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Volumn 44, Issue 36, 2005, Pages 12120-12127

Topological equilibria of ion channel peptides in oriented lipid bilayers revealed by15N solid-state NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; MULTILAYERS; NUCLEAR MAGNETIC RESONANCE; PROTONS; TOPOLOGY;

EID: 24644445914     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050866n     Document Type: Article
Times cited : (15)

References (75)
  • 2
    • 0032884395 scopus 로고    scopus 로고
    • Structure and function of the bacterial mechanosensitive channel of large conductance
    • Oakley, A. J., Martinac, B., and Wilce, M. C. (1999) Structure and function of the bacterial mechanosensitive channel of large conductance, Protein Sci. 8, 1915-1921.
    • (1999) Protein Sci. , vol.8 , pp. 1915-1921
    • Oakley, A.J.1    Martinac, B.2    Wilce, M.C.3
  • 3
    • 0034986892 scopus 로고    scopus 로고
    • Structure of ligand-gated ion channels: Critical assessment of biochemical data supports novel topology
    • Leite, J. F., and Cascio, M. (2001) Structure of ligand-gated ion channels: critical assessment of biochemical data supports novel topology, Mol. Cell. Neurosci. 17, 777-792.
    • (2001) Mol. Cell. Neurosci. , vol.17 , pp. 777-792
    • Leite, J.F.1    Cascio, M.2
  • 4
    • 0033970888 scopus 로고    scopus 로고
    • Crystallographic analyses of ion channels: Lessons and challenges
    • Rees, D. C., Chang, G., and Spencer, R. H. (2000) Crystallographic analyses of ion channels: lessons and challenges, J. Biol. Chem. 275, 713-716.
    • (2000) J. Biol. Chem. , vol.275 , pp. 713-716
    • Rees, D.C.1    Chang, G.2    Spencer, R.H.3
  • 5
    • 0242405509 scopus 로고    scopus 로고
    • The structures of BtuCD and MscS and their implications for transporter and channel function
    • Bass, R. B., Locher, K. P., Borths, E., Poon, Y., Strop, P., Lee, A., and Rees, D. C. (2003) The structures of BtuCD and MscS and their implications for transporter and channel function, FEBS Lett. 555, 111-115.
    • (2003) FEBS Lett. , vol.555 , pp. 111-115
    • Bass, R.B.1    Locher, K.P.2    Borths, E.3    Poon, Y.4    Strop, P.5    Lee, A.6    Rees, D.C.7
  • 6
    • 2542466821 scopus 로고    scopus 로고
    • The structural basis of ClC chloride channel function
    • Dutzler, R. (2004) The structural basis of ClC chloride channel function, Trends Neurosci. 27, 315-320.
    • (2004) Trends Neurosci. , vol.27 , pp. 315-320
    • Dutzler, R.1
  • 7
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorensen, T. L., Moller, J. V., and Nissen, P. (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump, Science 304, 1672-1675.
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.1    Moller, J.V.2    Nissen, P.3
  • 8
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • Dempsey, C. E. (1990) The actions of melittin on membranes, Biochim. Biophys. Acta 1031, 143-161.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 9
    • 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
  • 10
    • 0026754487 scopus 로고
    • Model ion channels: Gramicidin and alamethicin
    • Woolley, G. A., and Wallace, B. A. (1992) Model ion channels: gramicidin and alamethicin, J. Membr. Biol. 129, 109-136.
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 11
    • 0030981655 scopus 로고    scopus 로고
    • Structure and functions of channel-forming polypeptides: Magainins, cecropins, melittin and alamethicin
    • Bechinger, B. (1997) Structure and functions of channel-forming polypeptides: magainins, cecropins, melittin and alamethicin, J. Membr. Biol. 156, 197-211.
    • (1997) J. Membr. Biol. , vol.156 , pp. 197-211
    • Bechinger, B.1
  • 12
    • 4344653004 scopus 로고    scopus 로고
    • Ion channels: From biophysics to disorders
    • Duclohier, H., and Pichon, Y. (2004) Ion channels: from biophysics to disorders, Eur. Biophys. J. 33, 167-168.
