메뉴 건너뛰기




Volumn 46, Issue 11, 2007, Pages 3576-3585

Solution structure and interaction of Cupiennin 1a, a spider venom peptide, with phospholipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBACTERIAL PEPTIDE; HELIX-HINGE-HELIX STRUCTURE; MEMBRANE BINDING; SPIDER VENOM PEPTIDE;

EID: 33947380145     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062306+     Document Type: Article
Times cited : (41)

References (79)
  • 1
    • 0030974953 scopus 로고    scopus 로고
    • Ribosomally synthesized antimicrobial peptides: Their function, structure, biogenesis, and mechanism of action
    • Nissen-Meyer, J., and Nes, I. F. (1997) Ribosomally synthesized antimicrobial peptides: their function, structure, biogenesis, and mechanism of action, Arch. Microbiol. 167, 67-77.
    • (1997) Arch. Microbiol , vol.167 , pp. 67-77
    • Nissen-Meyer, J.1    Nes, I.F.2
  • 2
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. (1995) Peptide antibiotics and their role in innate immunity, Annu. Rev. Immunol. 13, 91-92.
    • (1995) Annu. Rev. Immunol , vol.13 , pp. 91-92
    • Boman, H.G.1
  • 3
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: Defensins, cathelicidins and histatins
    • Smet, K., and Contreras, R. (2005) Human antimicrobial peptides: Defensins, cathelicidins and histatins, Biotechnol. Lett. 27, 1337-1347.
    • (2005) Biotechnol. Lett , vol.27 , pp. 1337-1347
    • Smet, K.1    Contreras, R.2
  • 4
    • 0032741453 scopus 로고    scopus 로고
    • Antibiotic resistance in microbes
    • Mazel, D., and Davies, J. (1999) Antibiotic resistance in microbes, Cell. Mol. Life Sci. 56, 742-754.
    • (1999) Cell. Mol. Life Sci , vol.56 , pp. 742-754
    • Mazel, D.1    Davies, J.2
  • 5
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming peptides-magainins, cecropins, melittin and alamethicin
    • Bechinger, B. (1997) Structure and functions of channel-forming peptides-magainins, cecropins, melittin and alamethicin, J. Membr. Biol. 156, 197-211.
    • (1997) J. Membr. Biol , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 6
    • 0029146071 scopus 로고
    • Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides
    • Epand, R. M., Shai, Y. C., Segrest, J. P., and Anantharamaiah, G. M. (1995) Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides, Biopolymers 37, 319-338.
    • (1995) Biopolymers , vol.37 , pp. 319-338
    • Epand, R.M.1    Shai, Y.C.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 7
    • 0032930291 scopus 로고    scopus 로고
    • Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide-containing liposomes as a model for outer membranes of Gram-negative bacteria
    • Matsuzaki, K., Sugishita, K., and Miyajima, K. (1999) Interactions of an antimicrobial peptide, magainin 2, with lipopolysaccharide-containing liposomes as a model for outer membranes of Gram-negative bacteria, FEBS Lett. 449, 221-224.
    • (1999) FEBS Lett , vol.449 , pp. 221-224
    • Matsuzaki, K.1    Sugishita, K.2    Miyajima, K.3
  • 8
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic α-helical antimicrobial peptides
    • Oren, Z., and Shai, Y. (1998) Mode of action of linear amphipathic α-helical antimicrobial peptides, Biopolymers 47, 451-463.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 9
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • Tossi, A., Sandri, L., and Giangaspero, A. (2000) Amphipathic, α-helical antimicrobial peptides, Biopolymers 55, 4-30.
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 10
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G., and Lecar, H. (1977) Electrically gated ionic channels in lipid bilayers, Q. Rev. Biophys. 10, 1-34.
    • (1977) Q. Rev. Biophys , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 11
    • 0025935264 scopus 로고
    • The biophysics of peptide models of ion channels
    • Sansom, M. S. P. (1991) The biophysics of peptide models of ion channels, Prog. Biophys. Mol. Biol. 55, 139-235.
