메뉴 건너뛰기




Volumn 136, Issue 1, 2008, Pages 38-43

Photostability of green and yellow fluorescent proteins with fluorinated chromophores, investigated by fluorescence correlation spectroscopy

Author keywords

Autofluorescent protein; Electron transfer reactions; Fluorescence correlation spectroscopy; Fluorinated tyrosine; Photobleaching; Photostability

Indexed keywords

GREEN FLUORESCENT PROTEIN; YELLOW FLUORESCENT PROTEIN;

EID: 44349151727     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.04.006     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0004085382 scopus 로고    scopus 로고
    • (eds.) Green fluorescent proteins
    • Sullivan K.F., and Kay S.A. (eds.) Green fluorescent proteins. Methods Cell Biol. 58 (1999) 1-369
    • (1999) Methods Cell Biol. , vol.58 , pp. 1-369
    • Sullivan, K.F.1    Kay, S.A.2
  • 2
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., and Prasher D.C. Green fluorescent protein as a marker for gene expression. Science 263 (1994) 802-805
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 3
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • Vladislav V.V., and Lukyanov K.A. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nat. Biotechnol. 22 (2004) 289-296
    • (2004) Nat. Biotechnol. , vol.22 , pp. 289-296
    • Vladislav, V.V.1    Lukyanov, K.A.2
  • 4
    • 33645825831 scopus 로고    scopus 로고
    • Living cells as test tubes
    • Xie X.S., Yu J., and Yang W.Y. Living cells as test tubes. Science 312 (2006) 228-230
    • (2006) Science , vol.312 , pp. 228-230
    • Xie, X.S.1    Yu, J.2    Yang, W.Y.3
  • 6
    • 19744365121 scopus 로고    scopus 로고
    • The photophysics of green fluorescent protein: influence of the key amino acids at position 65, 203, and 222
    • Jung G., Wiehler J., and Zumbush A. The photophysics of green fluorescent protein: influence of the key amino acids at position 65, 203, and 222. Biophys. J. 88 (2005) 1932-1947
    • (2005) Biophys. J. , vol.88 , pp. 1932-1947
    • Jung, G.1    Wiehler, J.2    Zumbush, A.3
  • 7
    • 0001350436 scopus 로고    scopus 로고
    • Effect of threonine 203 replacements on excited-state dynamics and fluorescence properties of green fluorescent protein (GFP)
    • Kummer A., Wiehler H., Rehaber H., Kompa C., Steipe B., and Michel-Beyerle M.E. Effect of threonine 203 replacements on excited-state dynamics and fluorescence properties of green fluorescent protein (GFP). J. Phys. Chem. B. 104 (2000) 4791-4798
    • (2000) J. Phys. Chem. B. , vol.104 , pp. 4791-4798
    • Kummer, A.1    Wiehler, H.2    Rehaber, H.3    Kompa, C.4    Steipe, B.5    Michel-Beyerle, M.E.6
  • 8
    • 14844361031 scopus 로고    scopus 로고
    • Structural and spectral response of Aequorea victoria green fluorescent proteins to chromophore fluorination
    • Pal P.P., Bae J.H., K Azim M., Hess P., Friedrich R., Huber R., Moroder L., and Budisa N. Structural and spectral response of Aequorea victoria green fluorescent proteins to chromophore fluorination. Biochemistry 44 (2005) 3663-3672
    • (2005) Biochemistry , vol.44 , pp. 3663-3672
    • Pal, P.P.1    Bae, J.H.2    K Azim, M.3    Hess, P.4    Friedrich, R.5    Huber, R.6    Moroder, L.7    Budisa, N.8
  • 9
    • 4544351549 scopus 로고    scopus 로고
    • Crystallographic evidence for isomeric chromophores in 3-fluorotyrosyl-green fluorescent protein
    • Bae J.H., P Pal P., Moroder L., Huber R., and Budisa N. Crystallographic evidence for isomeric chromophores in 3-fluorotyrosyl-green fluorescent protein. ChemBioChem 5 (2004) 720-722
    • (2004) ChemBioChem , vol.5 , pp. 720-722
    • Bae, J.H.1    P Pal, P.2    Moroder, L.3    Huber, R.4    Budisa, N.5
  • 10
  • 11
    • 0035033890 scopus 로고    scopus 로고
    • Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy
    • Harms G.S., Cogent L., Lommerse P.H.M., Blab G.A., and Schmidt T. Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy. Biophys. J. 80 (2001) 2396-2408
    • (2001) Biophys. J. , vol.80 , pp. 2396-2408
    • Harms, G.S.1    Cogent, L.2    Lommerse, P.H.M.3    Blab, G.A.4    Schmidt, T.5
  • 12
    • 18744397828 scopus 로고    scopus 로고
    • Molecular photobleaching kinetics of rhodamine 6G by one- and two-photon induced confocal fluorescence microscopy
    • Eggeling C., Volkmer A., and Seidel C.A.M. Molecular photobleaching kinetics of rhodamine 6G by one- and two-photon induced confocal fluorescence microscopy. ChemPhysChem 6 (2005) 791-804
    • (2005) ChemPhysChem , vol.6 , pp. 791-804
    • Eggeling, C.1    Volkmer, A.2    Seidel, C.A.M.3
  • 13
  • 14
    • 0032128026 scopus 로고    scopus 로고
    • Photobleaching of fluorescent dyes under conditions used for single-molecule detection: evidence of two-step photolysis
    • Eggeling C., Widegren J., Rigler R., and Seidel C.A.M. Photobleaching of fluorescent dyes under conditions used for single-molecule detection: evidence of two-step photolysis. Anal. Chem. 70 (1998) 2651-2659
    • (1998) Anal. Chem. , vol.70 , pp. 2651-2659
    • Eggeling, C.1    Widegren, J.2    Rigler, R.3    Seidel, C.A.M.4
  • 15
    • 13444306203 scopus 로고    scopus 로고
    • Optical saturation in fluorescence correlation spectroscopy under continuous-wave and pulsed excitation
    • Gregor I., Patra D., and Enderlein J. Optical saturation in fluorescence correlation spectroscopy under continuous-wave and pulsed excitation. ChemPhysChem 6 (2005) 164-170
    • (2005) ChemPhysChem , vol.6 , pp. 164-170
    • Gregor, I.1    Patra, D.2    Enderlein, J.3
  • 16
    • 0035248838 scopus 로고    scopus 로고
    • Two-color fluorescence correlation spectroscopy of one chromophore: application to the E222Q mutant of the green fluorescent protein
    • Jung G., Bräuchle C., and Zumbusch A. Two-color fluorescence correlation spectroscopy of one chromophore: application to the E222Q mutant of the green fluorescent protein. J. Chem. Phys. 114 (2001) 3149-3156
    • (2001) J. Chem. Phys. , vol.114 , pp. 3149-3156
    • Jung, G.1    Bräuchle, C.2    Zumbusch, A.3
  • 17
    • 5244244652 scopus 로고
    • Fast and accurate method for measuring photon flux in the range 2500-6000 Å
    • Yguerabide J. Fast and accurate method for measuring photon flux in the range 2500-6000 Å. Rev. Sci. Instr. 39 (1968) 1048-1052
    • (1968) Rev. Sci. Instr. , vol.39 , pp. 1048-1052
    • Yguerabide, J.1
  • 18
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate at low background: analysis of translational diffusion
    • Rigler R., Mets Ü., Widengren J., and Kask P. Fluorescence correlation spectroscopy with high count rate at low background: analysis of translational diffusion. Eur. Biophys J. 22 (1993) 169-175
    • (1993) Eur. Biophys J. , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, Ü.2    Widengren, J.3    Kask, P.4
  • 19
    • 33645508362 scopus 로고    scopus 로고
    • Improving autofluorescent proteins: comparative studies of the effective brightness of green fluorescent protein (GFP) mutants
    • Jung G., and Zumbusch A. Improving autofluorescent proteins: comparative studies of the effective brightness of green fluorescent protein (GFP) mutants. Micros. Res. Techn. 69 (2006) 175-185
    • (2006) Micros. Res. Techn. , vol.69 , pp. 175-185
    • Jung, G.1    Zumbusch, A.2
  • 20
    • 0035678612 scopus 로고    scopus 로고
    • Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two-photon excitation
    • Dittrich P., and Schwille P. Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two-photon excitation. Appl. Phys. B. 73 (2001) 829-837
