메뉴 건너뛰기




Volumn 237, Issue 3, 1996, Pages 619-628

Conformational transitions within the calmodulin-binding site of Bordetella pertussis adenylate cyclase studied by time-resolved fluorescence of Trp242 and circular dichroism

Author keywords

Adenylate cyclase; Bordetella pertussis; Calmodulin binding; Fluorescence properties; Peptide

Indexed keywords

ADENYLATE CYCLASE; CALMODULIN;

EID: 0029934149     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0619p.x     Document Type: Article
Times cited : (11)

References (70)
  • 1
    • 0023357309 scopus 로고
    • Interpretation of fluorescence decays in proteins using continuous lifetime distributions
    • Alcala, J. R., Gratton, E. & Prendergast, F. G. (1987) Interpretation of fluorescence decays in proteins using continuous lifetime distributions, Biophys. J. 51, 925-936.
    • (1987) Biophys. J. , vol.51 , pp. 925-936
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 2
    • 0016355828 scopus 로고
    • The interaction of protein functional groups with indole chromophore. I. Imidazole group
    • Bushueva, T. L., Busel, E. P., Bushueva, V. N. & Burstein, E. A. (1974) The interaction of protein functional groups with indole chromophore. I. Imidazole group, Stud. Biophys. 44, 129-139.
    • (1974) Stud. Biophys. , vol.44 , pp. 129-139
    • Bushueva, T.L.1    Busel, E.P.2    Bushueva, V.N.3    Burstein, E.A.4
  • 3
    • 0016775598 scopus 로고
    • The interaction of protein functional groups with indole chromophore. III. Amide, amine and thiol groups
    • Bushueva, T. L., Busel, E. P. & Burstein, E. A. (1975) The interaction of protein functional groups with indole chromophore. III. Amide, amine and thiol groups, Stud. Biophys. 52, 41-52.
    • (1975) Stud. Biophys. , vol.52 , pp. 41-52
    • Bushueva, T.L.1    Busel, E.P.2    Burstein, E.A.3
  • 4
    • 0027395160 scopus 로고
    • Cooperative phenomena in binding and activation of Bordetella pertussis adenylate cyclase by calmodulin
    • Bouhss, A., Krin, E., Munier, H., Gilles, A.-M., Danchin, A., Glaser, P. & Bârzu, O. (1993) Cooperative phenomena in binding and activation of Bordetella pertussis adenylate cyclase by calmodulin, J. Biol. Chem. 268, 1690-1694
    • (1993) J. Biol. Chem. , vol.268 , pp. 1690-1694
    • Bouhss, A.1    Krin, E.2    Munier, H.3    Gilles, A.-M.4    Danchin, A.5    Glaser, P.6    Bârzu, O.7
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0028672799 scopus 로고
    • Maximum entropy method of data analysis in time-resolved spectroscopy
    • Brochon, J. C. (1994) Maximum entropy method of data analysis in time-resolved spectroscopy. Methods Enzymol. 240, 262-311.
    • (1994) Methods Enzymol. , vol.240 , pp. 262-311
    • Brochon, J.C.1
  • 7
    • 0025885581 scopus 로고
    • Fluorescence analysis of calmodulin mutants containing tryptophan: Conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II
    • Chabbert, M., Lukas, T. J., Watterson, D. M., Axelsen, P. H. & Prendergast. F. G. (1991) Fluorescence analysis of calmodulin mutants containing tryptophan: conformational changes induced by calmodulin-binding peptides from myosin light chain kinase and protein kinase II. Biochemistry 30, 7615-7630.
    • (1991) Biochemistry , vol.30 , pp. 7615-7630
    • Chabbert, M.1    Lukas, T.J.2    Watterson, D.M.3    Axelsen, P.H.4    Prendergast, F.G.5
  • 8
    • 0025830305 scopus 로고
    • Fluorescence of tryptophan dipeptides: Correlations with the retamer model
    • Chen, R. F., Knutson, J. R., Ziffer, H. & Porter, D. (1991) Fluorescence of tryptophan dipeptides: correlations with the retamer model. Biochemistry 30, 5184-5195.
