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Volumn 257, Issue 2, 1998, Pages 479-487

The structure of the melittin tetramer at different temperatures: An NOE-based calculation with chemical shift refinement

Author keywords

Chemical shift; Melittin tetramer; NOE; Ring current effect; Temperature dependence

Indexed keywords

BEE VENOM; DIMER; MELITTIN; MONOMER; SODIUM DIHYDROGEN PHOSPHATE; TETRAMER; WATER;

EID: 0032532218     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570479.x     Document Type: Article
Times cited : (44)

References (30)
  • 1
    • 0022798958 scopus 로고
    • The structure of melittin in membranes
    • Vogel, H. & Jähnig, F. (1986) The structure of melittin in membranes, Biophys. J. 50, 573-582.
    • (1986) Biophys. J. , vol.50 , pp. 573-582
    • Vogel, H.1    Jähnig, F.2
  • 2
    • 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
  • 8
    • 0024357186 scopus 로고
    • Structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by two-dimensional NMR and distance 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 distance 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
  • 9
    • 0025978713 scopus 로고
    • Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by two-dimensional NMR and distance geometry calculations
    • Ikura, T., Go, N. & Inagaki, F. (1991) Refined structure of melittin bound to perdeuterated dodecylphosphocholine micelles as studied by two-dimensional NMR and distance geometry calculations, Proteins Struct. Funct. Genet. 9, 81-89.
    • (1991) Proteins Struct. Funct. Genet. , vol.9 , pp. 81-89
    • Ikura, T.1    Go, N.2    Inagaki, F.3
  • 10
    • 0028022950 scopus 로고
    • Vesicle-bound conformation of melittin: Transferred nuclear Overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholine vesicles
    • Okada, A., Wakamatsu, K., Miyazawa, T. & Higashijima, T. (1994) Vesicle-bound conformation of melittin: Transferred nuclear Overhauser enhancement analysis in the presence of perdeuterated phosphatidylcholine vesicles, Biochemistry 33, 9438-9446.
    • (1994) Biochemistry , vol.33 , pp. 9438-9446
    • Okada, A.1    Wakamatsu, K.2    Miyazawa, T.3    Higashijima, T.4
  • 11
    • 0020479083 scopus 로고
    • The structure of melittin. 1. Structure determination and partial refinement
    • Terwilliger, T. C. & Fisenberg, D. (1982) The structure of melittin. 1. Structure determination and partial refinement, J. Biol. Chem. 257, 6010-6015.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Fisenberg, D.2
  • 12
    • 0020479123 scopus 로고
    • The structure of melittin. 2. Interpretation of the structure
    • Terwilliger, T. C. & Eisenberg, D. (1982) The structure of melittin. 2. Interpretation of the structure, J. Biol. Chem. 257, 6016-6022.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 13
    • 0028132243 scopus 로고
    • Thermal unfolding of tetrameric melittin: Comparison with the molten globule state of cytochrome c
    • Hagihara, Y., Oobatake, M. & Goto, Y. (1994) Thermal unfolding of tetrameric melittin: comparison with the molten globule 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
  • 14
    • 0028921486 scopus 로고
    • Circular dichroism and fluorescence studies on melittin: Effects of C-terminal modifications on tetramer formation and binding to phospholipid vesicles
    • van Veen, M., Georgiou, G. N., Drake, A. F. & Cherry, R. J. (1995) Circular dichroism and fluorescence studies on melittin: effects of C-terminal modifications on tetramer formation and binding to phospholipid vesicles, Biochem. J. 305, 785-790.
    • (1995) Biochem. J. , vol.305 , pp. 785-790
    • Van Veen, M.1    Georgiou, G.N.2    Drake, A.F.3    Cherry, R.J.4
  • 15
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerisation
    • Runnels, L. W. & Scarlata, S. F. (1995) Theory and application of fluorescence homotransfer to melittin oligomerisation, Biophys. J. 69, 1569-1583.
    • (1995) Biophys. J. , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 17
    • 45949117843 scopus 로고
    • A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data
