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Volumn 142, Issue 5, 2007, Pages 655-661

Spectrally and time-resolved fluorescence spectroscopic study on melittin-calmodulin interaction

Author keywords

Calmodulin; Dielectric relaxation; Melittin; TCSPC; Time resolved fluorescence

Indexed keywords

CALMODULIN; MELITTIN; TRYPTOPHAN;

EID: 38849198556     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvm180     Document Type: Article
Times cited : (6)

References (24)
  • 2
    • 3442896792 scopus 로고    scopus 로고
    • Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution
    • Slaughter, B.D., Allen, M.W., Unruh, J.R., Urbauer, R.J.B., and Johnson, C.K. (2004) Single-molecule resonance energy transfer and fluorescence correlation spectroscopy of calmodulin in solution. J. Phys. Chem. B 108, 10388-10397
    • (2004) J. Phys. Chem. B , vol.108 , pp. 10388-10397
    • Slaughter, B.D.1    Allen, M.W.2    Unruh, J.R.3    Urbauer, R.J.B.4    Johnson, C.K.5
  • 3
    • 33746969931 scopus 로고    scopus 로고
    • Revealing two-state protein-protein interactions of calmodulin by singlemolecule spectroscopy
    • Liu, R., Hu, D., Tin, X., and Lu, H.P. (2006) Revealing two-state protein-protein interactions of calmodulin by singlemolecule spectroscopy. J. Am. Chem. Soc. 128, 10034-10042
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10034-10042
    • Liu, R.1    Hu, D.2    Tin, X.3    Lu, H.P.4
  • 4
    • 0038649991 scopus 로고    scopus 로고
    • Interpretation of fluorescence decays using a power-like model
    • Włodarczyk, J. and Kierdaszuk, B. (2003) Interpretation of fluorescence decays using a power-like model. Biophys. J. 85, 589-598
    • (2003) Biophys. J , vol.85 , pp. 589-598
    • Włodarczyk, J.1    Kierdaszuk, B.2
  • 6
    • 2942694454 scopus 로고    scopus 로고
    • Conformational effects on tryptophan fluorescence in cyclic hexapeptides
    • Pan, C.P. and Barkley, M.D. (2004) Conformational effects on tryptophan fluorescence in cyclic hexapeptides. Biophys. J. 86, 3828-3835
    • (2004) Biophys. J , vol.86 , pp. 3828-3835
    • Pan, C.P.1    Barkley, M.D.2
  • 7
    • 0001307623 scopus 로고    scopus 로고
    • A reversible dark state' mechanism for complexity of the fluorescence of tryptophan in proteins
    • Hudson, B.S., Huston, J.M., and S-Campos, G. (1999) A reversible "dark state' mechanism for complexity of the fluorescence of tryptophan in proteins. J. Phys. Chem. A 103, 2227-2234
    • (1999) J. Phys. Chem. A , vol.103 , pp. 2227-2234
    • Hudson, B.S.1    Huston, J.M.2    S-Campos, G.3
  • 9
    • 33846380618 scopus 로고    scopus 로고
    • Nanosecond relaxation dynamics of protein GB1 identified by the time-dependent red shift in the fluorescence of tryptophan and 5-fluorotryptophan
    • Toptygin, D., Gronenborn, A.M., and Brand, L. (2006) Nanosecond relaxation dynamics of protein GB1 identified by the time-dependent red shift in the fluorescence of tryptophan and 5-fluorotryptophan. J. Phys. Chem. B 110, 26292-26302
    • (2006) J. Phys. Chem. B , vol.110 , pp. 26292-26302
    • Toptygin, D.1    Gronenborn, A.M.2    Brand, L.3
  • 11
    • 0000861904 scopus 로고    scopus 로고
    • Spectrally- and time-resolved fluorescence emission of indole during solvent relaxation: A quantitative model
    • Toptygin, D. and Brand, L. (2000) Spectrally- and time-resolved fluorescence emission of indole during solvent relaxation: a quantitative model. Chem. Phys. Lett. 322, 496-502
    • (2000) Chem. Phys. Lett , vol.322 , pp. 496-502
    • Toptygin, D.1    Brand, L.2
  • 13
    • 0037137214 scopus 로고    scopus 로고
    • Temperature dependence of the internal dynamics of a calmodulin-peptide complex
    • Lee, A.L., Sharp, K.A., Kranz, J.K., Song, X.J., and Wand, A.J. (2002) Temperature dependence of the internal dynamics of a calmodulin-peptide complex. Biochemistry 41, 13814-13825