    • (1991) Biochemistry , vol.30 , pp. 5184-5195
    • Chen, R.F.1    Knutson, J.R.2    Ziffer, H.3    Porter, D.4
  • 10
    • 0019973678 scopus 로고
    • Phagocyte impotence caused by an invasive bacterial adenylate cyclase
    • Confer, D. L. & Eaton, J. W. (1982) Phagocyte impotence caused by an invasive bacterial adenylate cyclase. Science 217, 948-950.
    • (1982) Science , vol.217 , pp. 948-950
    • Confer, D.L.1    Eaton, J.W.2
  • 11
    • 0014209817 scopus 로고
    • Fluorescence and protein structure. X. Reappraisal of solvent and structural effects
    • Cowgill, R. W. (1967) Fluorescence and protein structure. X. Reappraisal of solvent and structural effects, Biochim. Biophys. Acta 133, 6-18.
    • (1967) Biochim. Biophys. Acta , vol.133 , pp. 6-18
    • Cowgill, R.W.1
  • 12
    • 0028965080 scopus 로고
    • Calmodulin binding of a peptide derived from the regulatory domain of Bordetella pertussis adenylate cyclase
    • Craescu, C. T., Bouhss, A., Mispelter, J., Diesis, E., Popescu, A., Chiriac, M. & Bârzu, O. (1995) Calmodulin binding of a peptide derived from the regulatory domain of Bordetella pertussis adenylate cyclase, J. Biol. Chem. 270, 7088-7096.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7088-7096
    • Craescu, C.T.1    Bouhss, A.2    Mispelter, J.3    Diesis, E.4    Popescu, A.5    Chiriac, M.6    Bârzu, O.7
  • 13
    • 0024341971 scopus 로고
    • The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin
    • Dasgupta, M., Honeycutt, T. & Blumenthal, D. K. (1989) The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin, J. Biol. Chem. 264, 17 156-17 163.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17156-17163
    • Dasgupta, M.1    Honeycutt, T.2    Blumenthal, D.K.3
  • 14
    • 0015242342 scopus 로고
    • Effect of solvent upon the fluorescence decay of indole
    • De Lauder, W. B. & Wahl, P. (1971) Effect of solvent upon the fluorescence decay of indole, Biochim. Biophys. Acta 243, 153-163.
    • (1971) Biochim. Biophys. Acta , vol.243 , pp. 153-163
    • De Lauder, W.B.1    Wahl, P.2
  • 15
    • 0029215767 scopus 로고
    • On the photophysics of indole in polar environments
    • Laser applications in life sciences (Apanasevich, P. A., Koroteev, N. I., Kruglik, S. G., Zadkov, V. N., eds)
    • Demchenko, A. P., Gallay, J. & Vincent, M. (1995) On the photophysics of indole in polar environments, in Laser applications in life sciences (Apanasevich, P. A., Koroteev, N. I., Kruglik, S. G., Zadkov, V. N., eds) SPIE Proceedings 2370, 693-699.
    • (1995) SPIE Proceedings 2370 , pp. 693-699
    • Demchenko, A.P.1    Gallay, J.2    Vincent, M.3
  • 16
    • 0017298143 scopus 로고
    • Dynamic interactions of fluorescence probes with the solvent environment
    • De Toma, R. P., Easter, J. H. & Brand, L. (1976) Dynamic interactions of fluorescence probes with the solvent environment. J. Am. Chem. Soc. 98, 5001-5007.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 5001-5007
    • De Toma, R.P.1    Easter, J.H.2    Brand, L.3
  • 17
    • 33847804116 scopus 로고
    • Study of the conformation in the excited state of two tryptophanyl diketopiperazines
    • Donzel, B., Gauduchon, P. & Wahl, P. (1974) Study of the conformation in the excited state of two tryptophanyl diketopiperazines, J. Am. Chem. Soc. 96, 801-808.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 801-808
    • Donzel, B.1    Gauduchon, P.2    Wahl, P.3
  • 18
    • 0343312277 scopus 로고
    • Evidences for excited state reactions of indole derivatives in alcoholic solvents, reverse micelles and proteins
    • Time-resolved laser spectroscopy in biochemistry (Lakowicz, J. R., ed.)
    • Gallay, J., Vekshin, N., Sopkova, J. & Vincent, M. (1994) Evidences for excited state reactions of indole derivatives in alcoholic solvents, reverse micelles and proteins, in Time-resolved laser spectroscopy in biochemistry (Lakowicz, J. R., ed.) SPIE Proceeding 2170, vol. IV, pp. 390-400.
