메뉴 건너뛰기




Volumn 82, Issue 2, 2006, Pages 373-379

Time-resolved emission spectra of green fluorescent protein

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33646252468     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2005-05-07-RA-518     Document Type: Conference Paper
Times cited : (18)

References (49)
  • 1
    • 0036489443 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP): Applications, structure, and related photophysical behavior
    • Zimmer, M. (2002) Green fluorescent protein (GFP): applications, structure, and related photophysical behavior. Chem. Rev. 102, 759-782.
    • (2002) Chem. Rev. , vol.102 , pp. 759-782
    • Zimmer, M.1
  • 2
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 3
    • 0029757121 scopus 로고    scopus 로고
    • Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj, M., B. A. King, G. Bublitz and S. G. Boxer (1996) Ultra-fast excited state dynamics in green fluorescent protein: multiple states and proton transfer. Proc. Natl. Acad. Sci. U.S.A. 93, 8362-8367.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.3    Boxer, S.G.4
  • 4
    • 0037207122 scopus 로고    scopus 로고
    • Green fluorescent protein variants as ratiometric dual emission pH sensors. 2. Excited state dynamics
    • McAnaney, T. B., E. S. Park, G. T. Hanson, S. J. Remington and S. G. Boxer (2002) Green fluorescent protein variants as ratiometric dual emission pH sensors. 2. Excited state dynamics. Biochemistry 41, 15489-15494.
    • (2002) Biochemistry , vol.41 , pp. 15489-15494
    • McAnaney, T.B.1    Park, E.S.2    Hanson, G.T.3    Remington, S.J.4    Boxer, S.G.5
  • 6
    • 0001350436 scopus 로고    scopus 로고
    • Effects of threonine 203 replacements on excited-state dynamics and fluorescence properties of the green fluorescent protein (GFP)
    • Kummer, A. D., J. Wiehler, H. Rehaber, C. Kompa, B. Steipe and M. E. Michel-Beyerle (2000) Effects of threonine 203 replacements on excited-state dynamics and fluorescence properties of the green fluorescent protein (GFP). J. Phys. Chem. B 104, 4791-4798.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4791-4798
    • Kummer, A.D.1    Wiehler, J.2    Rehaber, H.3    Kompa, C.4    Steipe, B.5    Michel-Beyerle, M.E.6
  • 8
    • 0036903811 scopus 로고    scopus 로고
    • Picosecond time-resolved fluorescence from blue-emitting chromophore variants Y66F and Y66H of the green fluorescent protein
    • Kummer, A. D., J. Wiehler, T. A. Schüttrigkeit, B. W. Berger, B. Streipe and M. E. Michel-Beyerle (2002) Picosecond time-resolved fluorescence from blue-emitting chromophore variants Y66F and Y66H of the green fluorescent protein. ChemBioChem 3, 659-663.
    • (2002) ChemBioChem , vol.3 , pp. 659-663
    • Kummer, A.D.1    Wiehler, J.2    Schüttrigkeit, T.A.3    Berger, B.W.4    Streipe, B.5    Michel-Beyerle, M.E.6
  • 9
    • 0035831564 scopus 로고    scopus 로고
    • Coherent dynamics of photoexcited green fluorescent proteins
    • Cinelli, R. A. G. (2001) Coherent dynamics of photoexcited green fluorescent proteins. Phys. Rev. Lett. 86, 3439-3442.
    • (2001) Phys. Rev. Lett. , vol.86 , pp. 3439-3442
    • Cinelli, R.A.G.1
  • 10
    • 0035928131 scopus 로고    scopus 로고
    • Ab initio molecular dynamics of the green fluorescent protein (GFP) chromophore: An insight into the photoinduced dynamics of green fluorescent proteins
    • Tozzini, V. and R. Nifosì (2001) Ab initio molecular dynamics of the green fluorescent protein (GFP) chromophore: an insight into the photoinduced dynamics of green fluorescent proteins. J. Phys. Chem. B 105, 5797-5803.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5797-5803
    • Tozzini, V.1    Nifosì, R.2
  • 11
    • 0034647977 scopus 로고    scopus 로고
    • Low-lying electronic excitations of the green fluorescent protein chromophore
    • Helms, V., C. Winstead and P. W. Langhoff (2000) Low-lying electronic excitations of the green fluorescent protein chromophore. J. Mol. Struct. 506, 179-189.
