메뉴 건너뛰기




Volumn 94, Issue 5, 2008, Pages 1826-1835

An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; CARBOCYANINE; CATALASE; CYANINE DYE 3; CYANINE DYE 5; FLUORESCENT DYE; GALLIC ACID PROPYL ESTER; GLUCOSE OXIDASE; HYDROXYBENZOIC ACID DERIVATIVE; OXYGEN; PROTOCATECHUATE 3,4 DIOXYGENASE; PROTOCATECHUIC ACID; REACTIVE OXYGEN METABOLITE; SCAVENGER;

EID: 41449108157     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.117689     Document Type: Article
Times cited : (631)

References (61)
  • 1
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • Weiss, S. 1999. Fluorescence spectroscopy of single biomolecules. Science. 283:1676-1683.
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 2
    • 33947517676 scopus 로고    scopus 로고
    • Cornish, P. V., and T. Ha. 2007. A survey of single-molecule techniques in chemical biology. ACS Chem. Biol. 2:53-61.
    • Cornish, P. V., and T. Ha. 2007. A survey of single-molecule techniques in chemical biology. ACS Chem. Biol. 2:53-61.
  • 4
    • 22444436718 scopus 로고    scopus 로고
    • Single-molecule fluorescence spectroscopy of protein folding
    • Schuler, B. 2005. Single-molecule fluorescence spectroscopy of protein folding. ChemPhysChem. 6:1206-1220.
    • (2005) ChemPhysChem , vol.6 , pp. 1206-1220
    • Schuler, B.1
  • 5
    • 0041321045 scopus 로고    scopus 로고
    • Single molecule measurement of protein folding kinetics
    • Lipman, E. A., B. Schuler, O. Bakajin, and W. A. Eaton. 2003. Single molecule measurement of protein folding kinetics. Science. 301:1233-1235.
    • (2003) Science , vol.301 , pp. 1233-1235
    • Lipman, E.A.1    Schuler, B.2    Bakajin, O.3    Eaton, W.A.4
  • 7
    • 0033523011 scopus 로고    scopus 로고
    • Single-molecule enzymology
    • Xie, X. S., and H. P. Lu. 1999. Single-molecule enzymology. J. Biol. Chem. 274:15967-15970.
    • (1999) J. Biol. Chem , vol.274 , pp. 15967-15970
    • Xie, X.S.1    Lu, H.P.2
  • 11
    • 33847051154 scopus 로고    scopus 로고
    • Identification of two distinct hybrid state intermediates on the ribosome
    • Munro, J. B., R. B. Altman, N. O'Connor, and S. C. Blanchard. 2007. Identification of two distinct hybrid state intermediates on the ribosome. Mol. Cell. 25:505-517.
    • (2007) Mol. Cell , vol.25 , pp. 505-517
    • Munro, J.B.1    Altman, R.B.2    O'Connor, N.3    Blanchard, S.C.4
  • 13
    • 33746713745 scopus 로고    scopus 로고
    • Real-time observation of RecA filament dynamics with single monomer resolution
    • Joo, C., S. A. McKinney, M. Nakamura, I. Rasnik, S. Myong, and T. Ha. 2006. Real-time observation of RecA filament dynamics with single monomer resolution. Cell. 126:515-527.
    • (2006) Cell , vol.126 , pp. 515-527
    • Joo, C.1    McKinney, S.A.2    Nakamura, M.3    Rasnik, I.4    Myong, S.5    Ha, T.6
  • 14
    • 33751292868 scopus 로고    scopus 로고
    • Blinking fluorophores: What do they tell us about protein dynamics?
    • Bagshaw, C. R., and D. Cherny. 2006. Blinking fluorophores: what do they tell us about protein dynamics? Biochem. Soc. Trans. 34:979-982.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 979-982
    • Bagshaw, C.R.1    Cherny, D.2
  • 15
    • 0033469230 scopus 로고    scopus 로고
    • Temporal fluctuations of fluorescence resonance energy transfer between two dyes conjugated to a single protein
    • Ha, T. J., A. Y. Ting, J. Liang, A. A. Deniz, D. S. Chemla, P. G. Schultz, and S. Weiss. 1999. Temporal fluctuations of fluorescence resonance energy transfer between two dyes conjugated to a single protein. Chem. Phys. 247:107-118.