    • (1994) SPIE Proceeding 2170 , vol.4 , pp. 390-400
    • Gallay, J.1    Vekshin, N.2    Sopkova, J.3    Vincent, M.4
  • 20
    • 0025083125 scopus 로고
    • Intrinsic fluorescence of a truncated Bordetella pertussis adenylate cyclase expressed in Escherichia coli
    • Gilles, A.-M., Munier, H., Rose, T., Glaser, P., Krin, E., Danchin, A., Pellecuer, C. & Bârzu, O. (1990) Intrinsic fluorescence of a truncated Bordetella pertussis adenylate cyclase expressed in Escherichia coli, Biochemistry 29, 8126-8130.
    • (1990) Biochemistry , vol.29 , pp. 8126-8130
    • Gilles, A.-M.1    Munier, H.2    Rose, T.3    Glaser, P.4    Krin, E.5    Danchin, A.6    Pellecuer, C.7    Bârzu, O.8
  • 21
    • 0023674373 scopus 로고
    • The calmodulin-sensitive adenylate cyclase of Bordetella pertussis: Cloning and expression in Escherichia coli
    • Glaser, P., Ladant, D., Sezer, O., Pichot, F., Ullmann, A. & Danchin, A. (1988a) The calmodulin-sensitive adenylate cyclase of Bordetella pertussis: cloning and expression in Escherichia coli, Mol. Microbiol. 2, 19-30.
    • (1988) Mol. Microbiol. , vol.2 , pp. 19-30
    • Glaser, P.1    Ladant, D.2    Sezer, O.3    Pichot, F.4    Ullmann, A.5    Danchin, A.6
  • 22
    • 0024195829 scopus 로고
    • Secretion of cyclolysin, the calmodulin-sensitive adenylate-cyclase-haemolysin bifunctional protein of Bordetella pertussis
    • Glaser, P., Sakamoto, H., Bellalou, J., Ullmann, A. & Danchin, A. (1988b) Secretion of cyclolysin, the calmodulin-sensitive adenylate-cyclase-haemolysin bifunctional protein of Bordetella pertussis, EMBO J. 7, 3997-4004.
    • (1988) EMBO J. , vol.7 , pp. 3997-4004
    • Glaser, P.1    Sakamoto, H.2    Bellalou, J.3    Ullmann, A.4    Danchin, A.5
  • 23
    • 0024447834 scopus 로고
    • Identification of residues essential for catalysis and binding of calmodulin in Bordetella pertussis adenylate cyclase by site-directed mutagenesis
    • Glaser, P., Elmaoglou-Lazaridou, A., Krin, E., Ladant, D., Bârzu, O. & Danchin, A. (1989) Identification of residues essential for catalysis and binding of calmodulin in Bordetella pertussis adenylate cyclase by site-directed mutagenesis. EMBO J. 8, 967-972.
    • (1989) EMBO J. , vol.8 , pp. 967-972
    • Glaser, P.1    Elmaoglou-Lazaridou, A.2    Krin, E.3    Ladant, D.4    Bârzu, O.5    Danchin, A.6
  • 24
    • 0025817116 scopus 로고
    • Functional consequences of single amino acid substitutions in calmodulin-activated adenylate cyclase of Bordetella pertussis
    • Glaser, P., Munier, H., Gilles, A.-M., Krin, E., Porumb, T., Bârzu, O., Sarfati, R. S., Pellecuer, C. & Danchin, A. (1991) Functional consequences of single amino acid substitutions in calmodulin-activated adenylate cyclase of Bordetella pertussis, EMBO J. 10, 1683-1688.
