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Volumn 275, Issue 2, 1998, Pages 365-378

Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins

Author keywords

Alcohol; Hexafluoroisopropanol; Melittin; Protein folding; helix

Indexed keywords

ALCOHOL; ALKANOL; BEE VENOM; HALOGEN; HYDROCARBON; HYDROXYL GROUP; MELITTIN; PROPANOL;

EID: 0032536194     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1468     Document Type: Article
Times cited : (236)

References (55)
  • 1
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease
    • Barrow, C. J., Yasuda, A., Kenny, P. T. & Zagorski, M. G. (1992). Solution conformations and aggregational properties of synthetic amyloid beta-peptides of Alzheimer's disease. J. Mol. Biol. 225, 1075-1093.
    • (1992) J. Mol. Biol. , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 3
    • 0020473234 scopus 로고
    • Conformation and aggregation of melittin: Dependence on pH and concentration
    • Bello, J., Bello, H. R. & Granados, E. (1982). Conformation and aggregation of melittin: dependence on pH and concentration. Biochemistry, 21, 461-465.
    • (1982) Biochemistry , vol.21 , pp. 461-465
    • Bello, J.1    Bello, H.R.2    Granados, E.3
  • 4
    • 0028301327 scopus 로고
    • NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation
    • Blanco, F. J., Jimenez, M. A., Rico, M., Santoro, J., Pineda, A. & Nieto, J. L. (1994). NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation. Biochemistry, 33, 6009-6014.
    • (1994) Biochemistry , vol.33 , pp. 6009-6014
    • Blanco, F.J.1    Jimenez, M.A.2    Rico, M.3    Santoro, J.4    Pineda, A.5    Nieto, J.L.6
  • 5
    • 0027492170 scopus 로고
    • A partially folded state of hen lysozyme in trifluoroethanol: Structural characterization and implication for protein folding
    • Buck, M., Radford, S. E. & Dobson, C. M. (1993). A partially folded state of hen lysozyme in trifluoroethanol: structural characterization and implication for protein folding. Biochemistry, 32, 669-678.
    • (1993) Biochemistry , vol.32 , pp. 669-678
    • Buck, M.1    Radford, S.E.2    Dobson, C.M.3
  • 6
    • 0028882136 scopus 로고
    • Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: Assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol
    • Buck, M., Schwalbe, H. & Dobson, C. M. (1995). Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol. Biochemistry, 34, 13219-13232.
    • (1995) Biochemistry , vol.34 , pp. 13219-13232
    • Buck, M.1    Schwalbe, H.2    Dobson, C.M.3
  • 7
    • 0029967685 scopus 로고    scopus 로고
    • 15N NMR relaxation measurements of hen egg-white lysozyme denatured in trifluoroethanol
    • 15N NMR relaxation measurements of hen egg-white lysozyme denatured in trifluoroethanol. J. Mol. Biol. 257, 669-683.
    • (1996) J. Mol. Biol. , vol.257 , pp. 669-683
    • Buck, M.1    Schwalbe, H.2    Dobson, C.M.3
  • 8
    • 9944232242 scopus 로고
    • Group contribution to the thermodynamic properties of non-ionic organic solutes in dilute aqueous solution
    • Cabani, S., Gianni, P., Mollica, V. & Lepori, L. (1981). Group contribution to the thermodynamic properties of non-ionic organic solutes in dilute aqueous solution. J. Sol. Chem. 10, 563-595.
    • (1981) J. Sol. Chem. , vol.10 , pp. 563-595
    • Cabani, S.1    Gianni, P.2    Mollica, V.3    Lepori, L.4
  • 10
    • 84996102538 scopus 로고
    • Analysis of the interaction of membrane-active peptides with membranes: The case of melittin in surfactant assemblies
    • Chandani, B. & Balasubramanian, D. (1986). Analysis of the interaction of membrane-active peptides with membranes: the case of melittin in surfactant assemblies. Biopolymers, 25, 1259-1272.
    • (1986) Biopolymers , vol.25 , pp. 1259-1272
    • Chandani, B.1    Balasubramanian, D.2
  • 11
    • 0028289435 scopus 로고
    • Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N- and C-capping
    • Doig, A. J., Chakrabartty, A., Klingler, T. M. & Baldwin, R. L. (1994). Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N- and C-capping. Biochemistry, 33, 3396-3403.
    • (1994) Biochemistry , vol.33 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 12
