
    • Multiple states of beta-sheet peptide protegrin in lipid bilayers
    • W.T. Heller, et al. Multiple states of beta-sheet peptide protegrin in lipid bilayers. Biochemistry, 37(49), 17331 (1998).
    • (1998) Biochemistry , vol.37 , Issue.49 , pp. 17331
    • Heller, W.T.1
  • 13
    • 0034635136 scopus 로고    scopus 로고
    • Membrane thinning effect of the beta-sheet antimicrobial protegrin
    • W.T. Heller, et al Membrane thinning effect of the beta-sheet antimicrobial protegrin. Biochemistry, 39(1), 139 (2000).
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 139
    • Heller, W.T.1
  • 14
    • 0032445402 scopus 로고    scopus 로고
    • Dodecylphosphocholine micelles as a membrane-like environment: New results from NMR relaxation and paramagnetic relaxation enhancement analysis
    • V. Beswick, et al. Dodecylphosphocholine micelles as a membrane-like environment: new results from NMR relaxation and paramagnetic relaxation enhancement analysis. Eur. Biophys. J., 28(1), 48 (1999).
    • (1999) Eur. Biophys. J. , vol.28 , Issue.1 , pp. 48
    • Beswick, V.1
  • 15
    • 0029381531 scopus 로고
    • The use of dodecylphosphocholine micelles in solution NMR
    • D.A. Kallick, et al. The use of dodecylphosphocholine micelles in solution NMR. J. Magn. Reson. B, 109(1), 60 (1995).
    • (1995) J. Magn. Reson. B , vol.109 , Issue.1 , pp. 60
    • Kallick, D.A.1
  • 16
    • 0034655496 scopus 로고    scopus 로고
    • An NMR study of conformations of substituted dipeptides in dodecylphosphocholine micelles: Implications for drug transport
    • D.A. Kloosterman, et at. An NMR study of conformations of substituted dipeptides in dodecylphosphocholine micelles: implications for drug transport. Biopolymers, 53(5), 396 (2000).
    • (2000) Biopolymers , vol.53 , Issue.5 , pp. 396
    • Kloosterman, D.A.1
  • 17
    • 0018798032 scopus 로고
    • Physicochemical studies of the protein-lipid interactions in melittin-containing micelles
    • J. Lauterwein, el al Physicochemical studies of the protein-lipid interactions in melittin-containing micelles. Biochim. Biophys. Acta, 556(2), 244 (1979).
    • (1979) Biochim. Biophys. Acta , vol.556 , Issue.2 , pp. 244
    • Lauterwein, J.1
  • 18
    • 27844534774 scopus 로고    scopus 로고
    • Simulation studies of the interactions between membrane proteins and detergents
    • P.J. Bond, J. Cuthbertson, M.S. Sansom. Simulation studies of the interactions between membrane proteins and detergents. Biochem. Soc. Trans., 33(Pt 5), 910 (2005).
    • (2005) Biochem. Soc. Trans. , vol.33 , Issue.5 PART , pp. 910
    • Bond, P.J.1    Cuthbertson, J.2    Sansom, M.S.3
  • 19
    • 10344247720 scopus 로고    scopus 로고
    • MD simulations of spontaneous membrane protein/detergent micelle formation
    • P.J. Bond, et al. MD simulations of spontaneous membrane protein/detergent micelle formation. J. Am. Chem. Soc., 126(49), 15948 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.49 , pp. 15948
    • Bond, P.J.1
  • 20
    • 0037129516 scopus 로고    scopus 로고
    • Molecular dynamics simulation of sodium dodecyl sulfate micelle in water: Micellar structural characteristics and counterion distribution
    • C.D.B. Bruce, L. Max, L. Perera, M.D.E. Forbes. Molecular dynamics simulation of sodium dodecyl sulfate micelle in water: micellar structural characteristics and counterion distribution. J. Phys. Chem. B, 106(15), 3788 (2002).
    • (2002) J. Phys. Chem. B , vol.106 , Issue.15 , pp. 3788
    • Bruce, C.D.B.1    Max, L.2    Perera, L.3    Forbes, M.D.E.4
  • 21
    • 0347963579 scopus 로고
    • Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution: Decreased fluidity of the micelle hydrocarbon interior
    • A.D. MacKerell. Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution: decreased fluidity of the micelle hydrocarbon interior. J. Phys. Chem., 99, 327 (1995).
    • (1995) J. Phys. Chem. , vol.99 , pp. 327
    • MacKerell, A.D.1
  • 22
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • A. Rozek, C.L. Friedrich, R.E. Hancock. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry, 39(51), 15765 (2000).