    • (1991) EMBO J. , vol.10 , pp. 1683-1688
    • Glaser, P.1    Munier, H.2    Gilles, A.-M.3    Krin, E.4    Porumb, T.5    Bârzu, O.6    Sarfati, R.S.7    Pellecuer, C.8    Danchin, A.9
  • 25
    • 0023914447 scopus 로고
    • Affinity-based chromatography utilizing genetically engineered proteins: Interaction of Bordetella pertussis adenylate cyclase with calmodulin
    • Haiech, J., Predeleanu, R., Watterson, M. D., Ladant, D., Bellalou, J., Ullmann, A. & Bârzu, O. (1988) Affinity-based chromatography utilizing genetically engineered proteins: interaction of Bordetella pertussis adenylate cyclase with calmodulin. J. Biol. Chem. 263, 4259-4262.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4259-4262
    • Haiech, J.1    Predeleanu, R.2    Watterson, M.D.3    Ladant, D.4    Bellalou, J.5    Ullmann, A.6    Bârzu, O.7
  • 26
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B. & Bax, A. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR, Science 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 27
    • 0017729574 scopus 로고
    • A theory of fluorescence polarization decay in membranes
    • Kinosita, K. Jr, Kawato, S. & Ikegami, A. (1977) A theory of fluorescence polarization decay in membranes, Biophys. J. 20, 289-305.
    • (1977) Biophys. J. , vol.20 , pp. 289-305
    • Kinosita Jr., K.1    Kawato, S.2    Ikegami, A.3
  • 28
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D. & Zakour, R. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
    • (1985) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 29
    • 0023030052 scopus 로고
    • Bordetella pertussis adenylate cyclase: Purification, characterization and radioimmunoassay
    • Ladant, D., Brézin, C., Alonso, J.-M., Crenon, I. & Guiso, N. (1986) Bordetella pertussis adenylate cyclase: purification, characterization and radioimmunoassay. J. Biol. Chem. 261, 16264-16269.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16264-16269
    • Ladant, D.1    Brézin, C.2    Alonso, J.-M.3    Crenon, I.4    Guiso, N.5
  • 30
    • 0024513349 scopus 로고
    • Characterization of the calmodulin-binding and of the catalytic domain of Bordetella pertussis adenylate cyclase
    • Ladant, D., Michelson, S., Sarfati, R., Gilles, A.-M., Predeleanu, R. & Bârzu, O. (1989) Characterization of the calmodulin-binding and of the catalytic domain of Bordetella pertussis adenylate cyclase. J. Biol. Chem. 264, 4015-4020.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4015-4020
    • Ladant, D.1    Michelson, S.2    Sarfati, R.3    Gilles, A.-M.4    Predeleanu, R.5    Bârzu, O.6
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0019320690 scopus 로고
    • Dipolar relaxation in proteins on the nanosecond time scale observed by wavelength-resolved phase fluorimetry of tryptophan fluorescence
    • Lakowicz, J. R. & Cherek, H. (1980) Dipolar relaxation in proteins on the nanosecond time scale observed by wavelength-resolved phase fluorimetry of tryptophan fluorescence. J. Biol. Chem. 255, 831-834.
    • (1980) J. Biol. Chem. , vol.255 , pp. 831-834
    • Lakowicz, J.R.1    Cherek, H.2
  • 33
    • 0000677865 scopus 로고
    • Indole solvatochromism revisited
    • Lami, H. & Glasser, N. (1986) Indole solvatochromism revisited, J. Chem. Phys. 84, 597-604.
    • (1986) J. Chem. Phys. , vol.84 , pp. 597-604
    • Lami, H.1    Glasser, N.2
  • 34
    • 0001464493 scopus 로고
    • Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method
    • Livesey, A. K. & Brochon, J.-C. (1987) Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method. Biophys. J. 52, 693-706.
    • (1987) Biophys. J. , vol.52 , pp. 693-706
    • Livesey, A.K.1    Brochon, J.-C.2
  • 35
    • 0001002661 scopus 로고
    • Maximum entropy-analysis of quasielastic light scattering from colloidal dispersions
    • Livesey, A. K., Licinio, P. & Delaye, M. (1986) Maximum entropy-analysis of quasielastic light scattering from colloidal dispersions. J. Chem. Phys. 84, 5102-5107.
    • (1986) J. Chem. Phys. , vol.84 , pp. 5102-5107
    • Livesey, A.K.1    Licinio, P.2    Delaye, M.3
  • 36
    • 0000185769 scopus 로고
    • Status of indole photochemistry with special references to biological applications
    • Lumry, R. & Hershberger, M. (1978) Status of indole photochemistry with special references to biological applications. Photochem. Photobiol. 27, 819-840.