    • (1991) Prog. Biophys. Mol. Biol , vol.55 , pp. 139-235
    • Sansom, M.S.P.1
  • 12
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides, Biochim. Biophys. Acta 1462, 55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 13
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as arche-types
    • Matsuzaki, K. (1999) Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as arche-types, Biochim. Biophys. Acta 1462, 1-10.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 14
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to denovo designed diastereomeric cell-selective antimicrobial peptides
    • Shai, Y., and Oren, Z. (2001) From "carpet" mechanism to denovo designed diastereomeric cell-selective antimicrobial peptides, Peptides 22, 1629-1641.
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 15
    • 0347991711 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic peptides of venomous arthropods
    • Kuhn-Nentwig, L. (2003) Antimicrobial and cytolytic peptides of venomous arthropods, Cell. Mol. Life Sci. 60, 2651-2668.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 2651-2668
    • Kuhn-Nentwig, L.1
  • 16
    • 0022497150 scopus 로고
    • Interactions between membranes and cytolytic peptides
    • Bernheimer, A. W., and Rudy, B. (1985) Interactions between membranes and cytolytic peptides, Biochim. Biophys. Acta 864, 123-141.
    • (1985) Biochim. Biophys. Acta , vol.864 , pp. 123-141
    • Bernheimer, A.W.1    Rudy, B.2
  • 17
    • 0001075714 scopus 로고    scopus 로고
    • A novel class of pore-forming peptides in the venom of Parabuthus schlechteri Percell (Scorpions: Buthidae)
    • Verdonk, F., Bosteels, S., Desmet, J., Moerman, L., Noppe, W., Willems, J., Tytgat, J., and van der Walt, J. (2000) A novel class of pore-forming peptides in the venom of Parabuthus schlechteri Percell (Scorpions: Buthidae), Cimbebasia 16, 247-260.
    • (2000) Cimbebasia , vol.16 , pp. 247-260
    • Verdonk, F.1    Bosteels, S.2    Desmet, J.3    Moerman, L.4    Noppe, W.5    Willems, J.6    Tytgat, J.7    van der Walt, J.8
  • 18
    • 18344373480 scopus 로고    scopus 로고
    • Scorpion venom peptides without disulfide bridges
    • Zeng, X., Corzo, G., and Hahin, R. (2005) Scorpion venom peptides without disulfide bridges, IUBMB Life 57, 13-21.
    • (2005) IUBMB Life , vol.57 , pp. 13-21
    • Zeng, X.1    Corzo, G.2    Hahin, R.3
  • 19
    • 1942534998 scopus 로고    scopus 로고
    • Biochemistry, toxicology and ecology of the venom of the spider Cupiennius salei (Ctenidae)
    • Kuhn-Nentwig, L., Schaller, J., and Nentwig, W. (2004) Biochemistry, toxicology and ecology of the venom of the spider Cupiennius salei (Ctenidae), Toxicon 43, 543-553.
    • (2004) Toxicon , vol.43 , pp. 543-553
    • Kuhn-Nentwig, L.1    Schaller, J.2    Nentwig, W.3
  • 20
    • 0037063310 scopus 로고    scopus 로고
    • Cupiennin 1d*: The cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus
    • Kuhn-Nentwig, L., Dathe, M., Walz, A., Schaller, J., and Nentwig, W. (2002) Cupiennin 1d*: The cytolytic activity depends on the hydrophobic N-terminus and is modulated by the polar C-terminus, FEBS Lett. 527, 193-198.
    • (2002) FEBS Lett , vol.527 , pp. 193-198
    • Kuhn-Nentwig, L.1    Dathe, M.2    Walz, A.3    Schaller, J.4    Nentwig, W.5
  • 21
    • 0037192798 scopus 로고    scopus 로고
    • Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae)
    • Kuhn-Nentwig, L., Müller, J., Schaller, J., Walz, A., Dathe, M., and Nentwig, W. (2002) Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae), J. Biol. Chem. 277, 11208-11216.
    • (2002) J. Biol. Chem , vol.277 , pp. 11208-11216
    • Kuhn-Nentwig, L.1    Müller, J.2    Schaller, J.3    Walz, A.4    Dathe, M.5    Nentwig, W.6
  • 22
    • 33947424175 scopus 로고    scopus 로고
    • Evans, J. N. S. (1995) Biomolecular NMR Spectroscopy, Oxford University Press, Oxford.
    • Evans, J. N. S. (1995) Biomolecular NMR Spectroscopy, Oxford University Press, Oxford.