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 15765
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.3
  • 23
    • 0033543147 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the structure and dynamics of a dodecylphosphocholine micelle in aqueous solution
    • T. Wymore, X.F. Gao, T.C. Wong. Molecular dynamics simulation of the structure and dynamics of a dodecylphosphocholine micelle in aqueous solution. J. Mol. Struct., 485, 195 (1999).
    • J. Mol. Struct. , vol.485 , Issue.195 , pp. 1999
    • Wymore, T.1    Gao, X.F.2    Wong, T.C.3
  • 24
    • 0033047067 scopus 로고    scopus 로고
    • Molecular dynamics study of substance P peptides partitioned in a sodium dodecylsulfate micelle
    • T. Wymore, T.C. Wong. Molecular dynamics study of substance P peptides partitioned in a sodium dodecylsulfate micelle. Biophys. J., 76(3), 1213 (1999).
    • (1999) Biophys. J. , vol.76 , Issue.3 , pp. 1213
    • Wymore, T.1    Wong, T.C.2
  • 25
    • 0037197683 scopus 로고    scopus 로고
    • Molecular dynamics simulations of mixed micelles modeling human bile
    • S. J. Marrink, A.E. Mark. Molecular dynamics simulations of mixed micelles modeling human bile. Biochemistry, 41(17), 5375 (2002).
    • (2002) Biochemistry , vol.41 , Issue.17 , pp. 5375
    • Marrink, S.J.1    Mark, A.E.2
  • 26
    • 0024960156 scopus 로고
    • Molecular dynamics simulation of a phospholipid micelle
    • J.J. Wendoloski, et al. Molecular dynamics simulation of a phospholipid micelle. Science, 243(4891), 636 (1989).
    • (1989) Science , vol.243 , Issue.4891 , pp. 636
    • Wendoloski, J.J.1
  • 27
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • M.R. Yeaman, N.Y. Yount. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev., 55(1), 27 (2003).
    • (2003) Pharmacol. Rev. , vol.55 , Issue.1 , pp. 27
    • Yeaman, M.R.1    Yount, N.Y.2
  • 28
    • 1542474068 scopus 로고    scopus 로고
    • Effects of two glycine residues in positions 13 and 17 of pleurocidin on structure and bacterial cell selectivity
    • S.S. Lim, et al. Effects of two glycine residues in positions 13 and 17 of pleurocidin on structure and bacterial cell selectivity. Protein Pept. Lett., 11(1), 35 (2004).
    • (2004) Protein Pept. Lett. , vol.11 , Issue.1 , pp. 35
    • Lim, S.S.1
  • 29
    • 18344377528 scopus 로고    scopus 로고
    • Interactions of the antimicrobial peptide Ac-FRWWHR-NH(2) with model membrane systems and bacterial cells
    • A.J. Rezansoff, et al. Interactions of the antimicrobial peptide Ac-FRWWHR-NH(2) with model membrane systems and bacterial cells. J. Pept. Res., 65(5), 491 (2005).
    • (2005) J. Pept. Res. , vol.65 , Issue.5 , pp. 491
    • Rezansoff, A.J.1
  • 30
    • 0036389644 scopus 로고    scopus 로고
    • Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide
    • S.T. Yang, et al. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. Biochem. Biophys. Res. Commun., 296(5), 1044 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , Issue.5 , pp. 1044
    • Yang, S.T.1
  • 31
    • 0030067073 scopus 로고    scopus 로고
    • Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulfate
    • H.W. van den Hooven, et al. Surface location and orientation of the lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulfate. Eur. J, Biochem., 235(1/2), 394 (1996).
    • (1996) Eur. J, Biochem. , vol.235 , Issue.1-2 , pp. 394
    • Van Den Hooven, H.W.1
  • 32
    • 0037443086 scopus 로고    scopus 로고
    • Interactions of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: Molecular dynamics simulations
    • C.M. Shepherd, H.J. Vogel, D.P. Tieleman. Interactions of the designed antimicrobial peptide MB21 and truncated dermaseptin S3 with lipid bilayers: molecular dynamics simulations. Biochem. J., 370, 233 (2003).
    • (2003) Biochem. J. , vol.370 , pp. 233
    • Shepherd, C.M.1    Vogel, H.J.2    Tieleman, D.P.3
  • 33
    • 7644222023 scopus 로고    scopus 로고
    • Binding and insertion of alphahelical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations
    • S.K. Kandasamy, R.G. Larson. Binding and insertion of alphahelical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations. Chem. Phys. Lipids, 132(1), 113 (2004).