  • 13
    • 0000421373 scopus 로고
    • Alcohol-water mixtures revisited
    • Franks, F., ed., Cambridge University Press, London
    • Franks, F. & Desnoyers, J. E. (1986). Alcohol-water mixtures revisited. In Water Science Review 1 (Franks, F., ed.), pp. 171-231, Cambridge University Press, London.
    • (1986) Water Science Review , vol.1 , pp. 171-231
    • Franks, F.1    Desnoyers, J.E.2
  • 15
    • 0026602028 scopus 로고
    • Mechanism of the conformational transition of melittin
    • Goto, Y. & Hagihara, Y. (1992). Mechanism of the conformational transition of melittin. Biochemistry, 31, 732-738.
    • (1992) Biochemistry , vol.31 , pp. 732-738
    • Goto, Y.1    Hagihara, Y.2
  • 16
    • 0015527253 scopus 로고
    • Bee and wasp venoms. the biochemistry and pharmacology of their peptides and enzymes are reviewed
    • Habermann, H. (1972). Bee and wasp venoms. The biochemistry and pharmacology of their peptides and enzymes are reviewed. Science, 177, 314-322.
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, H.1
  • 17
    • 0026470007 scopus 로고
    • Charge repulsion in the conformational stability of melittin
    • Hagihara, Y., Kataoka, M., Aimoto, S. & Goto, Y. (1992). Charge repulsion in the conformational stability of melittin. Biochemistry, 31, 11908-11914.
    • (1992) Biochemistry , vol.31 , pp. 11908-11914
    • Hagihara, Y.1    Kataoka, M.2    Aimoto, S.3    Goto, Y.4
  • 18
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Kuroda, Y., Tanaka, T. & Goto, Y. (1995). High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254, 737-746.
    • (1995) J. Mol. Biol. , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 19
    • 0029740071 scopus 로고    scopus 로고
    • Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Segawa, S. & Goto, Y. (1996). Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct. Biol. 3, 868-873.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 20
    • 0031042309 scopus 로고    scopus 로고
    • Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol
    • Hirota, N., Mizuno, K. & Goto, Y. (1997). Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol. Protein Sci. 6, 416-421.
    • (1997) Protein Sci. , vol.6 , pp. 416-421
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 21
    • 0026516588 scopus 로고
    • Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies
    • Jackson, M. & Mantsch, H. H. (1992). Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. Biochim. Biophys. Acta, 1118, 139-143.
    • (1992) Biochim. Biophys. Acta , vol.1118 , pp. 139-143
    • Jackson, M.1    Mantsch, H.H.2
  • 22
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities from trifluoroethanol titration curves
    • Jasanoff, A. & Fersht, A. R. (1994). Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry, 33, 2129-2135.
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 24
    • 0002889181 scopus 로고    scopus 로고
    • CD spectroscopy and the helix-coil transition in peptides and polypeptides
    • Fasman, G. D., ed., Plenum Press, New York
    • Kallenbach, N. R., Lyu, P. & Zhou, H. (1996). CD spectroscopy and the helix-coil transition in peptides and polypeptides. In Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G. D., ed.), pp. 201-259, Plenum Press, New York.
    • (1996) Circular Dichroism and the Conformational Analysis of Biomolecules , pp. 201-259
    • Kallenbach, N.R.1    Lyu, P.2    Zhou, H.3
  • 25
    • 0000725041 scopus 로고    scopus 로고
    • Mixing schemes in aqueous solutions of nonelectrolytes: A thermodynamic approach
    • Koga, Y. (1996). Mixing schemes in aqueous solutions of nonelectrolytes: a thermodynamic approach. J. Phys. Chem. 100, 5172-5181.
    • (1996) J. Phys. Chem. , vol.100 , pp. 5172-5181
    • Koga, Y.1
  • 26
    • 0030334664 scopus 로고    scopus 로고
    • High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D NMR spectroscopy
    • Kuroda, Y., Hamada, D., Tanaka, T. & Goto, Y. (1996). High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D NMR spectroscopy. Fold. Des. 1, 255-263.
    • (1996) Fold. Des. , vol.1 , pp. 255-263