  • 23
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints-the refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges, M., Macias, M. J., Odonoghue, S. I., and Oschkinat, H. (1997) Automated NOESY interpretation with ambiguous distance restraints-the refined NMR solution structure of the pleckstrin homology domain from β-spectrin, J. Mol. Biol. 269, 408-422.
    • (1997) J. Mol. Biol , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    Odonoghue, S.I.3    Oschkinat, H.4
  • 24
    • 0034535525 scopus 로고    scopus 로고
    • Structure determination of biological macromolecules in solution using nuclear magnetic resonance spectroscopy
    • Wider, G. (2000) Structure determination of biological macromolecules in solution using nuclear magnetic resonance spectroscopy, Biotechniques 29, 1278-1294.
    • (2000) Biotechniques , vol.29 , pp. 1278-1294
    • Wider, G.1
  • 25
    • 0020475314 scopus 로고
    • Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance
    • Wüthrich, K., and Wider, G. (1982) Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance, J. Mol. Biol. 155, 311-319.
    • (1982) J. Mol. Biol , vol.155 , pp. 311-319
    • Wüthrich, K.1    Wider, G.2
  • 26
    • 20444400818 scopus 로고    scopus 로고
    • Detergent-like properties of magainin antibiotic peptides: A 31P solid-state NMR spectroscopy study
    • Bechinger, B. (2005) Detergent-like properties of magainin antibiotic peptides: a 31P solid-state NMR spectroscopy study, Biochim. Biophys. Acta 1712, 101-108.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 101-108
    • Bechinger, B.1
  • 28
    • 23044450818 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer systems
    • Lu, J., Damodaran, K., Blazyk, J., and Lorigan, G. A. (2005) Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer systems, Biochemistry 44, 10208-10217.
    • (2005) Biochemistry , vol.44 , pp. 10208-10217
    • Lu, J.1    Damodaran, K.2    Blazyk, J.3    Lorigan, G.A.4
  • 29
    • 0031740077 scopus 로고    scopus 로고
    • Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes
    • Watts, A. (1998) Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes, Biochim. Biophys. Acta 1376, 297-318.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 297-318
    • Watts, A.1
  • 30
    • 0000510171 scopus 로고
    • Transverse nuclear spin relaxation in phospholipid bilayer membranes
    • Bloom, M., and Sternin, E. (1987) Transverse nuclear spin relaxation in phospholipid bilayer membranes, Biochemistry 26, 2101-2105.
    • (1987) Biochemistry , vol.26 , pp. 2101-2105
    • Bloom, M.1    Sternin, E.2
  • 32
    • 0031081881 scopus 로고    scopus 로고
    • 31P NMR: The effects of a peripheral protein on collective lipid fluctuations
    • 31P NMR: The effects of a peripheral protein on collective lipid fluctuations, Solid State NMR 8, 55-64.
    • (1997) Solid State NMR , vol.8 , pp. 55-64
    • Pinheiro, T.J.T.1    Duer, M.J.2    Watts, A.3
  • 33
    • 44049117096 scopus 로고
    • Effective combination of gradients and crafted RF pulses for water suppression in biological samples
    • John, B. K., Plant, D., Webb, P., and Hurd, R. E. (1992) Effective combination of gradients and crafted RF pulses for water suppression in biological samples, J. Magn. Reson. 98, 200-206.
    • (1992) J. Magn. Reson , vol.98 , pp. 200-206
    • John, B.K.1    Plant, D.2    Webb, P.3    Hurd, R.E.4
  • 36
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge, J. P., Habeck, M., Rieping, W., and Nilges, M. (2003) ARIA: Automated NOE assignment and NMR structure calculation, Bioinformatics 19, 315-316.
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 37
    • 0024279342 scopus 로고
    • Crystallosraphic refinement by simulated annealing-application to a 2.8 Å resolution structure of aspartate aminotransferase
    • Brünger, A. T. (1988) Crystallosraphic refinement by simulated annealing-application to a 2.8 Å resolution structure of aspartate aminotransferase, J. Mol. Biol. 203, 803-816.
    • (1988) J. Mol. Biol , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 38
    • 0031110495 scopus 로고    scopus 로고
    • Floating stereospecific assignment revisited-application to an 18 kDa protein and comparison with J-coupling data
    • Folmer, R. H. A., Hilbers, C. W., Konings, R. N. H., and Nilges, M. (1997) Floating stereospecific assignment revisited-application to an 18 kDa protein and comparison with J-coupling data, J. Biomol. NMR 9, 245-258.
