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Volumn 41, Issue 7, 2012, Pages 629-636

NMR studies on the monomer-tetramer transition of melittin in an aqueous solution at high and low temperatures

Author keywords

Cis and trans proline peptide bonds; Cold and heat denaturation; Melittin; Monomer tetramer transition; NMR spectroscopy; Self association

Indexed keywords

MELITTIN;

EID: 84866347612     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-012-0831-7     Document Type: Article
Times cited : (15)

References (30)
  • 2
    • 0020473234 scopus 로고
    • Conformation and aggregation of melittin: Dependence on pH and concentration
    • Bello J, Bello HR, 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
    • 26944481188 scopus 로고    scopus 로고
    • Interfaces and the driving force of hydrophobic assembly
    • Chandler D (2005) Interfaces and the driving force of hydrophobic assembly. Nature 437:640-647
    • (2005) Nature , vol.437 , pp. 640-647
    • Chandler, D.1
  • 5
    • 0025217893 scopus 로고
    • The action of melittin on membranes
    • Dempsey CE (1990) The action of melittin on membranes. Biochim Biophys Acta 1031:143-230
    • (1990) Biochim Biophys Acta , vol.1031 , pp. 143-230
    • Dempsey, C.E.1
  • 7
    • 0018487558 scopus 로고
    • The self-association of melittin and its binding to lipids
    • Faucon JF, Dufourco J, Lussan C (1979) The self-association of melittin and its binding to lipids. FEBS Lett 102:187-190
    • (1979) FEBS Lett , vol.102 , pp. 187-190
    • Faucon, J.F.1    Dufourco, J.2    Lussan, C.3
  • 8
    • 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
  • 9
    • 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
  • 10
    • 0028132243 scopus 로고
    • Thermal unfolding of tetramer melittin: Comparison with the molten golobule state of cytochrome c
    • Hagihara Y, OObatake M, Goto Y (1994) Thermal unfolding of tetramer melittin: comparison with the molten golobule state of cytochrome c. Protein Sci 3:1418-1429
    • (1994) Protein Sci , vol.3 , pp. 1418-1429
    • Hagihara, Y.1    Oobatake, M.2    Goto, Y.3
  • 11
    • 0024357186 scopus 로고
    • Structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by two-dimensional NMR and distant geometry calculations
    • Inagaki F, Shimada I, Kawaguchi K, Hirano M, Terasawa I, Ikura T, Go N (1989) Structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by two-dimensional NMR and distant geometry calculations. Biochemistry 28: 5985-5991
    • (1989) Biochemistry , vol.28 , pp. 5985-5991
    • Inagaki, F.1    Shimada, I.2    Kawaguchi, K.3    Hirano, M.4    Terasawa, I.5    Ikura, T.6    Go, N.7
  • 12
    • 0032532218 scopus 로고    scopus 로고
    • The structure of the melittin at different temperatures: An NOE-based calculation with chemical shift refinement
    • Iwadate M, Asakura T, Williamson MP (1998) The structure of the melittin at different temperatures: an NOE-based calculation with chemical shift refinement. Eur J Biochem 257:479-487
    • (1998) Eur J Biochem , vol.257 , pp. 479-487
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 13
    • 63449104638 scopus 로고    scopus 로고
    • Importance of translational entropy of water in biological self-assembly processes like protein folding
    • Kinoshita M (2009) Importance of translational entropy of water in biological self-assembly processes like protein folding. Int J Mol Sci 10:1064-1080
    • (2009) Int J Mol Sci , vol.10 , pp. 1064-1080
    • Kinoshita, M.1
  • 14
    • 0019332428 scopus 로고
    • High-resolution 1HNMR studies of monomeric melittin in aqueous solution
    • Lauterwein J, Brown LR, Wüthrich K (1980) High-resolution 1HNMR studies of monomeric melittin in aqueous solution. Biochim Biophys Acta 622:219-230
    • (1980) Biochim Biophys Acta , vol.622 , pp. 219-230
    • Lauterwein, J.1    Brown, L.R.2    Wüthrich, K.3
  • 16
    • 79951669244 scopus 로고    scopus 로고
    • Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR
    • Miura Y (2011) Helix conformation of a small peptide melittin in a methanol-water mixed solvent studied by NMR. Protein Pept Lett 18:318-326
    • (2011) Protein Pept Lett , vol.18 , pp. 318-326
    • Miura, Y.1
  • 17
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy KP, Privalov PL, Gill SJ (1990) Common features of protein unfolding and dissolution of hydrophobic compounds. Science 247:559-561
