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Volumn 242, Issue 2, 1996, Pages 372-386

Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments

Author keywords

Antennapedia; Membrane; Modeling; NMR; Vector

Indexed keywords

HOMEODOMAIN PROTEIN;

EID: 0029802678     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0372r.x     Document Type: Article
Times cited : (156)

References (63)
  • 1
    • 5144233105 scopus 로고
    • MLEV-17 based two dimensional homonuclear magnetization transfer spectoscopy
    • Bax, A. & Davis, D. G. (1985) MLEV-17 based two dimensional homonuclear magnetization transfer spectoscopy, J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0028072087 scopus 로고
    • Three dimensional structure of the highly conserved seventh transmembrane domain of G-protein coupled receptors
    • Berlose, J. P., Convert, O., Brunissen, A., Chassaing, G. & Lavielle, S. (1994) Three dimensional structure of the highly conserved seventh transmembrane domain of G-protein coupled receptors, Eur. J. Biochem. 225, 827-843.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 827-843
    • Berlose, J.P.1    Convert, O.2    Brunissen, A.3    Chassaing, G.4    Lavielle, S.5
  • 3
    • 0022497150 scopus 로고
    • Interactions between membranes and cytolytic peptides
    • Bernheimer, A. W. & Rudy, B. (1986) Interactions between membranes and cytolytic peptides, Biochim. Biophys. Acta 864, 123-141.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 123-141
    • Bernheimer, A.W.1    Rudy, B.2
  • 5
    • 0025119481 scopus 로고
    • Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance
    • Bradley, E. K., Thomason, J. F., Cohen, F. E., Kosen, P. A. & Kuntz, I. D. (1990) Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance, J. Mol. Biol. 215, 607-622.
    • (1990) J. Mol. Biol. , vol.215 , pp. 607-622
    • Bradley, E.K.1    Thomason, J.F.2    Cohen, F.E.3    Kosen, P.A.4    Kuntz, I.D.5
  • 7
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid residues measured in aqueous solution of the linear tetrapeptide Gly-Gly-X-Ala-OH
    • 1H NMR parameters of the common amino acid residues measured in aqueous solution of the linear tetrapeptide Gly-Gly-X-Ala-OH, Biopolymers 18, 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 8
    • 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. & 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
  • 9
    • 0000939457 scopus 로고
    • The three-dimensional structure of α1-purothionin in solution: Combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore, G. M., Nilges, M., Subumaran, D. K., Brünger, A. T., Karplus, M. & Gronenborn, A. M. (1986) The three-dimensional structure of α1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics, EMBO J. 5, 2729-2735.
    • (1986) EMBO J. , vol.5 , pp. 2729-2735
    • Clore, G.M.1    Nilges, M.2    Subumaran, D.K.3    Brünger, A.T.4    Karplus, M.5    Gronenborn, A.M.6
  • 10
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophane fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • De Kroon, A. I. P. M., Soekarjo, M. W., De Gier, J. & De Kruijff, B. (1990) The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophane fluorescence measurements combined with the use of aqueous and hydrophobic quenchers, Biochemistry 29, 8229-8240.
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.P.M.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 11
    • 9544251481 scopus 로고
    • Lipid-peptide interactions in model systems: Membrane insertion and translocation of peptides
    • Elsevier, Amsterdam
    • De Kroon, A. I. P. M., De Gier, J. & De Kruijff, B. (1993) Lipid-peptide interactions in model systems: Membrane insertion and translocation of peptides, in Protein-lipid interactions, pp. 107-126, Elsevier, Amsterdam.
    • (1993) Protein-lipid Interactions , pp. 107-126
    • De Kroon, A.I.P.M.1    De Gier, J.2    De Kruijff, B.3
  • 13
    • 0024433591 scopus 로고
    • The photosynthetic reaction center from the purple Bacterium Rhodopseudomonas viridis
    • Deisenhofer, J. & Michel, H. (1989) The photosynthetic reaction center from the purple Bacterium Rhodopseudomonas viridis, Science 245, 1463-1473.
    • (1989) Science , vol.245 , pp. 1463-1473
    • Deisenhofer, J.1    Michel, H.2
  • 14
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D., Joliot, A., Chassaing, G. & Prochiantz, A. (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes, J. Biol. Chem. 269, 10444-10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.2    Chassaing, G.3    Prochiantz, A.4