    • (1978) Photochem. Photobiol. , vol.27 , pp. 819-840
    • Lumry, R.1    Hershberger, M.2
  • 37
    • 0026439297 scopus 로고
    • Deuterium isotope effects in constrained tryptophan derivatives implication for Trp
    • McMahon, L. P., Colucci, W. J., McLaughlin, M. L. & Barkley, M. D. (1992) Deuterium isotope effects in constrained tryptophan derivatives implication for Trp, J. Am. Chem. Soc. 114, 8442-8448.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8442-8448
    • McMahon, L.P.1    Colucci, W.J.2    McLaughlin, M.L.3    Barkley, M.D.4
  • 38
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex
    • Meador, W. E., Means, A. R. & Quiocho, F. A. (1992) Target enzyme recognition by calmodulin: 2.4 Å structure of a calmodulin-peptide complex. Science 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 39
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador, W. E., Means, A. R. & Quiocho, F. A. (1993) Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262, 1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 40
    • 0027234756 scopus 로고
    • Calmodulin-activated bacterial adenylate cyclases as virulence factors
    • Mock, M. & Ullmann, A. (1993) Calmodulin-activated bacterial adenylate cyclases as virulence factors. Trends Microbiol. 1, 187-192.
    • (1993) Trends Microbiol. , vol.1 , pp. 187-192
    • Mock, M.1    Ullmann, A.2
  • 41
    • 0042132504 scopus 로고
    • Subnanosecond time-resolved emission spectroscopy of 1-methyl and 2,3-dimethyl indole in n-butanol
    • Montoro, T. Chabbert, M., Tyrzyk, J. & Lami, H. (1988) Subnanosecond time-resolved emission spectroscopy of 1-methyl and 2,3-dimethyl indole in n-butanol, J. Chem. Phys. 89, 2712-2719.
    • (1988) J. Chem. Phys. , vol.89 , pp. 2712-2719
    • Montoro, T.1    Chabbert, M.2    Tyrzyk, J.3    Lami, H.4
  • 42
    • 0026027810 scopus 로고
    • Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase
    • Munier, H., Gilles, A.-M., Glaser, P., Krin, E., Danchin, A., Sarfati, R. S. & Bârzu, O. (1991) Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adenylate cyclase, Eur. J. Biochem. 196, 469-474.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 469-474
    • Munier, H.1    Gilles, A.-M.2    Glaser, P.3    Krin, E.4    Danchin, A.5    Sarfati, R.S.6    Bârzu, O.7
  • 43
    • 0029009033 scopus 로고
    • Structural characterization by nuclear magnetic resonance spectroscopy of a genetically engineered high-affinity calmodulin-binding peptide derived from Bordetella pertussis adenylate cyclase
    • Munier, H., Bouhss, A., Gilles, A.-M., Palibroda, N., Bârzu, O., Mispelter, J. & Craescu, C. T. (1995) Structural characterization by nuclear magnetic resonance spectroscopy of a genetically engineered high-affinity calmodulin-binding peptide derived from Bordetella pertussis adenylate cyclase, Arch. Biochem. Biophys. 320, 224-235.
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 224-235
    • Munier, H.1    Bouhss, A.2    Gilles, A.-M.3    Palibroda, N.4    Bârzu, O.5    Mispelter, J.6    Craescu, C.T.7
  • 44
    • 0022804939 scopus 로고
    • Stabilization of the ribonuclease S-pcptide α-helix by trifluoroethanol
    • Nelson, J. W. & Kallenbach, N. R. (1986) Stabilization of the ribonuclease S-pcptide α-helix by trifluoroethanol, Proteins 1, 211-217.
    • (1986) Proteins , vol.1 , pp. 211-217
    • Nelson, J.W.1    Kallenbach, N.R.2
  • 45
    • 0023226103 scopus 로고
    • Fluorescence properties of calmodulin-binding peptides reflect α-helical periodicity
    • O'Neil, K. T., Wolfe, H. R. Jr, Erickson-Viitanen, S. & DeGrado, W. F. (1987) Fluorescence properties of calmodulin-binding peptides reflect α-helical periodicity, Science 236, 1454-1456.