    • (1997) J. Biomol. NMR , vol.9 , pp. 245-258
    • Folmer, R.H.A.1    Hilbers, C.W.2    Konings, R.N.H.3    Nilges, M.4
  • 39
    • 0037469137 scopus 로고    scopus 로고
    • Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium
    • Pari, K., Mueller, G. A., DeRose, E. F., Kirby, T. W., and London, R. E. (2003) Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium, Biochemistry 42, 639-650.
    • (2003) Biochemistry , vol.42 , pp. 639-650
    • Pari, K.1    Mueller, G.A.2    DeRose, E.F.3    Kirby, T.W.4    London, R.E.5
  • 40
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL-a program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL-a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 43
    • 0000745176 scopus 로고
    • Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis, J. H., Jeffrey, K. R., Bloom, M., Valic, M. I., and Higgs, T. P. (1976) Quadrupolar echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains, Chem. Phys. Lett. 42, 390-394.
    • (1976) Chem. Phys. Lett , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 44
    • 33947415536 scopus 로고    scopus 로고
    • Galassi, M., Davies, J., Theiler, J., Gough, B., Jungman, G., Booth, M., and F., R. GNU Scientific Library Reference Manual, revised 2nd ed. ISBN 0954161734, http://www.gnu.org.software/gsl/.
    • Galassi, M., Davies, J., Theiler, J., Gough, B., Jungman, G., Booth, M., and F., R. GNU Scientific Library Reference Manual, revised 2nd ed. ISBN 0954161734, http://www.gnu.org.software/gsl/.
  • 45
    • 0029181728 scopus 로고
    • H-1, C-13 and N-15 random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects
    • Wishart, D. S., Bigam, C. G., Holm, A., Hodges, R. S., and Sykes, B. D. (1995) H-1, C-13 and N-15 random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects, J. Biomol. NMR 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 46
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 47
    • 0001675109 scopus 로고
    • Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides
    • Zhou, N. E., Zhu, B., Sykes, B. D., and Hodges, R. S. (1992) Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides, J. Am. Chem. Soc. 114, 4320-4326.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 4320-4326
    • Zhou, N.E.1    Zhu, B.2    Sykes, B.D.3    Hodges, R.S.4
  • 48
    • 0017902280 scopus 로고
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes
    • 31P nuclear magnetic resonance and the head group structure of phospholipids in membranes, Biochim. Biophys. Acta 515, 105-140.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 105-140
    • Seelig, J.1
  • 49
    • 0017580849 scopus 로고
    • 31P nuclear magnetic resonance chemical shielding tensors
    • 31P nuclear magnetic resonance chemical shielding tensors, Biochemistry 16, 519-526.
    • (1977) Biochemistry , vol.16 , pp. 519-526
    • Kohler, S.J.1    Klein, M.P.2
  • 50
    • 0018982584 scopus 로고
    • Lipid conformation in model membranes and biological membranes
    • Seelig, J., and Seelig, A. (1980) Lipid conformation in model membranes and biological membranes, Q. Rev. Biophys. 13, 19-61.
    • (1980) Q. Rev. Biophys , vol.13 , pp. 19-61
    • Seelig, J.1    Seelig, A.2
  • 51
    • 0033646558 scopus 로고    scopus 로고
    • Biophysical investigations of membrane perturbations by polypeptides using solid-state NMR spectroscopy (review)
    • Bechinger, B. (2000) Biophysical investigations of membrane perturbations by polypeptides using solid-state NMR spectroscopy (review), Mol. Membr. Biol. 17, 135-142.
    • (2000) Mol. Membr. Biol , vol.17 , pp. 135-142
    • Bechinger, B.1
  • 52
    • 0024974068 scopus 로고
    • Electric charge effects on phospholipid headgroups. Phosphatidylcholine in mixtures with cationic and anionic amphiphiles
    • Scherer, P. G., and Seelig, J. (1989) Electric charge effects on phospholipid headgroups. Phosphatidylcholine in mixtures with cationic and anionic amphiphiles, Biochemistry 28, 7720-7728.
    • (1989) Biochemistry , vol.28 , pp. 7720-7728
    • Scherer, P.G.1    Seelig, J.2
  • 53
    • 3342906298 scopus 로고    scopus 로고
    • Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes
    • Balla, M. S., Bowie, J. H., and Separovic, F. (2004) Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes, Eur. Biophys. J. 33, 109-116.