  • 15
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor independent
    • Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G. & Prochiantz, A. (1996) Cell internalization of the third helix of the Antennapedia homeodomain is receptor independent, J. Biol. Chem. 271, 18188-18193.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 17
    • 0029111532 scopus 로고
    • Interaction of the mammalian antibacterial cecropin P1 with phospholipid vesicles
    • Gazit, E., Boman, A., Boman, H. G. & Shai, Y. (1995) Interaction of the mammalian antibacterial cecropin P1 with phospholipid vesicles, Biochemistry 34, 11479-11488.
    • (1995) Biochemistry , vol.34 , pp. 11479-11488
    • Gazit, E.1    Boman, A.2    Boman, H.G.3    Shai, Y.4
  • 18
    • 0023239424 scopus 로고
    • Homeo boxes in the study of development
    • Gehring, W. J. (1987) Homeo boxes in the study of development, Science 236, 1245-1252.
    • (1987) Science , vol.236 , pp. 1245-1252
    • Gehring, W.J.1
  • 19
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, G. D. (1969) Computed circular dichroism spectra for the evaluation of protein conformation, Biochemistry 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 20
    • 0014441009 scopus 로고
    • Studies on phosphatidylcholine vesicles. Formation and physical characteristics
    • Huang, C. H. (1969) Studies on phosphatidylcholine vesicles. Formation and physical characteristics, Biochemistry 8, 344-352.
    • (1969) Biochemistry , vol.8 , pp. 344-352
    • Huang, C.H.1
  • 21
    • 0344620689 scopus 로고
    • Gradient-enhanced proton-detected heteronuclear multiple-quantum coherence spectroscopy
    • Hurd, R. E. & John, B. (1991) Gradient-enhanced proton-detected heteronuclear multiple-quantum coherence spectroscopy, J. Magn. Reson. 91, 648-653.
    • (1991) J. Magn. Reson. , vol.91 , pp. 648-653
    • Hurd, R.E.1    John, B.2
  • 22
    • 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. & White, S. H. (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
  • 23
    • 0024322106 scopus 로고
    • Interaction of the saccharomyces cerevisae α-factor with phospholipid vesicles as revealed by proton and phosphorus NMR
    • Jelicks, L. A., Broido, M. S., Becker, J. M. & Naider, F. R. (1989) Interaction of the saccharomyces cerevisae α-factor with phospholipid vesicles as revealed by proton and phosphorus NMR, Biochemistry 28, 4233-4240.
    • (1989) Biochemistry , vol.28 , pp. 4233-4240
    • Jelicks, L.A.1    Broido, M.S.2    Becker, J.M.3    Naider, F.R.4
  • 25
    • 0022318901 scopus 로고
    • II phase formation in phosphatidylethanolamine
    • II phase formation in phosphatidylethanolamine, Biochemistry 24, 7881-7890.
    • (1985) Biochemistry , vol.24 , pp. 7881-7890
    • Killian, J.A.1    De Kruijff, B.2
  • 26
    • 0023154683 scopus 로고
    • II phase formation by gramicidins A, B and C in dioleoyl phosphatidylcholine model membranes. A study on the role of tryptophan residues
    • II phase formation by gramicidins A, B and C in dioleoyl phosphatidylcholine model membranes. A study on the role of tryptophan residues, Biochim. Biophys. Acta 897, 269-284.
    • (1987) Biochim. Biophys. Acta , vol.897 , pp. 269-284
    • Killian, J.A.1    Burger, K.N.J.2    De Kruijff, B.3
  • 28
    • 10544221599 scopus 로고
    • Amide chemical shifts in many helices and proteins are periodic
    • Kuntz, I. D., Kosen, P. A. & Craig, E. C. (1991) Amide chemical shifts in many helices and proteins are periodic, J. Am. Chem. Soc. 105, 5948-5949.
    • (1991) J. Am. Chem. Soc. , vol.105 , pp. 5948-5949
    • Kuntz, I.D.1    Kosen, P.A.2    Craig, E.C.3
  • 29
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two dimensional NMR spectroscopy
    • Macura, S. & Ernst, R. R. (1980) Elucidation of cross-relaxation in liquids by two dimensional NMR spectroscopy, Mol. Phys. 41, 95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 30
    • 0021765676 scopus 로고
    • Structural changes in membrane produced by the binding of small amphipatic molecules
    • Maher, P. & Singer, S. J. (1984) Structural changes in membrane produced by the binding of small amphipatic molecules, Biochemistry 23, 232-240.
    • (1984) Biochemistry , vol.23 , pp. 232-240
    • Maher, P.1    Singer, S.J.2
  • 31
    • 0025797055 scopus 로고
    • Endocytosis and targeting of exogenous HIV-1 Tat protein
    • Mann, D. A. & Frankel, D. (1991) Endocytosis and targeting of exogenous HIV-1 Tat protein, EMBO J. 10, 1733-1739.
    • (1991) EMBO J. , vol.10 , pp. 1733-1739