    • (2000) J. Mol. Struct. , vol.506 , pp. 179-189
    • Helms, V.1    Winstead, C.2    Langhoff, P.W.3
  • 12
    • 0033065308 scopus 로고    scopus 로고
    • Shedding light on the dark and weakly fluorescent states of green fluorescent proteins
    • Weber, W., V. Helms, J. A. McCammon and P. W. Langhoff (1999) Shedding light on the dark and weakly fluorescent states of green fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A. 96, 6177-6182.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6177-6182
    • Weber, W.1    Helms, V.2    McCammon, J.A.3    Langhoff, P.W.4
  • 13
    • 0036202903 scopus 로고    scopus 로고
    • Ultrafast dynamics in the excited state of green fluorescent protein (wt) studied by frequency-resolved femtosecond pump-probe spectroscopy
    • Winkler, K. (2002) Ultrafast dynamics in the excited state of green fluorescent protein (wt) studied by frequency-resolved femtosecond pump-probe spectroscopy. Phys. Chem. Chem. Phys. 4, 1072-1081.
    • (2002) Phys. Chem. Chem. Phys. , vol.4 , pp. 1072-1081
    • Winkler, K.1
  • 14
    • 2942613404 scopus 로고    scopus 로고
    • Observation of low frequency vibrational modes in a mutant of green fluorescent protein
    • Litvinenko, K. L. and S. R. Meech (2004) Observation of low frequency vibrational modes in a mutant of green fluorescent protein. Phys. Chem. Chem. Phys. 6, 2012-2014.
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 2012-2014
    • Litvinenko, K.L.1    Meech, S.R.2
  • 15
    • 3442888534 scopus 로고    scopus 로고
    • Fluorescence photoconversion kinetics in novel green fluorescent protein pH sensors (pHlourins)
    • Hess, S. T., A. A. Heikal and W. W. Webb (2004) Fluorescence photoconversion kinetics in novel green fluorescent protein pH sensors (pHlourins). J. Phys. Chem. B 108, 10138-10148.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 10138-10148
    • Hess, S.T.1    Heikal, A.A.2    Webb, W.W.3
  • 18
    • 0037022637 scopus 로고    scopus 로고
    • Proton shuttle in green fluorescent protein studies by dynamic simulations
    • Lill, M. A. and V. Helms (2002) Proton shuttle in green fluorescent protein studies by dynamic simulations. Proc. Natl. Acad. Sci. U.S.A. 99, 2778-2781.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2778-2781
    • Lill, M.A.1    Helms, V.2
  • 19
    • 14844302645 scopus 로고    scopus 로고
    • Observation of excited-state proton transfer in green fluorescent protein using ultrafast vibrational spectroscopy
    • Stoner-Ma, D., A. A. Jaye, P. Matousek, M. Towrie, S. R. Meech and P. J. Tonge (2005) Observation of excited-state proton transfer in green fluorescent protein using ultrafast vibrational spectroscopy. J. Am. Chem. Soc. 127, 2864-2865.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2864-2865
    • Stoner-Ma, D.1    Jaye, A.A.2    Matousek, P.3    Towrie, M.4    Meech, S.R.5    Tonge, P.J.6
  • 20
    • 0034966140 scopus 로고    scopus 로고
    • Computational analysis of Thr203 isomerization in green fluorescent protein
    • Warren, A. and M. Zimmer (2001) Computational analysis of Thr203 isomerization in green fluorescent protein. J. Mol. Graph. Model. 19, 297-303.