    • Kuroda, Y.1    Hamada, D.2    Tanaka, T.3    Goto, Y.4
  • 27
    • 0029620988 scopus 로고
    • Nonideality of water-hexafluoroethanol mixtures as studied by X-ray small angle scattering
    • Kurpin, S., Grauslund, A., Ehrenberg, A. & Koch, M. H. J. (1995). Nonideality of water-hexafluoroethanol mixtures as studied by X-ray small angle scattering. Biochem. Biophys. Res. Commun. 217, 1151-1156.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1151-1156
    • Kurpin, S.1    Grauslund, A.2    Ehrenberg, A.3    Koch, M.H.J.4
  • 28
    • 0020480265 scopus 로고
    • Infrared spectroscopic study of the secondary structure of melittin in water, 2-chloroethanol, and phospholipid bilayer dispersions
    • Lavialle, F., Adams, R. G. & Levin, I. W. (1982). Infrared spectroscopic study of the secondary structure of melittin in water, 2-chloroethanol, and phospholipid bilayer dispersions. Biochemistry, 21, 2305-2312.
    • (1982) Biochemistry , vol.21 , pp. 2305-2312
    • Lavialle, F.1    Adams, R.G.2    Levin, I.W.3
  • 30
    • 33847801579 scopus 로고
    • Charge relay at the peptide bond. a protein magnetic resonance study of solvation effects on the amide electron density distribution
    • Llinas, M. & Klein, M. P. (1975). Charge relay at the peptide bond. A protein magnetic resonance study of solvation effects on the amide electron density distribution. J. Am. Chem. Soc. 97, 4731-4737.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4731-4737
    • Llinas, M.1    Klein, M.P.2
  • 31
    • 0000333671 scopus 로고
    • On the theory of helix-coil transitions in polypeptides
    • Lifson, S. & Roig, A. (1961). On the theory of helix-coil transitions in polypeptides. J. Chem. Phys. 34, 1963-1974.
    • (1961) J. Chem. Phys. , vol.34 , pp. 1963-1974
    • Lifson, S.1    Roig, A.2
  • 32
    • 0028862864 scopus 로고
    • Peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu, Y. & Bolen, D. W. (1995). Peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry, 34, 12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 33
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptide from trifluoroethanol/water mixtures back to water
    • Luo, P. & Baldwin, R. L. (1997). Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptide from trifluoroethanol/water mixtures back to water. Biochemistry, 36, 8413-8421.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 36
    • 0022804939 scopus 로고
    • Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol
    • Nelson, J. W. & Kallenbach, N. R. (1986). Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol. Proteins: Struct. Funct. Genet. 1, 211-217.
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 211-217
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 37
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki, Y. & Tanford, C. (1971). The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J. Biol. Chem. 246, 2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 38
    • 0027349239 scopus 로고
    • Hydration and heat stability effects on protein unfolding
    • Oobatake, M. & Ooi, T. (1992). Hydration and heat stability effects on protein unfolding. Prog. Biophys. Mol. Biol. 59, 237-284.
    • (1992) Prog. Biophys. Mol. Biol. , vol.59 , pp. 237-284
    • Oobatake, M.1    Ooi, T.2
  • 39
    • 0017891481 scopus 로고
    • Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5. 8
    • Pittz, E. P. & Timasheff, S. N. (1978). Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5. 8. Biochemistry, 17, 615-623.
    • (1978) Biochemistry , vol.17 , pp. 615-623
    • Pittz, E.P.1    Timasheff, S.N.2
  • 40
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction
    • Quay, S. C. & Condie, C. C. (1983). Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction. Biochemistry, 22, 695-700.
    • (1983) Biochemistry , vol.22 , pp. 695-700
    • Quay, S.C.1    Condie, C.C.2
  • 41
    • 0028356365 scopus 로고
    • 15N-labeled helical peptides measured by isotope-edited NMR
    • 15N-labeled helical peptides measured by isotope-edited NMR. Biochemistry, 33, 7760-7767.