    • Mann, D.A.1    Frankel, D.2
  • 33
    • 0025941179 scopus 로고
    • Interactions of an antimicrobial peptide tachyplesin 1 with lipid membranes
    • Matsuzaki, K., Fukui, M., Fujii, N. & Miyajima, K. (1991) Interactions of an antimicrobial peptide tachyplesin 1 with lipid membranes, Biochim. Biophys. Acta 1070, 259-234.
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 259-1234
    • Matsuzaki, K.1    Fukui, M.2    Fujii, N.3    Miyajima, K.4
  • 34
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • Matsuzaki, K., Murase, O., Takuda, H., Funakoshi, S., Fujii, N. & 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    Takuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyajima, K.6
  • 35
    • 0029065501 scopus 로고
    • Translocation of a channel-forming peptide magainin 2 across lipid bilayers by forming a pore
    • Matsuzaki, K., Murase, O., Fujii, N. & Miyajima, K. (1995a) Translocation of a channel-forming peptide magainin 2 across lipid bilayers by forming a pore, Biochemistry 34, 6521-6526.
    • (1995) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 36
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide magainin 2
    • Matsuzaki, K., Sugishita, K., Fujii, N. & Miyajima, K. (1995b) Molecular basis for membrane selectivity of an antimicrobial peptide magainin 2, Biochemistry 34, 3423-3429.
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 37
    • 33947475091 scopus 로고
    • Light scattering by some lauryl sulfate solutions
    • Mysels, K. J. & Princen, L. H. (1959) Light scattering by some lauryl sulfate solutions, J. Phys. Chem. 63, 1699-1703.
    • (1959) J. Phys. Chem. , vol.63 , pp. 1699-1703
    • Mysels, K.J.1    Princen, L.H.2
  • 38
    • 0023732144 scopus 로고
    • Determination of the three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms
    • Nilges, M., Clore, G. M. & Gronenborn, A. M. (1988) Determination of the three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms, FEBS Lett. 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 39
    • 0027064667 scopus 로고
    • Application of active-phase plot to the kinetic analysis of lipoxygenase in reverse micelles
    • Perez-Gilabert, M., Sanchez-Ferrer, A. & Garcia-Carmona, F. (1992) Application of active-phase plot to the kinetic analysis of lipoxygenase in reverse micelles, Biochemistry J. 288, 1011-1015.
    • (1992) Biochemistry J. , vol.288 , pp. 1011-1015
    • Perez-Gilabert, M.1    Sanchez-Ferrer, A.2    Garcia-Carmona, F.3
  • 40
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solution
    • Piotto, M., Saudek, V. & Skelnar, V. J. (1992) Gradient-tailored excitation for single quantum NMR spectroscopy of aqueous solution, J. Biomol. NMR. 2, 661-665.
    • (1992) J. Biomol. NMR. , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Skelnar, V.J.3
  • 41
    • 0024407460 scopus 로고
    • The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: Comparison with prokaryotic repressors
    • Qian, Y. Q., Billeter, M., Otting, G., Müller, M., Gehring, W. J. & Wüthrich, K. (1989) The structure of the Antennapedia homeodomain determined by NMR spectroscopy in solution: comparison with prokaryotic repressors, Cell 59, 573-580.
    • (1989) Cell , vol.59 , pp. 573-580
    • Qian, Y.Q.1    Billeter, M.2    Otting, G.3    Müller, M.4    Gehring, W.J.5    Wüthrich, K.6
  • 42
    • 0026482958 scopus 로고
    • NMR structure determination reveals that the homeodomain is connected through a flexible linker to the main body in the Drosophila Antennapedia protein
    • Qian, Y., Otting, G., Furukubo-Tokunaga, K., Affolter, M., Gehring, W. J. & Wüthrich, K. (1992) NMR structure determination reveals that the homeodomain is connected through a flexible linker to the main body in the Drosophila Antennapedia protein, Proc. Natl Acad. Sci. USA 89, 10738-10742.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10738-10742
    • Qian, Y.1    Otting, G.2    Furukubo-Tokunaga, K.3    Affolter, M.4    Gehring, W.J.5    Wüthrich, K.6
  • 44
    • 0022997975 scopus 로고
    • Studies on the lipid dependency and mechanism of the translocation of the mitochondrial precursor protein apocytochrome c across model membrane
    • Rietveld, A., Jordi, W. & De Kruijff, B. (1986) Studies on the lipid dependency and mechanism of the translocation of the mitochondrial precursor protein apocytochrome c across model membrane, J. Biol. Chem. 261, 3846-3856.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3846-3856
    • Rietveld, A.1    Jordi, W.2    De Kruijff, B.3
  • 45
    • 0027180807 scopus 로고