    • (2001) J. Mol. Graph. Model. , vol.19 , pp. 297-303
    • Warren, A.1    Zimmer, M.2
  • 22
    • 0032537670 scopus 로고    scopus 로고
    • Fluorescent properties of model chromophores of tyrosine-66 substituted mutants of Aequorea green fluorescent protein (GFP)
    • Kojima, S., H. Ohkawa, T. Hirano, S. Maki, H. Niwa, M. Ohashi, S. Inouye and F. I. Tsuji (1998) Fluorescent properties of model chromophores of tyrosine-66 substituted mutants of Aequorea green fluorescent protein (GFP). Tetrahedron Lett. 39, 5239-5242.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 5239-5242
    • Kojima, S.1    Ohkawa, H.2    Hirano, T.3    Maki, S.4    Niwa, H.5    Ohashi, M.6    Inouye, S.7    Tsuji, F.I.8
  • 23
    • 0035940246 scopus 로고    scopus 로고
    • Radiationless relaxation in a synthetic analogue of the green fluorescent protein chromophore
    • Webber, N. M., K. L. Litvinenko and S. R. Meech (2001) Radiationless relaxation in a synthetic analogue of the green fluorescent protein chromophore. J. Phys. Chem. B 105, 8036-8039.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 8036-8039
    • Webber, N.M.1    Litvinenko, K.L.2    Meech, S.R.3
  • 24
    • 0035965168 scopus 로고    scopus 로고
    • An ultrafast polarisation spectroscopy study of internal conversion and orientational relaxation of the chromophore of the green fluorescent protein
    • Litvinenko, K. L., N. M. Webber and S. R. Meech (2001) An ultrafast polarisation spectroscopy study of internal conversion and orientational relaxation of the chromophore of the green fluorescent protein. Chem. Phys. Lett. 346, 47-53.
    • (2001) Chem. Phys. Lett. , vol.346 , pp. 47-53
    • Litvinenko, K.L.1    Webber, N.M.2    Meech, S.R.3
  • 25
    • 2342638866 scopus 로고    scopus 로고
    • Origin, nature, and fate of the fluorescent state of the green fluorescent protein chromophore at the CASPT2//CASSCF resolution
    • Martin, M. E., F. Negri and M. Olivucci (2004) Origin, nature, and fate of the fluorescent state of the green fluorescent protein chromophore at the CASPT2//CASSCF resolution. J. Am. Chem. Soc. 126, 5452-5464.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5452-5464
    • Martin, M.E.1    Negri, F.2    Olivucci, M.3
  • 26
    • 0037452021 scopus 로고    scopus 로고
    • Internal conversion in the chromophore of the green fluorescent protein: Temperature dependence and isoviscosity analysis
    • Litvinenko, K. L., N. M. Webber and S. R. Meech (2003) Internal conversion in the chromophore of the green fluorescent protein: Temperature dependence and isoviscosity analysis. J. Phys. Chem. A 107, 2616-2623.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 2616-2623
    • Litvinenko, K.L.1    Webber, N.M.2    Meech, S.R.3
  • 27
    • 0037035988 scopus 로고    scopus 로고
    • Ultrafast fluorescence of the chromophore of the green fluorescent protein in alcohol solutions
    • Mandal, D., T. Tahara, N. M. Webber and S. R. Meech (2002) Ultrafast fluorescence of the chromophore of the green fluorescent protein in alcohol solutions. Chem. Phys. Lett. 358, 495-501.
    • (2002) Chem. Phys. Lett. , vol.358 , pp. 495-501
    • Mandal, D.1    Tahara, T.2    Webber, N.M.3    Meech, S.R.4
  • 28
    • 0742286768 scopus 로고    scopus 로고
    • Excited-state dynamics in the green fluorescent protein chromophore
    • Mandal, D., T. Tahara and S. R. Meech (2004) Excited-state dynamics in the green fluorescent protein chromophore. J. Phys. Chem. B 108, 1102-1108.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 1102-1108
    • Mandal, D.1    Tahara, T.2    Meech, S.R.3
  • 29
    • 0036704071 scopus 로고    scopus 로고
    • Viscosity-dependent fluorescence decay of the GFP chromophore in solution due to fast internal conversion
    • Kummer, A. D., C. Kompa, H. Niwa, T. Hirano, S. Kojima and M. E. Michel-Beyerle (2002) Viscosity-dependent fluorescence decay of the GFP chromophore in solution due to fast internal conversion. J. Phys. Chem. B 106, 7554-7559.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 7554-7559
    • Kummer, A.D.1    Kompa, C.2    Niwa, H.3    Hirano, T.4    Kojima, S.5    Michel-Beyerle, M.E.6
  • 30
    • 5644244488 scopus 로고    scopus 로고
    • Conical intersection dynamics in solution: The chromophore of green fluorescent protein
    • Toniolo, A., S. Olsen, L. Manohar and T. J. Martinez (2004) Conical intersection dynamics in solution: the chromophore of green fluorescent protein. Faraday Discuss. 127, 149-163.