    • (2004) Eur. Biophys. J. , vol.33 , pp. 167-168
    • Duclohier, H.1    Pichon, Y.2
  • 13
    • 0024555637 scopus 로고
    • Structure and supramolecular architecture of membrane channel-forming peptides
    • Spach, G., Duclohier, H., Molle, G., and Valleton, J. M. (1989) Structure and supramolecular architecture of membrane channel-forming peptides, Biochimie 71, 11-21.
    • (1989) Biochimie , vol.71 , pp. 11-21
    • Spach, G.1    Duclohier, H.2    Molle, G.3    Valleton, J.M.4
  • 14
    • 0029100536 scopus 로고
    • Molecular mimicry in channel-protein structure
    • Montal, M. (1995) Molecular mimicry in channel-protein structure, Curr. Opin. Struct. Biol. 5, 501-506.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 501-506
    • Montal, M.1
  • 15
    • 0028788193 scopus 로고
    • Molecular recognition between membrane-spanning polypeptides
    • Shai, Y. (1995) Molecular recognition between membrane-spanning polypeptides, Trends Biochem. Sci. 20, 460-464.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 460-464
    • Shai, Y.1
  • 16
    • 0032455003 scopus 로고    scopus 로고
    • Synthetic peptide fragments as probes for structure determination of potassium ion-channel proteins
    • Haris, P. I. (1998) Synthetic peptide fragments as probes for structure determination of potassium ion-channel proteins, Biosci. Rep. 18, 299-312.
    • (1998) Biosci. Rep. , vol.18 , pp. 299-312
    • Haris, P.I.1
  • 17
    • 0033635131 scopus 로고    scopus 로고
    • Understanding peptide interactions with lipid bilayers: A guide to membrane protein engineering
    • Bechinger, B. (2000) Understanding peptide interactions with lipid bilayers: a guide to membrane protein engineering. Curr. Opin. Chem. Biol. 4, 639-644.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 639-644
    • Bechinger, B.1
  • 18
    • 0037064267 scopus 로고    scopus 로고
    • Structural aspects of oligomerization taking place between the transmembrane alpha-helices of bitopic membrane proteins
    • Arkin, I. T. (2002) Structural aspects of oligomerization taking place between the transmembrane alpha-helices of bitopic membrane proteins, Biochim. Biophys. Acta 1565, 347-363.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 347-363
    • Arkin, I.T.1
  • 19
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian, C., Gao, P. F., Pinto, L. H., Lamb, R. A., and Cross, T. A. (2003) Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers, Protein Sci. 12, 2597-2605.
    • (2003) Protein Sci. , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 20
    • 0037379072 scopus 로고    scopus 로고
    • How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles
    • DeGrado, W. F., Gratkowski, H., and Lear, J. D. (2003) How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles, Protein Sci. 12, 647-665.
    • (2003) Protein Sci. , vol.12 , pp. 647-665
    • DeGrado, W.F.1    Gratkowski, H.2    Lear, J.D.3
  • 21
    • 0020482906 scopus 로고
    • Ionic channels of some glycine-rich synthetic polypeptides
    • Heitz, F., and Spach, G. (1982) Ionic channels of some glycine-rich synthetic polypeptides, Biochem. Biophys. Res. Commun. 105, 179-185.
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 179-185
    • Heitz, F.1    Spach, G.2
  • 22
    • 0021978915 scopus 로고
    • Poly(DL-proline), a synthetic polypeptide behaving as an ion channel across bilayer membranes
    • de Santis, P., Palleschi, A., Savino, M., Scipioni, A., Sesta, B., and Verdini, A. (1985) Poly(DL-proline), a synthetic polypeptide behaving as an ion channel across bilayer membranes, Biophys. Chem. 21, 211-215.