    • (1999) Chem. Phys , vol.247 , pp. 107-118
    • Ha, T.J.1    Ting, A.Y.2    Liang, J.3    Deniz, A.A.4    Chemla, D.S.5    Schultz, P.G.6    Weiss, S.7
  • 17
    • 0033702974 scopus 로고    scopus 로고
    • Characterization of photoinduced isomerization and back-isomerization of the cyanine dye cy5 by fluorescence correlation spectroscopy
    • Widengren, J., and P. Schwille. 2000. Characterization of photoinduced isomerization and back-isomerization of the cyanine dye cy5 by fluorescence correlation spectroscopy. J. Phys. Chem. A. 104:6416-6428.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 6416-6428
    • Widengren, J.1    Schwille, P.2
  • 18
    • 0141459754 scopus 로고    scopus 로고
    • Photoblinking of rhodamine 6G in poly(vinyl alcohol): Radical dark state formed through the triplet
    • Zondervan, R., F. Kulzer, S. B. Orlinskii, and M. Orrit. 2003. Photoblinking of rhodamine 6G in poly(vinyl alcohol): radical dark state formed through the triplet. J. Phys. Chem. A. 107:6770-6776.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 6770-6776
    • Zondervan, R.1    Kulzer, F.2    Orlinskii, S.B.3    Orrit, M.4
  • 19
    • 0032570470 scopus 로고    scopus 로고
    • Dynamics of the electron transfer reaction between an oxazine dye and DNA oligonucleotides monitored on the single molecule level
    • Sauer, M., K. H. Drexhage, U. Lieberwirth, R. Muller, S. Nord, and C. Zander. 1998. Dynamics of the electron transfer reaction between an oxazine dye and DNA oligonucleotides monitored on the single molecule level. Chem. Phys. Lett. 284:153-163.
    • (1998) Chem. Phys. Lett , vol.284 , pp. 153-163
    • Sauer, M.1    Drexhage, K.H.2    Lieberwirth, U.3    Muller, R.4    Nord, S.5    Zander, C.6
  • 20
    • 0035652115 scopus 로고    scopus 로고
    • Hubner, C. G., A. Renn, I. Reng e, and U. P. Wild. 2001. Direct observation of the triplet lifetime quenching of single dye molecules by molecular oxygen. J. Chem. Phys. 115:9619-9622.
    • Hubner, C. G., A. Renn, I. Reng e, and U. P. Wild. 2001. Direct observation of the triplet lifetime quenching of single dye molecules by molecular oxygen. J. Chem. Phys. 115:9619-9622.
  • 21
    • 31844456049 scopus 로고    scopus 로고
    • Oxygen-dependent photochemistry of fluorescent dyes studied at the single-molecule level
    • Renn, A., J. Seelig, and V. Sandoghdar. 2006. Oxygen-dependent photochemistry of fluorescent dyes studied at the single-molecule level. Mol. Phys. 104:409-414.
    • (2006) Mol. Phys , vol.104 , pp. 409-414
    • Renn, A.1    Seelig, J.2    Sandoghdar, V.3
  • 22
    • 15944428132 scopus 로고    scopus 로고
    • Optimal oxygen concentration for the detection of single indocarbocyanine molecules in a polymeric matrix
    • Piwonski, H., R. Kolos, A. Meixner, and J. Sepiol. 2005. Optimal oxygen concentration for the detection of single indocarbocyanine molecules in a polymeric matrix. Chem. Phys. Lett. 405:352-356.
    • (2005) Chem. Phys. Lett , vol.405 , pp. 352-356
    • Piwonski, H.1    Kolos, R.2    Meixner, A.3    Sepiol, J.4
  • 23
    • 0026761340 scopus 로고
    • Singlet oxygen induced DNA damage
    • Sies, H., and C. F. Menck. 1992. Singlet oxygen induced DNA damage. Mutat. Res. 275:367-375.
    • (1992) Mutat. Res , vol.275 , pp. 367-375
    • Sies, H.1    Menck, C.F.2
  • 24
    • 3042688696 scopus 로고    scopus 로고
    • Reactive species formed on proteins exposed to singlet oxygen
    • Davies, M. J. 2004. Reactive species formed on proteins exposed to singlet oxygen. Photochem. Photobiol. Sci. 3:17-25.
    • (2004) Photochem. Photobiol. Sci , vol.3 , pp. 17-25
    • Davies, M.J.1
  • 25
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada, Y., K. Sakurada, T. Aoki, D. D. Thomas, and T. Yanagida. 1990. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216:49-68.
    • (1990) J. Mol. Biol , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 26
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino, A., and T. Yanagida. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature. 334:74-76.
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 28
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and long lasting single-molecule fluorescence imaging
    • Rasnik, I., S. A. McKinney, and T. Ha. 2006. Nonblinking and long lasting single-molecule fluorescence imaging. Nat. Methods. 3:891-893.