    • Conformational behavior of Escherichia coli OmpA signal peptides in membranes mimetics environments
    • Rizo, J., Blanco, F. J., Kobe, B., Bruch, M. D. & Gierasch, L. M. (1993) Conformational behavior of Escherichia coli OmpA signal peptides in membranes mimetics 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
  • 46
    • 0028147455 scopus 로고
    • Fragmentation of phospholipid bilayers by myelin basic protein
    • Roux, M., Nezil, F. A., Monck, M. & Bloom, M. (1994) Fragmentation of phospholipid bilayers by myelin basic protein, Biochemistry 33, 307-311.
    • (1994) Biochemistry , vol.33 , pp. 307-311
    • Roux, M.1    Nezil, F.A.2    Monck, M.3    Bloom, M.4
  • 47
    • 0000738920 scopus 로고
    • Conjugation of methroxate to poly(l-Lysine) increases drug transport and overcomes drug resistance in cultured cells
    • Ryser, H. J. P. & Shen, W. C. (1978) Conjugation of methroxate to poly(l-Lysine) increases drug transport and overcomes drug resistance in cultured cells, Proc. Natl Acad. Sci. USA 75, 3867-3870.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3867-3870
    • Ryser, H.J.P.1    Shen, W.C.2
  • 48
    • 0028986125 scopus 로고
    • Native Escherichia coli Ompf porin surfaces probed by atomic force microscopy
    • Schabert, F. A., Henn, C. & Engel, A. (1995) Native Escherichia coli Ompf porin surfaces probed by atomic force microscopy, Science 268, 92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henn, C.2    Engel, A.3
  • 49
    • 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
  • 51
    • 0028923477 scopus 로고
    • Loligomers: Design of de novo peptide-based intracellular vesicles
    • Sheldon, K., Liu, D., Ferguson, J. & Gariepy, J. (1995) Loligomers: design of de novo peptide-based intracellular vesicles, Proc. Natl Acad. Sci. USA 92, 2056-2060.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2056-2060
    • Sheldon, K.1    Liu, D.2    Ferguson, J.3    Gariepy, J.4
  • 52
    • 0021378778 scopus 로고
    • Inverted micellar structures in bilayers
    • Siegel, D. P. (1984) Inverted micellar structures in bilayers, Biophys. J. 45, 399-420.
    • (1984) Biophys. J. , vol.45 , pp. 399-420
    • Siegel, D.P.1
  • 55
    • 0030071721 scopus 로고    scopus 로고
    • Down regulation of SOD1 leads to cell death by the NO-peroxynitrite pathway
    • Troy, C. M., Derossi, D., Prochiantz, A. & Shelanski, M. L. (1996) Down regulation of SOD1 leads to cell death by the NO-peroxynitrite pathway, J. Neurosci. 16, 253-261.
    • (1996) J. Neurosci. , vol.16 , pp. 253-261
    • Troy, C.M.1    Derossi, D.2    Prochiantz, A.3    Shelanski, M.L.4
  • 56
    • 0015100247 scopus 로고
    • The gramicidin a transmembrane channel: Characteristics of head to head dimerized π(L,D) helices
    • Urry, D. W., Goodall, M. C., Glickson, J. D. & Mayers, D. F. (1971) The gramicidin A transmembrane channel: characteristics of head to head dimerized π(L,D) helices, Proc. Natl Acad. Sci. USA 68, 1907-1911.
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 1907-1911
    • Urry, D.W.1    Goodall, M.C.2    Glickson, J.D.3    Mayers, D.F.4
  • 57
    • 0027431865 scopus 로고
    • Effects of different continium dielectric models in a molecular dynamics and energy minimization study of the antigenic loop of foot- and-mouth disease virus
    • Vega, M. C., Aleman, C., Alhambra, C. & Perez, J. J. (1993) Effects of different continium dielectric models in a molecular dynamics and energy minimization study of the antigenic loop of foot- and-mouth disease virus, J. Biomol. Struct. Dyn. 11, 429-441.
    • (1993) J. Biomol. Struct. Dyn. , vol.11 , pp. 429-441
    • Vega, M.C.1    Aleman, C.2    Alhambra, C.3    Perez, J.J.4
  • 60
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S. J., Kollman, P. A., Nguyen, D. T. & Case, D. A. (1986) An all atom force field for simulations of proteins and nucleic acids, J. Comp. Chem. 7, 230-252.
    • (1986) J. Comp. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 61
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D. & 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
  • 63
    • 0001675109 scopus 로고
    • Relationship between amide proton chemical shifts and hydrogen bonding in amphipatic α-helical peptides
    • Zhou, N. E., Zhu, B. Y., Sykes, B. D. & Hodges, R. S. (1992) Relationship between amide proton chemical shifts and hydrogen bonding in amphipatic 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.Y.2    Sykes, B.D.3    Hodges, R.S.4


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