    • (1985) Biophys. Chem. , vol.21 , pp. 211-215
    • Santis, P.1    Palleschi, A.2    Savino, M.3    Scipioni, A.4    Sesta, B.5    Verdini, A.6
  • 23
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear, J. D., Wasserman, Z. R., and DeGrado, W. F. (1988) Synthetic amphiphilic peptide models for protein ion channels, Science 240, 1177-1181.
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 27
    • 0026721333 scopus 로고
    • Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles
    • Chung, L. A., Lear, J. D., and DeGrado, W. F. (1992) Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles, Biochemistry 31, 6608-6616.
    • (1992) Biochemistry , vol.31 , pp. 6608-6616
    • Chung, L.A.1    Lear, J.D.2    DeGrado, W.F.3
  • 29
    • 0030974351 scopus 로고    scopus 로고
    • Electrostatic effects on ion selectivity and rectification in designed ion channel peptides
    • Lear, J. D., Schneider, J. P., Kienker, P. K., and DeGrado, W. F. (1997) Electrostatic effects on ion selectivity and rectification in designed ion channel peptides, J. Am. Chem. Soc. 119, 3212-3217.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3212-3217
    • Lear, J.D.1    Schneider, J.P.2    Kienker, P.K.3    DeGrado, W.F.4
  • 30
    • 0031030225 scopus 로고    scopus 로고
    • Permeation through an open channel: Poisson-Nernst-Planck theory of a synthetic ionic channel
    • Chen, D., Lear, J., and Eisenberg, B. (1997) Permeation through an open channel: Poisson-Nernst-Planck theory of a synthetic ionic channel, Biophys. J. 72, 97-116.
    • (1997) Biophys. J. , vol.72 , pp. 97-116
    • Chen, D.1    Lear, J.2    Eisenberg, B.3
  • 31
    • 0032989631 scopus 로고    scopus 로고
    • Exploration of the structural features defining the conduction properties of a synthetic ion channel
    • Dieckmann, G. R., Lear, J. D., Zhong, Q., Klein, M. L., DeGrado, W. F., and Sharp, K. A. (1999) Exploration of the structural features defining the conduction properties of a synthetic ion channel, Biophys. J. 76, 618-630.
    • (1999) Biophys. J. , vol.76 , pp. 618-630
    • Dieckmann, G.R.1    Lear, J.D.2    Zhong, Q.3    Klein, M.L.4    DeGrado, W.F.5    Sharp, K.A.6
  • 32
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by solid-state NMR spectroscopy
    • Bechinger, B. (1999) The structure, dynamics and orientation of antimicrobial peptides in membranes by solid-state NMR spectroscopy, Biochim. Biophys. Acta 1462, 157-183.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 33
    • 7044224836 scopus 로고    scopus 로고
    • Tolology, structure and dynamics of membrane-associated peptides by solid-state NMR spectroscopy
    • Bechinger, B., Aisenbrey, C., and Bertani, P. (2004) Tolology, structure and dynamics of membrane-associated peptides by solid-state NMR spectroscopy, Biochim. Biophys. Acta 1666, 190-204.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 190-204
    • Bechinger, B.1    Aisenbrey, C.2    Bertani, P.3
  • 35
    • 0030724875 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance characterization of gramicidin channel structure
    • Cross, T. A. (1997) Solid-state nuclear magnetic resonance characterization of gramicidin channel structure, Methods Enzymol. 289, 672-696.
    • (1997) Methods Enzymol. , vol.289 , pp. 672-696
    • Cross, T.A.1
  • 38
    • 0034866022 scopus 로고    scopus 로고
    • Conformation of alamethicin in oriented phospholipid bilayers determined by N-15 solid-state nuclear magnetic resonance
    • Bak, M., Bywater, R. P., Hohwy, M., Thomsen, J. K., Adelhorst, K., Jakobsen, H. J., Sorensen, O. W., and Nielsen, N. C. (2001) Conformation of alamethicin in oriented phospholipid bilayers determined by N-15 solid-state nuclear magnetic resonance, Biophys. J. 81, 1684-1698.