    • (2004) Chem. Phys. Lipids , vol.132 , Issue.1 , pp. 113
    • Kandasamy, S.K.1    Larson, R.G.2
  • 34
    • 0034775147 scopus 로고    scopus 로고
    • Congeners of SMAP29 kill ovine pathogens and induce ultrastructural damage in bacterial cells
    • V.C. Kalfa, et al. Congeners of SMAP29 kill ovine pathogens and induce ultrastructural damage in bacterial cells. Antimicrob. Agents Chemother., 45(11), 3256 (2001).
    • (2001) Antimicrob. Agents Chemother. , vol.45 , Issue.11 , pp. 3256
    • Kalfa, V.C.1
  • 35
    • 0242488921 scopus 로고    scopus 로고
    • NMR solution structure determination of membrane proteins reconstituted in detergent micelles
    • C. Fernandez, K. Wuthrich. NMR solution structure determination of membrane proteins reconstituted in detergent micelles. FEBS Lett., 555(1), 144 (2003).
    • (2003) FEBS Lett. , vol.555 , Issue.1 , pp. 144
    • Fernandez, C.1    Wuthrich, K.2
  • 36
    • 1542335771 scopus 로고    scopus 로고
    • Molecular dynamics simulations of ionic interactions with dodecyl sulfate micelles
    • A.R. Rakitin, G.R. Pack. Molecular dynamics simulations of ionic interactions with dodecyl sulfate micelles. J. Phys. Chem. B, 108, 2712 (2004).
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2712
    • Rakitin, A.R.1    Pack, G.R.2
  • 37
    • 0036675379 scopus 로고    scopus 로고
    • Molecular dynamics simulations of adrenocorticotropin (1-24) peptide in a solvated dodecylpho-sphocholine (DPC) micelle and in a dimyistoylphosphatidylcholine (DMPC) bilayer
    • T.C. Wong, S. Kamath. Molecular dynamics simulations of adrenocorticotropin (1-24) peptide in a solvated dodecylpho-sphocholine (DPC) micelle and in a dimyistoylphosphatidylcholine (DMPC) bilayer. J. Biomol. Struct. Dyn., 20(1), 39 (2002).
    • (2002) J. Biomol. Struct. Dyn. , vol.20 , Issue.1 , pp. 39
    • Wong, T.C.1    Kamath, S.2
  • 38
    • 0034229640 scopus 로고    scopus 로고
    • Molecular dynamics simulations of dodecylphosphocholine micelles at three different aggregate sizes: Micellar structure and lipid chain relaxation
    • D.P. Tieleman, D. van der Spoel, H.J.C. Berendsen. Molecular dynamics simulations of dodecylphosphocholine micelles at three different aggregate sizes: micellar structure and lipid chain relaxation. J. Phys. Chem. B, 104, 6380 (2000).
    • J. Phys. Chem. B , vol.104 , Issue.6380 , pp. 2000
    • Tieleman, D.P.1    Van Der Spoel, D.2    Berendsen, H.J.C.3
  • 39
    • 0032738066 scopus 로고    scopus 로고
    • Simulation studies of the interaction of antimicrobial peptides and lipid bilayers
    • P. La Rocca, et al. Simulation studies of the interaction of antimicrobial peptides and lipid bilayers. Biochim. Biophys. Acta, 1462(1/2), 185 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1462 , Issue.1-2 , pp. 185
    • La Rocca, P.1
  • 40
    • 33645751940 scopus 로고    scopus 로고
    • How can a β-sheet peptide be both a potent antimicrobial and harmfully toxic? Molecular dynamics simulations of protegrin-1 in micelles
    • 101002/bip.20397
    • A. Langham, H. Khandelia, Y.N. Kaznessis. How can a β-sheet peptide be both a potent antimicrobial and harmfully toxic? Molecular dynamics simulations of protegrin-1 in micelles. J. Pept. Sci., (2005) 101002/bip.20397.
    • (2005) J. Pept. Sci.
    • Langham, A.1    Khandelia, H.2    Kaznessis, Y.N.3
  • 41
    • 0035017426 scopus 로고    scopus 로고
    • Molecular dynamics simulation of adrenocorticotropin (1-10) peptide in a solvated dodecylphosphocholine micelle
    • X. Gao, T.C. Wong. Molecular dynamics simulation of adrenocorticotropin (1-10) peptide in a solvated dodecylphosphocholine micelle. Biopolymers, 58(7), 643 (2001).
    • (2001) Biopolymers , vol.58 , Issue.7 , pp. 643
    • Gao, X.1    Wong, T.C.2
  • 42
    • 0037465469 scopus 로고    scopus 로고
    • Global structure and dynamics of human apolipoprotein CII in complex with micelles: Evidence for increased mobility of the helix involved in the activation of lipoprotein lipase
    • J. Zdunek, et al. Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase. Biochemistry, 42(7), 1872 (2003).
