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Volumn 1474, Issue 2, 2000, Pages 251-261

End-to-end distance distribution in bradykinin observed by Forster resonance energy transfer

Author keywords

Conformational dynamics; Distance distribution; Forster resonance energy transfer; Ortho aminobenzoyl peptide; Protease fluorescent substrate

Indexed keywords

AMINOBENZOIC ACID; BRADYKININ; BRADYKININ DERIVATIVE; FLUORESCENT DYE; PEPTIDE; PROTEINASE; SOLVENT; TRIFLUOROETHANOL; WATER;

EID: 0034611770     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(00)00004-0     Document Type: Article
Times cited : (33)

References (26)
  • 1
    • 0030607684 scopus 로고    scopus 로고
    • Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IEFTS)
    • Gershkolovich A.A., Kholodovich V.V. Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IEFTS). J. Biochem. Biophys. Methods. 33:1996;135-162.
    • (1996) J. Biochem. Biophys. Methods , vol.33 , pp. 135-162
    • Gershkolovich, A.A.1    Kholodovich, V.V.2
  • 2
    • 0029065458 scopus 로고
    • Fluorometric assays of proteolytic enzymes
    • Knight C.G. Fluorometric assays of proteolytic enzymes. Methods Enzymol. 248:1995;18-34.
    • (1995) Methods Enzymol. , vol.248 , pp. 18-34
    • Knight, C.G.1
  • 3
    • 33646846427 scopus 로고
    • Quantum efficiencies of fluorescence of organic substances: Effect of solvent and concentration of the fluorescent solute
    • Melhuish W.H. Quantum efficiencies of fluorescence of organic substances: effect of solvent and concentration of the fluorescent solute. J. Phys. Chem. 65:1961;229-235.
    • (1961) J. Phys. Chem. , vol.65 , pp. 229-235
    • Melhuish, W.H.1
  • 5
    • 0032572545 scopus 로고    scopus 로고
    • Ortho-aminobenzoic acid as a fluorescent probe for the interaction between peptides and micelles
    • Turchiello R.F., Lamy-Freund M.T., Hirata I.Y., Juliano L., Ito A.S. Ortho-aminobenzoic acid as a fluorescent probe for the interaction between peptides and micelles. Biophys. Chem. 73:1998;217-225.
    • (1998) Biophys. Chem. , vol.73 , pp. 217-225
    • Turchiello, R.F.1    Lamy-Freund, M.T.2    Hirata, I.Y.3    Juliano, L.4    Ito, A.S.5
  • 7
    • 0028788601 scopus 로고
    • Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments
    • Del Nery E., Chagas J.R., Juliano M.A., Prado E.S., Juliano L. Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments. Biochem. J. 312:1995;233-238.
    • (1995) Biochem. J. , vol.312 , pp. 233-238
    • Del Nery, E.1    Chagas, J.R.2    Juliano, M.A.3    Prado, E.S.4    Juliano, L.5
  • 8
    • 0013971012 scopus 로고
    • Abnormal forearm vascular responses in the carcinoid syndrome: The role of kinins and kinin-generating system
    • Mason D.T., Melmon K.L. Abnormal forearm vascular responses in the carcinoid syndrome: the role of kinins and kinin-generating system. J. Clin. Invest. 45:1966;1685-1699.
    • (1966) J. Clin. Invest. , vol.45 , pp. 1685-1699
    • Mason, D.T.1    Melmon, K.L.2
  • 9
    • 0018995127 scopus 로고
    • Pharmacology of bradykinin and related kinins
    • Regoli D., Barabe J. Pharmacology of bradykinin and related kinins. Pharmacol. Rev. 32:1980;1-46.
    • (1980) Pharmacol. Rev. , vol.32 , pp. 1-46
    • Regoli, D.1    Barabe, J.2
  • 10
    • 0028937974 scopus 로고
    • Bradykinin antagonists: Development and applications
    • Stewart J.M. Bradykinin antagonists: development and applications. Biopolymers. 37:1995;143-155.
    • (1995) Biopolymers , vol.37 , pp. 143-155
    • Stewart, J.M.1
  • 12
    • 0015814548 scopus 로고
    • A circular dichroism study of the secondary structure of bradykinin
    • Cann J.R., Stewart J.M., Matsueda G.R. A circular dichroism study of the secondary structure of bradykinin. Biochemistry. 12:1973;3780-3788.
    • (1973) Biochemistry , vol.12 , pp. 3780-3788
    • Cann, J.R.1    Stewart, J.M.2    Matsueda, G.R.3
  • 13
    • 0020360902 scopus 로고
    • Conformational diversity of bradykinin in aqueous solution
    • Denys L., Bothner-By A.A., Fisher G.H., Ryan J.W. Conformational diversity of bradykinin in aqueous solution. Biochemistry. 21:1982;6531-6536.
    • (1982) Biochemistry , vol.21 , pp. 6531-6536
    • Denys, L.1    Bothner-By, A.A.2    Fisher, G.H.3    Ryan, J.W.4
  • 14
    • 0022863482 scopus 로고
    • Interaction of bradykinin with sodium dodecyl sulfate and certain acidic lipids
    • Cann J.R., Vatter A., Vavrek R.J., Stewart J.M. Interaction of bradykinin with sodium dodecyl sulfate and certain acidic lipids. Peptides. 7:1986;1121-1130.
    • (1986) Peptides , vol.7 , pp. 1121-1130
    • Cann, J.R.1    Vatter, A.2    Vavrek, R.J.3    Stewart, J.M.4
  • 15
    • 0025345319 scopus 로고
    • Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics
    • Lee S.C., Russell A.F., Laidig W.D. Three-dimensional structure of bradykinin in SDS micelles. Study using nuclear magnetic resonance, distance geometry, and restrained molecular mechanics and dynamics. Int. J. Pept. Protein Res. 35:1990;367-377.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 367-377
    • Lee, S.C.1    Russell, A.F.2    Laidig, W.D.3
  • 16
    • 0028166870 scopus 로고
    • A CD and NMR study of multiple bradykinin conformations in aqueous trifluoroethanol solutions
    • Cann J.R., Liu X., Stewart J.M., Gera J., Kotovych G. A CD and NMR study of multiple bradykinin conformations in aqueous trifluoroethanol solutions. Biopolymers. 34:1994;869-878.
    • (1994) Biopolymers , vol.34 , pp. 869-878
    • Cann, J.R.1    Liu, X.2    Stewart, J.M.3    Gera, J.4    Kotovych, G.5
  • 17
    • 0032463260 scopus 로고    scopus 로고
    • NMR and CD conformational studies of bradykinin and its agonists and antagonists: Application to receptor binding
    • Kotovych G., Cann J.R., Stewart J.M., Yamamoto H. NMR and CD conformational studies of bradykinin and its agonists and antagonists: application to receptor binding. Biochem. Cell. Biol. 76:1998;257-266.
    • (1998) Biochem. Cell. Biol. , vol.76 , pp. 257-266
    • Kotovych, G.1    Cann, J.R.2    Stewart, J.M.3    Yamamoto, H.4
  • 19
    • 34249758919 scopus 로고
    • Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs
    • Hirata I.Y., Cezari M.H.S., Nakaie C., Boschcov P., Ito A.S., Juliano M., Juliano L. Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett. Peptide Sci. 1:1994;299-308.
    • (1994) Lett. Peptide Sci. , vol.1 , pp. 299-308
    • Hirata, I.Y.1    Cezari, M.H.S.2    Nakaie, C.3    Boschcov, P.4    Ito, A.S.5    Juliano, M.6    Juliano, L.7
  • 20
    • 0020176708 scopus 로고
    • CONTIN: A general purpose constrained regularization program for inverting noisy linear algebraic and integral equations
    • Provencher S.W. CONTIN: a general purpose constrained regularization program for inverting noisy linear algebraic and integral equations. Computer Phys. Commun. 27:1982;229-242.
    • (1982) Computer Phys. Commun. , vol.27 , pp. 229-242
    • Provencher, S.W.1
  • 21
    • 0011751065 scopus 로고
    • The amide-aromatic-ring system. An inherently dissymetric chromophore
    • Siemion I.Z., Wieland Th. The amide-aromatic-ring system. An inherently dissymetric chromophore. Tetrahedron. 33:1977;155-157.
    • (1977) Tetrahedron , vol.33 , pp. 155-157
    • Siemion, I.Z.1    Wieland, Th.2
  • 22
    • 0030870994 scopus 로고    scopus 로고
    • Conformational analysis of galanin using end to end distance distribution observed by Forster resonance energy transfer
    • Kulinski T., Wennerberg A.B., Rigler R., Provencher S.W., Pooga M., Langel U., Bartfai T. Conformational analysis of galanin using end to end distance distribution observed by Forster resonance energy transfer. Eur. Biophys. J. 26:1997;145-154.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 145-154
    • Kulinski, T.1    Wennerberg, A.B.2    Rigler, R.3    Provencher, S.W.4    Pooga, M.5    Langel, U.6    Bartfai, T.7
  • 23
    • 0023108019 scopus 로고
    • Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi
    • Kulinski T., Visser J.W.G., O'Kane D.J., Lee J. Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi. Biochemistry. 26:1987;540-549.
    • (1987) Biochemistry , vol.26 , pp. 540-549
    • Kulinski, T.1    Visser, J.W.G.2    O'Kane, D.J.3    Lee, J.4
  • 24
    • 0016287129 scopus 로고
    • Intramolecular distances determined by energy transfer dependence on orientational freedom of donor and acceptor
    • Dale R.E., Eisinger J. Intramolecular distances determined by energy transfer dependence on orientational freedom of donor and acceptor. Biopolymers. 13:1974;1573-1605.
    • (1974) Biopolymers , vol.13 , pp. 1573-1605
    • Dale, R.E.1    Eisinger, J.2
  • 25
    • 0028439188 scopus 로고
    • NMR and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles
    • Young J.K., Hicks R.P. NMR and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles. Biopolymers. 34:(1):1994;611-623.
    • (1994) Biopolymers , vol.34 , Issue.1 , pp. 611-623
    • Young, J.K.1    Hicks, R.P.2
  • 26
    • 0033152875 scopus 로고    scopus 로고
    • Calcium-binding properties and molecular organization of bradykinin - A solution H-1-NMR study
    • Gaggelli E., D'Amelio N., Maccotta A., Valensin G. Calcium-binding properties and molecular organization of bradykinin - a solution H-1-NMR study. Eur. J. Biochem. 262:1999;268-276.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 268-276
    • Gaggelli, E.1    D'Amelio, N.2    Maccotta, A.3    Valensin, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.