    • (2001) Biophys. J. , vol.81 , pp. 1684-1698
    • Bak, M.1    Bywater, R.P.2    Hohwy, M.3    Thomsen, J.K.4    Adelhorst, K.5    Jakobsen, H.J.6    Sorensen, O.W.7    Nielsen, N.C.8
  • 39
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin
    • Yamaguchi, S., Hong, T., Waring, A., Lehrer, R. I., and Hong, M. (2002) Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin, Biochemistry 41, 9852-9862.
    • (2002) Biochemistry , vol.41 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 41
    • 0032488653 scopus 로고    scopus 로고
    • 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers
    • 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers, Biochemistry 37, 16-22.
    • (1998) Biochemistry , vol.37 , pp. 16-22
    • Lambotte, S.1    Jasperse, P.2    Bechinger, B.3
  • 42
    • 0026732781 scopus 로고
    • Cationic lipids direct a viral glycoprotein into the class I major histocompatibility complex antigen-presentation pathway
    • Walker, C., Selby, M., Erickson, A., Cataldo, D., Valensi, J. P., and Van Nest, G. V. (1992) Cationic lipids direct a viral glycoprotein into the class I major histocompatibility complex antigen-presentation pathway, Proc. Natl. Acad. Sci. U.S.A 89, 7915-7918.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 7915-7918
    • Walker, C.1    Selby, M.2    Erickson, A.3    Cataldo, D.4    Valensi, J.P.5    Van Nest, G.V.6
  • 43
    • 37049106853 scopus 로고
    • α-fluorenyllmethoxycarbonylamino acids on polyamide supports. Synthesis of substance P and of acyl carrier proteins 65-74 decapeptide
    • α- fluorenyllmethoxycarbonylamino acids on polyamide supports. Synthesis of substance P and of acyl carrier proteins 65-74 decapeptide, J. Chem. Soc., Perkin Trans, 1, 538-546.
    • (1981) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 538-546
    • Atherton, E.1    Logan, C.J.2    Sheppart, R.C.3
  • 44
    • 33947091567 scopus 로고
    • The 9-fluorenylmethoxycarbonylamino-protecting group
    • Carpino, L. A., and Han, G. Y. (1972) The 9- fluorenylmethoxycarbonylamino-protecting group, J. Org. Chem. 37, 3404.
    • (1972) J. Org. Chem. , vol.37 , pp. 3404
    • Carpino, L.A.1    Han, G.Y.2
  • 45
    • 0026505925 scopus 로고
    • Serine derived oxazolidines as secondary structure disrupting, solubilizing building blocks in peptide synthesis
    • Haack, T., and Mutter, M. (1992) Serine derived oxazolidines as secondary structure disrupting, solubilizing building blocks in peptide synthesis, Tetrahedron Lett. 33, 1589-1592.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 1589-1592
    • Haack, T.1    Mutter, M.2
  • 46
    • 36149074059 scopus 로고
    • The control of humidity by saturated salt solutions
    • O'Brien, F. E. M. (1948) The control of humidity by saturated salt solutions, J. Sci. Instrum. 25, 73-76.
    • (1948) J. Sci. Instrum. , vol.25 , pp. 73-76
    • O'Brien, F.E.M.1
  • 47
    • 0001121265 scopus 로고
    • Flat-coil probe for NMR spectrscopy of oriented membrane samples
    • Bechinger, B., and Opella, S. J. (1991) Flat-coil probe for NMR spectrscopy of oriented membrane samples, J. Magn. Reson. 95, 585-588.
    • (1991) J. Magn. Reson. , vol.95 , pp. 585-588
    • Bechinger, B.1    Opella, S.J.2
  • 48
    • 0000599784 scopus 로고
    • Spin dynamics and thermodynamics in solid-state NMR cross polarization
    • Levitt, M. H., Suter, D., and Ernst, R. R. (1986) Spin dynamics and thermodynamics in solid-state NMR cross polarization, J. Chem. Phys. 84, 4243-4255.