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 1872
    • Zdunek, J.1
  • 43
    • 33746646076 scopus 로고    scopus 로고
    • Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: What do point mutations achieve?
    • in press
    • H. Khandelia, Y.N. Kaznessis. Molecular dynamics simulations of helical antimicrobial peptides in SDS micelles: what do point mutations achieve? Peptides, (2006) in press.
    • (2006) Peptides
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 44
    • 22344445910 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the helical antimicrobial peptide Ovispirin-1 in a zwitterionic dodecylphosphocholine micelle: Insights into host-cell toxicity
    • H. Khandelia, Y.N. Kaznessis. Molecular dynamics simulations of the helical antimicrobial peptide Ovispirin-1 in a zwitterionic dodecylphosphocholine micelle: insights into host-cell toxicity. J. Phys. Chem. B, 109(26). 12990 (2005).
    • (2005) J. Phys. Chem. B , vol.109 , Issue.26 , pp. 12990
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 45
    • 17444420716 scopus 로고    scopus 로고
    • Simulation of the N-terminus of HIV-1 glycoprotein 41,000 fusion peptide in micelles
    • A. Langham, Y. Kaznessis. Simulation of the N-terminus of HIV-1 glycoprotein 41,000 fusion peptide in micelles. J. Pept. Sci., 11(4), 215 (2004).
    • (2004) J. Pept. Sci. , vol.11 , Issue.4 , pp. 215
    • Langham, A.1    Kaznessis, Y.2
  • 46
    • 33746651219 scopus 로고    scopus 로고
    • Driving engineering of novel antimicrobial peptides from simulations of peptide-micelle interactions
    • in press
    • H. Khandelia, A.A. Langham, Y.N. Kaznessis. Driving Engineering of Novel Antimicrobial Peptides from Simulations of Peptide-Micelle Interactions. Biochim. Biophys. Acta. Biomembranes, (2006) in press.
    • (2006) Biochim. Biophys. Acta. Biomembranes
    • Khandelia, H.1    Langham, A.A.2    Kaznessis, Y.N.3
  • 47
    • 0038724257 scopus 로고    scopus 로고
    • Membrane protein dynamics versus environment: Simulations of OmpA in a micelle and in a bilayer
    • P.J. Bond, M.S. Sansom. Membrane protein dynamics versus environment: simulations of OmpA in a micelle and in a bilayer. J. Mol. Biol, 329(5), 1035 (2003).
    • (2003) J. Mol. Biol , vol.329 , Issue.5 , pp. 1035
    • Bond, P.J.1    Sansom, M.S.2
  • 48
    • 28144436374 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the influenza hemagglutinin fusion peptide in micelles and bilayers: Conformational analysis of peptide and lipids
    • P. Lague, B. Roux, R.W. Pastor. Molecular dynamics simulations of the influenza hemagglutinin fusion peptide in micelles and bilayers: conformational analysis of peptide and lipids. J. Mol. Biol., 354(5), 1129 (2005).
    • (2005) J. Mol. Biol. , vol.354 , Issue.5 , pp. 1129
    • Lague, P.1    Roux, B.2    Pastor, R.W.3
  • 49
    • 1842611408 scopus 로고    scopus 로고
    • Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy
    • L.M. Gordon, et al. Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy. Prottein Sci, 13(4), 1012 (2004).
    • (2004) Prottein Sci , vol.13 , Issue.4 , pp. 1012
    • Gordon, L.M.1
  • 50
    • 11144242839 scopus 로고    scopus 로고
    • Protegrin structure-activity relationships: Using homology models of synthetic sequences to determine structural characteristics important for activity
    • N. Ostberg, Y. Kaznessis. Protegrin structure-activity relationships: using homology models of synthetic sequences to determine structural characteristics important for activity. Peptides, 26(2), 297 (2005).
    • (2005) Peptides , vol.26 , Issue.2 , pp. 297
    • Ostberg, N.1    Kaznessis, Y.2
  • 51
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen, et al. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys., 79(2), 926 (1983).
    • (1983) J. Chem. Phys. , vol.79 , Issue.2 , pp. 926
    • Jorgensen, W.L.1
  • 52
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy, minimization, and dynamics simulations
    • B.R. Brooks, et al. CHARMM: A program for macromolecular energy, minimization, and dynamics simulations. J. Comp. Chem., 4, 187(1983).
    • (1983) J. Comp. Chem. , vol.4 , pp. 187
    • Brooks, B.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.