    • (2001) Appl. Phys. B. , vol.73 , pp. 829-837
    • Dittrich, P.1    Schwille, P.2
  • 21
    • 34248218211 scopus 로고    scopus 로고
    • Circumvention of fluorophore photobleaching in fluorescence fluctuation experiments: a beam scanning approach
    • Satsoura D., Leber B., V Andrews D., and Fradin C. Circumvention of fluorophore photobleaching in fluorescence fluctuation experiments: a beam scanning approach. ChemPhysChem 8 (2007) 834-848
    • (2007) ChemPhysChem , vol.8 , pp. 834-848
    • Satsoura, D.1    Leber, B.2    V Andrews, D.3    Fradin, C.4
  • 22
    • 0032493478 scopus 로고    scopus 로고
    • 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: effects of the modifications on isomerase kinetics
    • 5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: effects of the modifications on isomerase kinetics. Biochemistry 37 (1998) 9738-9742
    • (1998) Biochemistry , vol.37 , pp. 9738-9742
    • Brooks, B.1    Robert, S.P.2    William, F.B.3
  • 24
  • 25
    • 0029057619 scopus 로고
    • Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy
    • Song L., Hennink E.J., Young I.T., and Tannke H.J. Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy. Biophys. J. 68 (1995) 2588-2600
    • (1995) Biophys. J. , vol.68 , pp. 2588-2600
    • Song, L.1    Hennink, E.J.2    Young, I.T.3    Tannke, H.J.4
  • 26
    • 37749053853 scopus 로고    scopus 로고
    • Singlet oxygen photosensitization by EGFP and its chromophore HBDI
    • Jimenez-Banzo A., Nonell S., Hofkens J., and Flors C. Singlet oxygen photosensitization by EGFP and its chromophore HBDI. Biophys. J. 94 (2008) 168-172
    • (2008) Biophys. J. , vol.94 , pp. 168-172
    • Jimenez-Banzo, A.1    Nonell, S.2    Hofkens, J.3    Flors, C.4
  • 27
    • 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., Gensch T., Hellingwerf K.J., and Johnson L.N. Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222. Nat. Struct. Biol. 9 (2002) 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
  • 28
    • 32244442013 scopus 로고    scopus 로고
    • Mono-, Di-, and Tetra-substituted fluorotyrosines: New probes for enzymes that use tyrosyl radicals in catalysis
    • Seyedsayamdost M.R., Steven Y.R., Daniel G.N., and JoAnne S. Mono-, Di-, and Tetra-substituted fluorotyrosines: New probes for enzymes that use tyrosyl radicals in catalysis. J. Am. Chem. Soc. 28 (2006) 1569-1579
    • (2006) J. Am. Chem. Soc. , vol.28 , pp. 1569-1579
    • Seyedsayamdost, M.R.1    Steven, Y.R.2    Daniel, G.N.3    JoAnne, S.4
  • 29
    • 0034602653 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy reveals fast optical excitation-driven intramolecular dynamics of yellow fluorescent proteins
    • Schwille P., Kummer S., A Heikal A., Moerner W.E., and Webb W.W. Fluorescence correlation spectroscopy reveals fast optical excitation-driven intramolecular dynamics of yellow fluorescent proteins. Proc. Natl. Acad. Sci. U S A. 97 (2000) 151-156
    • (2000) Proc. Natl. Acad. Sci. U S A. , vol.97 , pp. 151-156
    • Schwille, P.1    Kummer, S.2    A Heikal, A.3    Moerner, W.E.4    Webb, W.W.5
  • 30
    • 0033702974 scopus 로고    scopus 로고
    • Characterisation of photo induced isomerisation and back isomerisation of the cyanine dye Cy5 by fluorescence correlation spectroscopy
    • Widengren J., and Schwille P. Characterisation of photo induced isomerisation and back isomerisation of the cyanine dye Cy5 by fluorescence correlation spectroscopy. J. Phys. Chem. A. 104 (2000) 6416-6428
    • (2000) J. Phys. Chem. A. , vol.104 , pp. 6416-6428
    • Widengren, J.1    Schwille, P.2
  • 31
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67 (1998) 509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.