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 18
    • 69149100640 scopus 로고    scopus 로고
    • Solvation in protein (un)folding of melittin tetramer-monomer transition
    • Othon CM, Kwon O, Lin MM, Zewail AH (2009) Solvation in protein (un)folding of melittin tetramer-monomer transition. PNAS 106:12593-12598
    • (2009) PNAS , vol.106 , pp. 12593-12598
    • Othon, C.M.1    Kwon, O.2    Lin, M.M.3    Zewail, A.H.4
  • 20
    • 0002693020 scopus 로고
    • Physical basis of the stability of the folded conformations of proteins
    • Creighton TE (ed), Freeman WE and Company, New York
    • Privalov PL (1992) Physical basis of the stability of the folded conformations of proteins. In: Creighton TE (ed) Protein folding. Freeman WE and Company, New York, pp 83-126
    • (1992) Protein Folding , pp. 83-126
    • Privalov, P.L.1
  • 21
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov PL, Gill SJ (1988) Stability of protein structure and hydrophobic interaction. Adv Protein Chem 39:191-234
    • (1988) Adv Protein Chem , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 22
    • 25444458922 scopus 로고    scopus 로고
    • Ultra hydration dynamics in melittin folding and aggregation: Helix formation and tetramer self-assembly
    • Qiu W, Zhang L, Kao Y, Lu W, Li T, Kim J, Sollenberger GM, Wang L, Zhong D (2005) Ultra hydration dynamics in melittin folding and aggregation: helix formation and tetramer self-assembly. J Phys Chem B 109:16901-16910
    • (2005) J Phys Chem B , vol.109 , pp. 16901-16910
    • Qiu, W.1    Zhang, L.2    Kao, Y.3    Lu, W.4    Li, T.5    Kim, J.6    Sollenberger, G.M.7    Wang, L.8    Zhong, D.9
  • 23
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction
    • Quay SC, Condie CC (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
  • 24
    • 0026317408 scopus 로고
    • Conformation changes in melittin upon complexation with an anionic melittin analog
    • Ramalingam K, Bello J, Aimoto S (1991) Conformation changes in melittin upon complexation with an anionic melittin analog. FEBS Lett 295:200-202
    • (1991) FEBS Lett , vol.295 , pp. 200-202
    • Ramalingam, K.1    Bello, J.2    Aimoto, S.3
  • 25
    • 0026910992 scopus 로고
    • Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength, and temperature - Models for protein folding and halophilic proteins
    • Ramalingam K, Aimoto S, Bello J (1992) Conformational studies of anionic melittin analogues: effect of peptide concentration, pH, ionic strength, and temperature - models for protein folding and halophilic proteins. Biopolymers 32:981-992
    • (1992) Biopolymers , vol.32 , pp. 981-992
    • Ramalingam, K.1    Aimoto, S.2    Bello, J.3
  • 26
    • 0038762371 scopus 로고
    • Does dimeric melittin occur in aqueous solutions?
    • Schubert D, Pappert G, Boss K (1985) Does dimeric melittin occur in aqueous solutions? Biophys J 48:327-329
    • (1985) Biophys J , vol.48 , pp. 327-329
    • Schubert, D.1    Pappert, G.2    Boss, K.3
  • 27
    • 0027754099 scopus 로고
    • Structural and thermodynamic aspects of the hydrophobic effect
    • Soda K (1993) Structural and thermodynamic aspects of the hydrophobic effect. Adv Biophys 29:1-54
    • (1993) Adv Biophys , vol.29 , pp. 1-54
    • Soda, K.1
  • 28
    • 0037076337 scopus 로고    scopus 로고
    • Drying-induced hydrophobic polymer collapse
    • ten Wolde PR, Chandler D (2002) Drying-induced hydrophobic polymer collapse. Proc Natl Acad Sci USA 99:6539-6543
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6539-6543
    • Ten Wolde, P.R.1    Chandler, D.2
  • 29
    • 0027056421 scopus 로고
    • Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding
    • Wilcox W, Eisenberg D (1992) Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding. Protein Sci 1:641-653
    • (1992) Protein Sci , vol.1 , pp. 641-653
    • Wilcox, W.1    Eisenberg, D.2
  • 30
    • 65349114143 scopus 로고    scopus 로고
    • Hydrophobicity at low temperatures and cold denaturation of a protein
    • Yoshidome T, Kinoshita M (2009) Hydrophobicity at low temperatures and cold denaturation of a protein. Phys Rev E 79:030905(R)
    • (2009) Phys Rev e , vol.79
    • Yoshidome, T.1    Kinoshita, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.