    • (1986) J. Chem. Phys. , vol.84 , pp. 4243-4255
    • Levitt, M.H.1    Suter, D.2    Ernst, R.R.3
  • 52
    • 0001164631 scopus 로고
    • 13N chemical-shift tensor orientation in a polypeptide
    • 13N chemical-shift tensor orientation in a polypeptide, J. Magn. Reson. 85, 439-447.
    • (1989) J. Magn. Reson. , vol.85 , pp. 439-447
    • Teng, Q.1    Cross, T.A.2
  • 53
    • 0032475385 scopus 로고    scopus 로고
    • 15N dipolar coupling interactions in a peptide bond of uniaxially oriented and polycrystalline samples by one-dimensional dipolar chemical shift solid-state NMR spectroscopy
    • 15N dipolar coupling interactions in a peptide bond of uniaxially oriented and polycrystalline samples by one-dimensional dipolar chemical shift solid-state NMR spectroscopy, J. Am. Chem. Soc. 120, 8868-8874.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8868-8874
    • Lee, D.K.1    Wittebort, R.J.2    Ramamoorthy, A.3
  • 56
    • 0028434564 scopus 로고
    • 13N NMR chemical shifts in proteins and secondary structure
    • 13N NMR chemical shifts in proteins and secondary structure, J. Biomol. NMR 4, 341-348.
    • (1994) J. Biomol. NMR , vol.4 , pp. 341-348
    • Le, H.1    Oldfield, E.2
  • 57
    • 0028278173 scopus 로고
    • A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel
    • Kienker, P. K., DeGrado, W. F., and Lear, J. D. (1994) A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel, Proc. Natl. Acad. Sci. U.S.A. 91, 4859-4863.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 4859-4863
    • Kienker, P.K.1    DeGrado, W.F.2    Lear, J.D.3
  • 59
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. (2002) Mode of action of membrane active antimicrobial peptides, Biopolymers 66, 236-248.
    • (2002) Biopolymers , vol.66 , pp. 236-248
    • Shai, Y.1
  • 60
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • Matsuzaki, K., Murase, O., Tokuda, H., Funakoshi, S., Fujii, N., and Miyajima, K. (1994) Orientational and aggregational states of magainin 2 in phospholipid bilayers, Biochemistry 33, 3342-3349.
    • (1994) Biochemistry , vol.33 , pp. 3342-3349
    • Matsuzaki, K.1    Murase, O.2    Tokuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyajima, K.6
  • 61
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion, and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selective lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion, and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selective lytic peptides, Biochim. Biophys. Acta 1462, 55-70.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 62
    • 0035979758 scopus 로고    scopus 로고
    • Solid-state NMR investigations of interaction contributions that determine the alignment of helical polypeptides in biological membranes
    • Bechinger, B. (2001) Solid-state NMR investigations of interaction contributions that determine the alignment of helical polypeptides in biological membranes, FEBS Lett. 504, 161-165.
    • (2001) FEBS Lett. , vol.504 , pp. 161-165
    • Bechinger, B.1
  • 63
    • 0028879250 scopus 로고
    • The infrared dichroism of transmembrane helical polypeptides
    • Axelsen, P. H., Kaufman, B. K., McElhaney, R. N., and Lewis, R. N. (1995) The infrared dichroism of transmembrane helical polypeptides, Biophys. J. 69, 2770-2781.
    • (1995) Biophys. J. , vol.69 , pp. 2770-2781
    • Axelsen, P.H.1    Kaufman, B.K.2    McElhaney, R.N.3    Lewis, R.N.4
  • 64
    • 0037093905 scopus 로고    scopus 로고
    • Mechanisms of the interaction of alpha-helical transmembrane peptides with phospholipid bilayers
    • Lewis, R. N., Zhang, Y. P., Liu, F., and McElhaney, R. N. (2002) Mechanisms of the interaction of alpha-helical transmembrane peptides with phospholipid bilayers, Bioelectrochemistry 56, 135-140.