    • (2004) Eur. Biophys. J , vol.33 , pp. 109-116
    • Balla, M.S.1    Bowie, J.H.2    Separovic, F.3
  • 55
    • 0016283654 scopus 로고
    • The dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance
    • Seelig, A., and Seelig, J. (1974) The dynamic structure of fatty acyl chains in a phospholipid bilayer measured by deuterium magnetic resonance, Biochemistry 13, 4839-4845.
    • (1974) Biochemistry , vol.13 , pp. 4839-4845
    • Seelig, A.1    Seelig, J.2
  • 56
    • 0025973403 scopus 로고
    • On the use of deuterium nuclear magetic resonance as a probe of chain packing in lipid bilayers
    • Boden, N., Jones, S. A., and Sixl, F. (1991) On the use of deuterium nuclear magetic resonance as a probe of chain packing in lipid bilayers, Biochemistry 30, 2146-2155.
    • (1991) Biochemistry , vol.30 , pp. 2146-2155
    • Boden, N.1    Jones, S.A.2    Sixl, F.3
  • 59
    • 0034499164 scopus 로고    scopus 로고
    • Softening of membrane bilayers by detergents elucidated by deuterium NMR spectroscopy
    • Otten, D., Brown, M. F., and Beyer, K. (2000) Softening of membrane bilayers by detergents elucidated by deuterium NMR spectroscopy, J. Phys. Chem. 104, 12119-12129.
    • (2000) J. Phys. Chem , vol.104 , pp. 12119-12129
    • Otten, D.1    Brown, M.F.2    Beyer, K.3
  • 60
    • 0028861208 scopus 로고
    • Smoothed acyl chain orientational order parameter profiles in dimyristoylphosphatidylcholine- distearoylphosphatidylcholine mixtures: A 2H-NMR study
    • Lu, D., Vavasour, I., and Morrow, M. R. (1995) Smoothed acyl chain orientational order parameter profiles in dimyristoylphosphatidylcholine- distearoylphosphatidylcholine mixtures: a 2H-NMR study, Biophys. J. 68, 574-583.
    • (1995) Biophys. J , vol.68 , pp. 574-583
    • Lu, D.1    Vavasour, I.2    Morrow, M.R.3
  • 61
    • 26244434597 scopus 로고    scopus 로고
    • Probing segmental order in lipid bilayers at variable hydration levels by amplitude- and phase-modulated cross-polarization NMR
    • Dvinskikh, S. V., Castro, V., and Sandstrom, D. (2005) Probing segmental order in lipid bilayers at variable hydration levels by amplitude- and phase-modulated cross-polarization NMR, Phys. Chem. Chem. Phys. 7, 3255-3257.
    • (2005) Phys. Chem. Chem. Phys , vol.7 , pp. 3255-3257
    • Dvinskikh, S.V.1    Castro, V.2    Sandstrom, D.3
  • 62
    • 4043165350 scopus 로고
    • Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation
    • Andrew, E. G., Bradbury, A., and Eades, R. G. (1959) Removal of dipolar broadening of nuclear magnetic resonance spectra of solids by specimen rotation, Nature 183, 1802-1803.
    • (1959) Nature , vol.183 , pp. 1802-1803
    • Andrew, E.G.1    Bradbury, A.2    Eades, R.G.3
  • 63
    • 0006627015 scopus 로고    scopus 로고
    • Static and magic angle spinning NMR of membrane peptides and proteins
    • Davis, J. H., and Auger, M. (1999) Static and magic angle spinning NMR of membrane peptides and proteins, Prog. Nucl. Magn. Reson. Spectrosc. 35, 1-84.
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc , vol.35 , pp. 1-84
    • Davis, J.H.1    Auger, M.2
  • 66
    • 0029860833 scopus 로고    scopus 로고
    • A model for the interaction of trifluoroethanol with peptides and proteins
    • Rajan, R., and Balaram, P. (1996) A model for the interaction of trifluoroethanol with peptides and proteins, Int. J. Pept. Protein Res. 48, 328-336.