    • (2004) Faraday Discuss. , vol.127 , pp. 149-163
    • Toniolo, A.1    Olsen, S.2    Manohar, L.3    Martinez, T.J.4
  • 32
    • 0035250678 scopus 로고    scopus 로고
    • A determination of the structure of the intramolecular charge transfer state of 4-dimethylaminobenzonitrile (DMABN) by time-resolved resonance Raman spectroscopy
    • Kwok, W. M., C. Ma, P. Matousek, A. W. Parker, D. Phillips, T. W. T., M. Towrie and S. Umapathy (2001) A determination of the structure of the intramolecular charge transfer state of 4-dimethylaminobenzonitrile (DMABN) by time-resolved resonance Raman spectroscopy. J. Phys. Chem. A 105, 984-990.
    • (2001) J. Phys. Chem. A , vol.105 , pp. 984-990
    • Kwok, W.M.1    Ma, C.2    Matousek, P.3    Parker, A.W.4    Phillips, D.5    T, T.W.6    Towrie, M.7    Umapathy, S.8
  • 33
    • 0042956534 scopus 로고
    • Picosecond solvation dynamics of coumarin 153: The importance of molecular aspects of solvation
    • Maroncelli, M. and G. R. Fleming (1987) Picosecond solvation dynamics of coumarin 153: the importance of molecular aspects of solvation. J. Chem. Phys. 86, 6221-6239.
    • (1987) J. Chem. Phys. , vol.86 , pp. 6221-6239
    • Maroncelli, M.1    Fleming, G.R.2
  • 34
    • 0032538062 scopus 로고    scopus 로고
    • Electronic structure of the chromophore in green fluorescent protein (GFP)
    • Bublitz, G., B. A. King and S. G. Boxer (1998) Electronic structure of the chromophore in green fluorescent protein (GFP). J. Am. Chem. Soc. 120, 9370-9371.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9370-9371
    • Bublitz, G.1    King, B.A.2    Boxer, S.G.3
  • 36
    • 33751271923 scopus 로고
    • The dynamics of solvation in polar liquids
    • Maroncelli, M. (1993) The dynamics of solvation in polar liquids. J. Mol. Liq. 57, 1-37.
    • (1993) J. Mol. Liq. , vol.57 , pp. 1-37
    • Maroncelli, M.1
  • 37
    • 0001779886 scopus 로고    scopus 로고
    • Solvent dynamics derived from optical Kerr effect, dielectric dispersion, and time resolved Stokes shifts measurements: An empirical comparison
    • Castner, E. W. J. and M. Maroncelli (1998) Solvent dynamics derived from optical Kerr effect, dielectric dispersion, and time resolved Stokes shifts measurements: an empirical comparison. J. Mol. Liq. 77, 1-36.
    • (1998) J. Mol. Liq. , vol.77 , pp. 1-36
    • Castner, E.W.J.1    Maroncelli, M.2
  • 38
    • 0035824832 scopus 로고    scopus 로고
    • Dielectric relaxation in a single tryptophan protein
    • Ghose, M., S. Mandal, D. Roy, R. K. Mandal and G. Basu (2001) Dielectric relaxation in a single tryptophan protein. FEBS Lett. 509, 337-340.
    • (2001) FEBS Lett. , vol.509 , pp. 337-340
    • Ghose, M.1    Mandal, S.2    Roy, D.3    Mandal, R.K.4    Basu, G.5
  • 39
    • 0037204951 scopus 로고    scopus 로고
    • Probing protein electrostatics with a synthetic fluorescent amino acid
    • Cohen, B. E., T. B. McAnaney, E. S. Park, Y. N. Jan, S. G. Boxer and L. Y. Jan (2002) Probing protein electrostatics with a synthetic fluorescent amino acid. Science 296, 1700-1703.