    • (2002) Bioelectrochemistry , vol.56 , pp. 135-140
    • Lewis, R.N.1    Zhang, Y.P.2    Liu, F.3    McElhaney, R.N.4
  • 65
    • 0033783447 scopus 로고    scopus 로고
    • 31P solid-state NMR spectroscopy investigation
    • 31P solid-state NMR spectroscopy investigation, Biochemistry 39, 13106-13114.
    • (2000) Biochemistry , vol.39 , pp. 13106-13114
    • Harzer, U.1    Bechinger, B.2
  • 66
    • 21844479041 scopus 로고    scopus 로고
    • Incorporation of hydrophobic helix-bundle peptides into lipid bilayer membranes facilitated by a peptide-umbrella structure
    • Ueda, H., Kimura, S., and Imanishi, Y. (1998) Incorporation of hydrophobic helix-bundle peptides into lipid bilayer membranes facilitated by a peptide-umbrella structure, Chem. Commun. 3, 363-364.
    • (1998) Chem. Commun. , vol.3 , pp. 363-364
    • Ueda, H.1    Kimura, S.2    Imanishi, Y.3
  • 67
    • 0034681908 scopus 로고    scopus 로고
    • Designing transmembrane alpha-helices that insert spontaneously
    • Wimley, W. C., and White, S. H. (2000) Designing transmembrane alpha-helices that insert spontaneously, Biochemistry 39, 4432-4442.
    • (2000) Biochemistry , vol.39 , pp. 4432-4442
    • Wimley, W.C.1    White, S.H.2
  • 68
    • 0030589158 scopus 로고    scopus 로고
    • Towards membrane protein design: PH dependent topology of histidine-containing polypeptides
    • Bechinger, B. (1996) Towards membrane protein design: pH dependent topology of histidine-containing polypeptides, J. Mol. Biol. 263, 768-775.
    • (1996) J. Mol. Biol. , vol.263 , pp. 768-775
    • Bechinger, B.1
  • 69
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. (2000) Action of antimicrobial peptides: Two-state model, Biochemistry 39, 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 71
    • 0036156880 scopus 로고    scopus 로고
    • Sigmoidal concentration dependence of antimicrobial peptide activities: A case study on alamethicin
    • Chen, F. Y., Lee, M. T., and Huang, H. W. (2002) Sigmoidal concentration dependence of antimicrobial peptide activities: a case study on alamethicin, Biophys. J. 82, 908-914.
    • (2002) Biophys. J. , vol.82 , pp. 908-914
    • Chen, F.Y.1    Lee, M.T.2    Huang, H.W.3
  • 72
    • 0023248806 scopus 로고
    • Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes
    • Vogel, H. (1987) Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes, Biochemistry 26, 4562-4572.
    • (1987) Biochemistry , vol.26 , pp. 4562-4572
    • Vogel, H.1
  • 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., Ding, 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    Ding, L.4    Huang, H.W.5
  • 74
    • 16344384943 scopus 로고    scopus 로고
    • Dynamic structure of vesicle-bound melittin in a variety of lipid chain length by solid-state NMR
    • Toraya, S., Nishimura, K., and Naito, A. (2004) Dynamic structure of vesicle-bound melittin in a variety of lipid chain length by solid-state NMR, Biophys. J. 87, 3323-3335.
    • (2004) Biophys. J. , vol.87 , pp. 3323-3335
    • Toraya, S.1    Nishimura, K.2    Naito, A.3
  • 75
    • 0023887975 scopus 로고
    • Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: Salt and cholesterol effects
    • Stankowski, S., Schwarz, U. D., and Schwarz, G. (1988) Voltage-dependent pore activity of the peptide alamethicin correlated with incorporation in the membrane: salt and cholesterol effects, Biochim. Biophys. Acta 941, 11-18.
    • (1988) Biochim. Biophys. Acta , vol.941 , pp. 11-18
    • Stankowski, S.1    Schwarz, U.D.2    Schwarz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.