    • (1996) Int. J. Pept. Protein Res , vol.48 , pp. 328-336
    • Rajan, R.1    Balaram, P.2
  • 67
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced alpha-helix formation of melittin-implication for the mechanism of the alcohol effects on proteins
    • Hirota, N., Mizuno, K., and Goto, Y. (1998) Group additive contributions to the alcohol-induced alpha-helix formation of melittin-implication for the mechanism of the alcohol effects on proteins, J. Mol. Biol. 275, 365-378.
    • (1998) J. Mol. Biol , vol.275 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 68
    • 0027180807 scopus 로고
    • Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments
    • Rizo, J., Blanco, F. J., Kobe, B., Bruch, M. D., and Gierasch, L. M. (1993) Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments, Biochemistry 32, 4881-4894.
    • (1993) Biochemistry , vol.32 , pp. 4881-4894
    • Rizo, J.1    Blanco, F.J.2    Kobe, B.3    Bruch, M.D.4    Gierasch, L.M.5
  • 69
    • 0031062621 scopus 로고    scopus 로고
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution
    • 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution, J. Biomol. NMR 9, 127-135.
    • (1997) J. Biomol. NMR , vol.9 , pp. 127-135
    • Gesell, J.1    Zasloff, M.2    Opella, S.J.3
  • 70
    • 0025602520 scopus 로고
    • The influence of proline residues on α-helical structure
    • Woolfson, D. N., and Williams, D. H. (1990) The influence of proline residues on α-helical structure, FEBS Lett. 277, 185-188.
    • (1990) FEBS Lett , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 71
    • 0032488824 scopus 로고    scopus 로고
    • Stereochemical punctuation marks in protein structures: Glycine and proline containing helix stop signals
    • Gunasekaran, K., Nagarajam, H. A., Ramakrishnan, C., and Balaram, P. (1998) Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals, J. Mol. Biol. 275, 917-932.
    • (1998) J. Mol. Biol , vol.275 , pp. 917-932
    • Gunasekaran, K.1    Nagarajam, H.A.2    Ramakrishnan, C.3    Balaram, P.4
  • 72
    • 0021099797 scopus 로고
    • 31P nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine
    • Smith, R., Cornell, B. A., Keniry, M. A., and Separovic, F. (1983) 31P nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine, Biochim. Biophys. Acta 732, 492-498.
    • (1983) Biochim. Biophys. Acta , vol.732 , pp. 492-498
    • Smith, R.1    Cornell, B.A.2    Keniry, M.A.3    Separovic, F.4
  • 73
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • Yang, L., Harroun, T. A., Weiss, T. M., Dong, L., and Huang, H. W. (2001) Barrel-stave model or toroidal model? A case study on melittin pores, Biophys. J. 81, 1475-1485.
    • (2001) Biophys. J , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Dong, L.4    Huang, H.W.5
  • 74
    • 17844376024 scopus 로고    scopus 로고
    • NMR methods for studying membrane-active antimicrobial peptides
    • Strandberg, E., and Ulrich, A. S. (2004) NMR methods for studying membrane-active antimicrobial peptides, Concepts Magn. Reson. A 23, 89-120.
    • (2004) Concepts Magn. Reson. A , vol.23 , pp. 89-120
    • Strandberg, E.1    Ulrich, A.S.2
  • 75
    • 0034804339 scopus 로고    scopus 로고
    • Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy
    • Yamaguchi, S., Huster, D., Waring, A., Lehrer, R. I., Kearney, W., Tack, B. F., and Hong, M. (2001) Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy, Biophys. J. 81, 2203-2214.
    • (2001) Biophys. J , vol.81 , pp. 2203-2214
    • Yamaguchi, S.1    Huster, D.2    Waring, A.3    Lehrer, R.I.4    Kearney, W.5    Tack, B.F.6    Hong, M.7
  • 78
    • 0004003561 scopus 로고
    • 4th ed, Prentice Hall Inc, Englewood Cliffs
    • Brock, T. D. (1984) Biology of Microorganisms, 4th ed., Prentice Hall Inc., Englewood Cliffs.
    • (1984) Biology of Microorganisms
    • Brock, T.D.1
  • 79
    • 0021111152 scopus 로고
    • Membrane thickness and acyl chain length
    • Cornell, B. A., and Separovic, F. (1983) Membrane thickness and acyl chain length, Biochim. Biophys. Acta 733, 189-193.
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 189-193
    • Cornell, B.A.1    Separovic, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.