    • Nilges, M., Clore, G. M & Gronenborn, A. M. (1987) A simple method for delineating well-defined and variable regions in protein structures determined from interproton distance data, FEBS Letts. 219, 11-16.
    • (1987) FEBS Letts. , vol.219 , pp. 11-16
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 18
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J. & Thornton, J. M. (1988) Helix geometry in proteins, J. Mol. Biol. 201, 601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 20
    • 0026621044 scopus 로고
    • A method for the calculation of protein α-CH chemical shifts
    • Williamson, M. P., Asakura, T., Nakamura, E. & Demura, M. (1992) A method for the calculation of protein α-CH chemical shifts, J. Biomol. NMR 2, 83-98.
    • (1992) J. Biomol. NMR , vol.2 , pp. 83-98
    • Williamson, M.P.1    Asakura, T.2    Nakamura, E.3    Demura, M.4
  • 21
    • 0028988451 scopus 로고
    • 1H-NMR chemical shifts to measure the quality of protein structures
    • 1H-NMR chemical shifts to measure the quality of protein structures, J. Mol. Biol. 247, 541-546.
    • (1995) J. Mol. Biol. , vol.247 , pp. 541-546
    • Williamson, M.P.1    Kikuchi, J.2    Asakura, T.3
  • 22
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance obser-vation of short proton-proton distances
    • Wüthrich, K., Billeter, M. & Braun, W. (1984) Polypeptide secondary structure determination by nuclear magnetic resonance obser-vation of short proton-proton distances, J. Mol. Biol. 180, 715-740.
    • (1984) J. Mol. Biol. , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 23
    • 0000958373 scopus 로고
    • Application of ring current calculations to the proton NMR of proteins and transfer RNA
    • Perkins, S. J. (1982) Application of ring current calculations to the proton NMR of proteins and transfer RNA, Biol. Magn. Reson. 4, 193-336.
    • (1982) Biol. Magn. Reson. , vol.4 , pp. 193-336
    • Perkins, S.J.1
  • 24
    • 0028127028 scopus 로고
    • Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints
    • Ösapay, K., Thériault, Y., Wright, P. E. & Case, D. A. (1994) Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints, J. Mol. Biol. 244, 183-197.
    • (1994) J. Mol. Biol. , vol.244 , pp. 183-197
    • Ösapay, K.1    Thériault, Y.2    Wright, P.E.3    Case, D.A.4
  • 25
    • 0028900809 scopus 로고
    • Protein structure refinement based on paramagnetic NMR shifts: Applications to wild-type and mutant forms of cytochrome c
    • Gochin, M. & Roder, H. (1995) Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c, Protein Sci. 4, 296-305.
    • (1995) Protein Sci. , vol.4 , pp. 296-305
    • Gochin, M.1    Roder, H.2
  • 26
    • 0030954693 scopus 로고    scopus 로고
    • Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins
    • Banci, L., Bertini, I., Savellini, G. G., Romagnoli, A., Turano, P., Cremonini, M. A., Luchinat, C. & Gray, H. B. (1997) Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins, Proteins Struct. Funct. Genet. 29, 68-76.
    • (1997) Proteins Struct. Funct. Genet. , vol.29 , pp. 68-76
    • Banci, L.1    Bertini, I.2    Savellini, G.G.3    Romagnoli, A.4    Turano, P.5    Cremonini, M.A.6    Luchinat, C.7    Gray, H.B.8
  • 27
    • 0029314335 scopus 로고
    • The impact of direct refinement against proton chemical shifts on protein structure determination by NMR
    • Kuszewski, J., Gronenborn, A. M. & Clore, G. M. (1995) The impact of direct refinement against proton chemical shifts on protein structure determination by NMR, J. Magn. Reson. Ser. B 107, 293-297.
    • (1995) J. Magn. Reson. Ser. B , vol.107 , pp. 293-297
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 30
    • 0031090730 scopus 로고    scopus 로고
    • Constrained refinement based on NOE and chemical shift information: The monomer form of arginine-vasopressin-like insect factor
    • Busetta, B. & Picard, P. (1997) Constrained refinement based on NOE and chemical shift information: the monomer form of arginine-vasopressin-like insect factor, J. Pept. Sci. 3, 133-140.
    • (1997) J. Pept. Sci. , vol.3 , pp. 133-140
    • Busetta, B.1    Picard, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.