    • (1994) Biochemistry , vol.33 , pp. 7760-7767
    • Rohl, C.A.1    Baldwin, R.L.2
  • 42
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acid measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl, C. A., Chakrabartty, A. & Baldwin, R. L. (1996). Helix propagation and N-cap propensities of the amino acid measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5, 2623-2637.
    • (1996) Protein Sci. , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 43
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz, J. M., Qian, H., York, E. J., Stewart, J. M. & Baldwin, R. L. (1991). Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers, 31, 1463-1470.
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 44
    • 0030593499 scopus 로고    scopus 로고
    • Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat
    • Schönbrunner, N., Wey, J., Engels, J., Gerog, H. & Kiefhaber, T. (1996). Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat. J. Mol. Biol. 260, 432-445.
    • (1996) J. Mol. Biol. , vol.260 , pp. 432-445
    • Schönbrunner, N.1    Wey, J.2    Engels, J.3    Gerog, H.4    Kiefhaber, T.5
  • 45
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K. & Goto, Y. (1995). Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 235, 180-194.
    • (1995) J. Mol. Biol. , vol.235 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 46
    • 0028774041 scopus 로고
    • Solution structure of a peptide fragment of human α-lactalbumin in trifluoroethanol: A model for local structure in the molten globule
    • Smith, L. J., Alexandrescu, A. T., Pitkeathly, M. & Dobson, C. M. (1994). Solution structure of a peptide fragment of human α-lactalbumin in trifluoroethanol: a model for local structure in the molten globule. Structure, 2, 703-712.
    • (1994) Structure , vol.2 , pp. 703-712
    • Smith, L.J.1    Alexandrescu, A.T.2    Pitkeathly, M.3    Dobson, C.M.4
  • 48
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • Soennichsen, F. D., Van Eyk, J. E., Hodges, R. S. & Sykes, B. D. (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry, 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Soennichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 49
    • 0014364651 scopus 로고
    • Protein denaturation. Part A. Characterization of the denatured state
    • Tanford, C. (1968). Protein denaturation. Part A. Characterization of the denatured state. Advan. Protein Chem. 23, 121-217.
    • (1968) Advan. Protein Chem. , vol.23 , pp. 121-217
    • Tanford, C.1
  • 50
    • 0020479083 scopus 로고
    • The structure of melittin. I. Structure determination and partial refinement
    • Terwilliger, T. C. & Eisenberg, D. (1982). The structure of melittin. I. Structure determination and partial refinement. J. Biol. Chem. 257, 6010-6015.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 51
    • 0027484016 scopus 로고
    • Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation
    • Thomas, P. D. & Dill, K. A. (1993). Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation. Protein Sci. 2, 2050-2065.
    • (1993) Protein Sci. , vol.2 , pp. 2050-2065
    • Thomas, P.D.1    Dill, K.A.2
  • 52
    • 0002960761 scopus 로고
    • Stabilization of protein structure by solvent
    • Creighton, T. E., ed., IRL Press, Oxford
    • Timasheff, S. N. & Arakawa, T. (1989). Stabilization of protein structure by solvent. In Protein Structure, A Practical Approach (Creighton, T. E., ed.), pp. 331-345, IRL Press, Oxford.
    • (1989) Protein Structure, A Practical Approach , pp. 331-345
    • Timasheff, S.N.1    Arakawa, T.2
  • 53
    • 0029996091 scopus 로고    scopus 로고
    • Physical, morphological and functional differences between pH 5. 8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ
    • Wood, S. J., Maleeff, B., Hart, T. & Wetzel, R. (1996). Physical, morphological and functional differences between pH 5. 8 and 7.4 aggregates of the Alzheimer's amyloid peptide Aβ. J. Mol. Biol. 256, 870-877.
    • (1996) J. Mol. Biol. , vol.256 , pp. 870-877
    • Wood, S.J.1    Maleeff, B.2    Hart, T.3    Wetzel, R.4


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