    • (1987) Science , vol.236 , pp. 1454-1456
    • O'Neil, K.T.1    Wolfe Jr., H.R.2    Erickson-Viitanen, S.3    DeGrado, W.F.4
  • 46
    • 0024806242 scopus 로고
    • The interaction of calmodulin with fluorescent and photoreactive model peptides: Evidence for a short interdomain separation
    • O'Neil, K. T. & DeGrado, W. F. (1989) The interaction of calmodulin with fluorescent and photoreactive model peptides: evidence for a short interdomain separation, Proteins 6, 284-293.
    • (1989) Proteins , vol.6 , pp. 284-293
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 47
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic α-helices
    • O'Neil, K. T. & DeGrado, W. F. (1990) How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices, Trends Biochem. Sci. 15, 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 48
    • 0020763601 scopus 로고
    • On the origin of the nonexponential fluorescence decay of tryptophan and its derivatives
    • Petrich, J. W., Chang, M. C., McDonald, D. M. & Fleming, G. R. (1983) On the origin of the nonexponential fluorescence decay of tryptophan and its derivatives, J. Am. Chem. Soc. 105, 3824-3832.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.M.3    Fleming, G.R.4
  • 50
    • 0026013584 scopus 로고
    • NMR and circular dichroism studies on the solution conformation of a synthetic peptide derived from the calmodulin-binding domain of Bordetella pertussis adenylate cyclase
    • Prêcheur, B., Siffert, O., Bârzu, O. & Craescu, C. T. (1991) NMR and circular dichroism studies on the solution conformation of a synthetic peptide derived from the calmodulin-binding domain of Bordetella pertussis adenylate cyclase, Eur. J Biochem. 196, 67-72.
    • (1991) Eur. J Biochem. , vol.196 , pp. 67-72
    • Prêcheur, B.1    Siffert, O.2    Bârzu, O.3    Craescu, C.T.4
  • 52
    • 0000611161 scopus 로고
    • Inter- and intramolecular quenching of indole by carbonyl compounds
    • Ricci, R. W. & Nesta, J. M. (1976) Inter- and intramolecular quenching of indole by carbonyl compounds, J. Phys. Chem. 80, 974-980.
    • (1976) J. Phys. Chem. , vol.80 , pp. 974-980
    • Ricci, R.W.1    Nesta, J.M.2
  • 54
    • 0014187163 scopus 로고
    • Fluorometric detection of histidine-tryptophan complexes in peptides and proteins
    • Shinitzy, M. & Goldman, R. (1967) Fluorometric detection of histidine-tryptophan complexes in peptides and proteins, Eur. J. Biochem. 3, 139-144.
    • (1967) Eur. J. Biochem. , vol.3 , pp. 139-144
    • Shinitzy, M.1    Goldman, R.2
  • 55
    • 0000974412 scopus 로고
    • Fluorescence quenching mechanism of tryptophan. Remarkably efficient internal proton-induced quenching and charge transfer quenching
    • Shizuka, H., Scrizawa, M., Shimo, T., Saito, I. & Matsuura, T. (1988) Fluorescence quenching mechanism of tryptophan. Remarkably efficient internal proton-induced quenching and charge transfer quenching, J. Am. Chem. Soc. 110, 1930-1934.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1930-1934
    • Shizuka, H.1    Scrizawa, M.2    Shimo, T.3    Saito, I.4    Matsuura, T.5
  • 56
    • 0014633510 scopus 로고
    • The interactions of the ground and excited states of indole with electron scavengers
    • Steiner, R. F. & Kirby, E. P. (1969) The interactions of the ground and excited states of indole with electron scavengers, J. Phys. Chem. 73, 4130-4135.
    • (1969) J. Phys. Chem. , vol.73 , pp. 4130-4135
    • Steiner, R.F.1    Kirby, E.P.2
  • 57
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo, A. G. & Rayner, D. M. (1980) Fluorescence decay of tryptophan conformers in aqueous solution, J. Am. Chem. Soc. 102, 554-563.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 58
    • 0025638855 scopus 로고
    • Fluorescenc of a rotationally coinstraint tryptophan derivative
    • Tilstra, L., Sattler, M. C. Cherry, W. R. & Barkley, M. D. (1990) Fluorescenc of a rotationally coinstraint tryptophan derivative, J. Am. Chem. Soc. 112, 9176-9182.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9176-9182
    • Tilstra, L.1    Sattler, M.C.2    Cherry, W.R.3    Barkley, M.D.4
  • 60
    • 0000256482 scopus 로고
    • Excited state lifetime distributions of tryptophan fluorescence in polar solutions. Evidences for solvent-exciplex formation
    • Vekshin, N., Vincent, M. & Gallay, J. (1992) Excited state lifetime distributions of tryptophan fluorescence in polar solutions. Evidences for solvent-exciplex formation, Chem. Phys. Lett. 199, 459-464.