    • (2002) Science , vol.296 , pp. 1700-1703
    • Cohen, B.E.1    McAnaney, T.B.2    Park, E.S.3    Jan, Y.N.4    Boxer, S.G.5    Jan, L.Y.6
  • 41
    • 0034301060 scopus 로고    scopus 로고
    • Ultrafast dielectric response of proteins from dynamics Stokes shifting of coumarin in calmodulin
    • Changenet-Barret, P., C. T. Choma, E. F. Gooding, W. F. Degrado and R. M. Hochstrasser (2000) Ultrafast dielectric response of proteins from dynamics Stokes shifting of coumarin in calmodulin. J. Phys. Chem. B 104, 9322-9329.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 9322-9329
    • Changenet-Barret, P.1    Choma, C.T.2    Gooding, E.F.3    Degrado, W.F.4    Hochstrasser, R.M.5
  • 42
    • 7044226398 scopus 로고    scopus 로고
    • Polar solvation dynamics in Zn(II)-substituted cytochrome c: Diffusive sampling of the energy landscape in the hydrophobic core and solvent-contact layer
    • Lampa-Pastirk, S. and W. F. Beck (2004) Polar solvation dynamics in Zn(II)-substituted cytochrome c: diffusive sampling of the energy landscape in the hydrophobic core and solvent-contact layer. J. Phys. Chem. B 108, 16288-16294.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 16288-16294
    • Lampa-Pastirk, S.1    Beck, W.F.2
  • 43
    • 0000405834 scopus 로고    scopus 로고
    • Solvation dynamics in protein environments studied by photon echo spectroscopy
    • Jordanides, X. J., M. J. Lang, X. Y. Song and G. R. Fleming (1999) Solvation dynamics in protein environments studied by photon echo spectroscopy. J. Phys. Chem. B 103, 7995-8005.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 7995-8005
    • Jordanides, X.J.1    Lang, M.J.2    Song, X.Y.3    Fleming, G.R.4
  • 45
    • 0036140797 scopus 로고    scopus 로고
    • Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222
    • Van Thor, J. J., T. Gensch, K. J. Hellingwerf and L. N. Johnson (2002) Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222. Nat. Struct. Biol. 9, 37-41.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 37-41
    • Van Thor, J.J.1    Gensch, T.2    Hellingwerf, K.J.3    Johnson, L.N.4
  • 46
    • 0037072006 scopus 로고    scopus 로고
    • Ultrafast protein dynamics of bacteriorhodopsin probed by photon echo and transient absorption spectroscopy. J
    • Kennis, J. T. M., D. S. Larsen, K. Ohta, M. T. Facciotti, R. M. Glaeser and G. R. Fleming (2002) Ultrafast protein dynamics of bacteriorhodopsin probed by photon echo and transient absorption spectroscopy. J. Phys. Chem. B 106, 6067-6080.
    • (2002) Phys. Chem. B , vol.106 , pp. 6067-6080
    • Kennis, J.T.M.1    Larsen, D.S.2    Ohta, K.3    Facciotti, M.T.4    Glaeser, R.M.5    Fleming, G.R.6
  • 47
    • 0033021944 scopus 로고    scopus 로고
    • Three photoconvertible forms of green fluorescent protein identified by spectral hole-burning
    • Creemers, T. M. H., A. J. Lock, V. Subramaniam, T. M. Jovin and S. Völker (1999) Three photoconvertible forms of green fluorescent protein identified by spectral hole-burning. Nat. Struct. Biol. 6, 557-560.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 557-560
    • Creemers, T.M.H.1    Lock, A.J.2    Subramaniam, V.3    Jovin, T.M.4    Völker, S.5
  • 48
    • 0034681929 scopus 로고    scopus 로고
    • Probing the ground state structure of the green fluorescent protein chromophore using Raman spectroscopy
    • Bell, A. F., X. He, R. M. Wachter and P. J. Tonge (2000) Probing the ground state structure of the green fluorescent protein chromophore using Raman spectroscopy. Biochemistry 39, 4423-4431.
    • (2000) Biochemistry , vol.39 , pp. 4423-4431
    • Bell, A.F.1    He, X.2    Wachter, R.M.3    Tonge, P.J.4
  • 49
    • 0035822210 scopus 로고    scopus 로고
    • Resonance Raman scattering by the green fluorescent protein and an analogue of its chromophore
    • Schellenberg, P., E. Johnson, A. P. Esposito, P. J. Reid and W. W. Parson (2001) Resonance Raman scattering by the green fluorescent protein and an analogue of its chromophore. J. Phys. Chem. B 105, 5316-5322.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 5316-5322
    • Schellenberg, P.1    Johnson, E.2    Esposito, A.P.3    Reid, P.J.4    Parson, W.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.