    • (2002) Biochemistry , vol.41 , pp. 13814-13825
    • Lee, A.L.1    Sharp, K.A.2    Kranz, J.K.3    Song, X.J.4    Wand, A.J.5
  • 14
    • 1942496481 scopus 로고    scopus 로고
    • Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides
    • Yamniuk, A.P. and Vogel, H.J. (2004) Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides. Mol. Biotechnol. 27, 33-58
    • (2004) Mol. Biotechnol , vol.27 , pp. 33-58
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 15
    • 33646409891 scopus 로고    scopus 로고
    • Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding
    • Ishida, H. and Vogel, H.J. (2006) Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding. Protein. Pept. Lett. 13, 455-465
    • (2006) Protein. Pept. Lett , vol.13 , pp. 455-465
    • Ishida, H.1    Vogel, H.J.2
  • 16
    • 0038236921 scopus 로고    scopus 로고
    • Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V
    • Bayley, P., Martin, S., Browne, P., and Royer, C. (2003) Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V. Eur. Biophys. J. 32, 122-127
    • (2003) Eur. Biophys. J , vol.32 , pp. 122-127
    • Bayley, P.1    Martin, S.2    Browne, P.3    Royer, C.4
  • 18
    • 0026670306 scopus 로고
    • Static and kinetic studies of calmodulin and melittin complex
    • Itakura, M. and Iio, T. (1992) Static and kinetic studies of calmodulin and melittin complex. J. Biochem. 112, 183-191
    • (1992) J. Biochem , vol.112 , pp. 183-191
    • Itakura, M.1    Iio, T.2
  • 19
    • 0018936548 scopus 로고
    • Calmodulins from muscles of marine invertebrates, scallop and sea anemone: Comparison with calmodulins from rabbit skeletal muscle and pig brain
    • Yazawa, M., Sakuma, M., and Yagi, K. (1980) Calmodulins from muscles of marine invertebrates, scallop and sea anemone: comparison with calmodulins from rabbit skeletal muscle and pig brain. J. Biochem. 87, 1313-1320
    • (1980) J. Biochem , vol.87 , pp. 1313-1320
    • Yazawa, M.1    Sakuma, M.2    Yagi, K.3
  • 20
    • 34147207323 scopus 로고    scopus 로고
    • The partially unfolded state of β-momorcharin characterized with steady-state and time-resolved fluorescence studies
    • Fukunaga, Y., Nishimoto, E., Yamashita, K., Otosu, T., and Yamashita, S. (2007) The partially unfolded state of β-momorcharin characterized with steady-state and time-resolved fluorescence studies. J. Biochem. 141, 9-18
    • (2007) J. Biochem , vol.141 , pp. 9-18
    • Fukunaga, Y.1    Nishimoto, E.2    Yamashita, K.3    Otosu, T.4    Yamashita, S.5
  • 21
    • 0001133461 scopus 로고
    • The deconvolution of photoluminescence data
    • McKinnon, A.E., Szabo, A.G., and Miller, D.R. (1977) The deconvolution of photoluminescence data. J. Phys. Chem. 81, 1564-1570
    • (1977) J. Phys. Chem , vol.81 , pp. 1564-1570
    • McKinnon, A.E.1    Szabo, A.G.2    Miller, D.R.3
  • 22
    • 0034809210 scopus 로고    scopus 로고
    • Steady-state and time-resolved fluorescence studies on wild type and mutant Chromatium vinosum high potential iron proteins: Holo- and apo-forms
    • Sau, A.K., Chen, C.A., Cowan, J.A., Mazumder, S., and Mitra, S. (2001) Steady-state and time-resolved fluorescence studies on wild type and mutant Chromatium vinosum high potential iron proteins: holo- and apo-forms. Biophys. J. 81, 2320-2330
    • (2001) Biophys. J , vol.81 , pp. 2320-2330
    • Sau, A.K.1    Chen, C.A.2    Cowan, J.A.3    Mazumder, S.4    Mitra, S.5
  • 23
    • 0036642824 scopus 로고    scopus 로고
    • Electric dipole moments of globular proteins: Measurement and calculation with NMR and X-ray databases
    • Takashima, S.J. (2002) Electric dipole moments of globular proteins: measurement and calculation with NMR and X-ray databases. Non-Cryst. Solids 305, 303-310
    • (2002) Non-Cryst. Solids , vol.305 , pp. 303-310
    • Takashima, S.J.1


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