    • (1992) Chem. Phys. Lett. , vol.199 , pp. 459-464
    • Vekshin, N.1    Vincent, M.2    Gallay, J.3
  • 61
    • 0024299704 scopus 로고
    • Nanosecond dynamics of horse heart apocytochrome c as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59)
    • Vincent, M., Brochon, J.-C., Mérola, F., Jordi, W. & Gallay, J. (1988) Nanosecond dynamics of horse heart apocytochrome c as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59), Biochemistry 27, 8752-8761.
    • (1988) Biochemistry , vol.27 , pp. 8752-8761
    • Vincent, M.1    Brochon, J.-C.2    Mérola, F.3    Jordi, W.4    Gallay, J.5
  • 62
    • 33751156520 scopus 로고
    • Solvent relaxation around the excited state of indole: Analysis of lifetime distributions and time-dependent spectral shifts
    • Vincent, M., Gallay, J. & Demchenko, A. P. (1995) Solvent relaxation around the excited state of indole: analysis of lifetime distributions and time-dependent spectral shifts, J. Phys. Chem. 99, 14931-14941.
    • (1995) J. Phys. Chem. , vol.99 , pp. 14931-14941
    • Vincent, M.1    Gallay, J.2    Demchenko, A.P.3
  • 63
    • 0028465491 scopus 로고
    • A fluorescence study of tryptophanhistidin interactions in the peptide anantin in solution
    • Vos, R. & Engelborghs, Y. (1994) A fluorescence study of tryptophanhistidin interactions in the peptide anantin in solution, Photochem. Photobiol. 60, 24-32.
    • (1994) Photochem. Photobiol. , vol.60 , pp. 24-32
    • Vos, R.1    Engelborghs, Y.2
  • 64
    • 9344235243 scopus 로고
    • Time-resolved spectroscopy in biochemistry and in biology (Cundall, R. B. & Dale, R. E., eds) Plenum Press, New York & London
    • Ware, W. R. (1983) in Time-resolved spectroscopy in biochemistry and in biology (Cundall, R. B. & Dale, R. E., eds) Advanced Sciences Institute Series A: Life Sciences, vol. 69, pp. 341-361, Plenum Press, New York & London.
    • (1983) Advanced Sciences Institute Series A: Life Sciences , vol.69 , pp. 341-361
    • Ware, W.R.1
  • 65
    • 0022437402 scopus 로고
    • Virulence factors of Bordetella pertussis
    • Weiss, A. A. & Hewlett, E. L. (1986) Virulence factors of Bordetella pertussis, Annu. Rev. Microbiol. 40, 661-686.
    • (1986) Annu. Rev. Microbiol. , vol.40 , pp. 661-686
    • Weiss, A.A.1    Hewlett, E.L.2
  • 66
    • 0016182374 scopus 로고
    • Separation and purification of cyclic nucleotides by alumina column chromatography
    • White, A. A. (1974) Separation and purification of cyclic nucleotides by alumina column chromatography, Methods Enzymol. 38, 41-46.
    • (1974) Methods Enzymol. , vol.38 , pp. 41-46
    • White, A.A.1
  • 67
    • 0028175552 scopus 로고
    • Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation
    • Willis, K. J., Neugebauer, W., Sikorska, M. & Szabo, A. G. (1994) Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation, Biophys. J. 66, 1623-1630.
    • (1994) Biophys. J. , vol.66 , pp. 1623-1630
    • Willis, K.J.1    Neugebauer, W.2    Sikorska, M.3    Szabo, A.G.4
  • 69
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu, C. S. & Martinez H. M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 70
    • 0001617063 scopus 로고
    • Efficient isolation of genes by using antibody probes
    • Young, R. A. & Davis, R. W. (1983) Efficient isolation of genes by using antibody probes, Proc. Natl Acad. Sci. USA 80, 1194-1198.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 1194-1198
    • Young, R.A.1    Davis, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.