    • (2006) Nat. Methods , vol.3 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 29
    • 33846964579 scopus 로고    scopus 로고
    • Strategies to improve photostabilities in ultrasensitive fluorescence spectroscopy
    • Widengren, J., A. Chmyrov, C. Eggeling, P. A. Lofdahl, and C. A. Seidel. 2007. Strategies to improve photostabilities in ultrasensitive fluorescence spectroscopy. J. Phys. Chem. A. 111:429-440.
    • (2007) J. Phys. Chem. A , vol.111 , pp. 429-440
    • Widengren, J.1    Chmyrov, A.2    Eggeling, C.3    Lofdahl, P.A.4    Seidel, C.A.5
  • 30
    • 2642522184 scopus 로고    scopus 로고
    • Combining optical trapping and single-molecule fluorescence spectroscopy: Enhanced photobleaching of fluorophores
    • van Dijk, M. A., L. C. Kapitein, J. van Mameren, C. F. Schmidt, and E. J. G. Peterman. 2004. Combining optical trapping and single-molecule fluorescence spectroscopy: enhanced photobleaching of fluorophores. J. Phys. Chem. B. 108:6479-6484.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6479-6484
    • van Dijk, M.A.1    Kapitein, L.C.2    van Mameren, J.3    Schmidt, C.F.4    Peterman, E.J.G.5
  • 31
    • 2642543406 scopus 로고    scopus 로고
    • Photodegradation of fluorescein in solutions containing n-propyl gallate
    • Gaigalas, A. K., L. Wang, K. D. Cole, and E. Humphries. 2004. Photodegradation of fluorescein in solutions containing n-propyl gallate. J. Phys. Chem. A. 108:4378-4384.
    • (2004) J. Phys. Chem. A , vol.108 , pp. 4378-4384
    • Gaigalas, A.K.1    Wang, L.2    Cole, K.D.3    Humphries, E.4
  • 32
    • 0035678612 scopus 로고    scopus 로고
    • Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two photon excitation
    • Dittrich, P. S., and P. Schwille. 2001. Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two photon excitation. Appl. Phys. B. 73:829-837.
    • (2001) Appl. Phys. B , vol.73 , pp. 829-837
    • Dittrich, P.S.1    Schwille, P.2
  • 33
    • 0032831171 scopus 로고    scopus 로고
    • Antifading agents for confocal fluorescence microscopy
    • Berrios, M., K. A. Conlon, and D. E. Colflesh. 1999. Antifading agents for confocal fluorescence microscopy. Methods Enzymol. 307:55-79.
    • (1999) Methods Enzymol , vol.307 , pp. 55-79
    • Berrios, M.1    Conlon, K.A.2    Colflesh, D.E.3
  • 34
    • 0029135913 scopus 로고
    • Analysis of antifading reagents for fluorescence microscopy
    • Florijn, R. J., J. Slats, H. J. Tanke, and A. K. Raap. 1995. Analysis of antifading reagents for fluorescence microscopy. Cytometry. 19:177-182.
    • (1995) Cytometry , vol.19 , pp. 177-182
    • Florijn, R.J.1    Slats, J.2    Tanke, H.J.3    Raap, A.K.4
  • 35
    • 0027495902 scopus 로고
    • Comparison of anti-fading agents used in fluorescence microscopy: Image analysis and laser confocal microscopy study
    • Longin, A., C. Souchier, M. Ffrench, and P. A. Bryon. 1993. Comparison of anti-fading agents used in fluorescence microscopy: image analysis and laser confocal microscopy study. J. Histochem. Cytochem. 41:1833-1840.
    • (1993) J. Histochem. Cytochem , vol.41 , pp. 1833-1840
    • Longin, A.1    Souchier, C.2    Ffrench, M.3    Bryon, P.A.4
  • 36
    • 0040369241 scopus 로고
    • DABCO stabilization of coumarin dye lasers
    • Von Trebra, R., and T. H. Koch. 1982. DABCO stabilization of coumarin dye lasers. Chem. Phys. Lett. 93:315-317.
    • (1982) Chem. Phys. Lett , vol.93 , pp. 315-317
    • Von Trebra, R.1    Koch, T.H.2
  • 38
    • 9244231291 scopus 로고    scopus 로고
    • Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxyogenase
    • Brown, C. K., M. W. Vetting, C. A. Earhart, and D. H. Ohlendorf. 2004. Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxyogenase. Annu. Rev. Microbiol. 58:555-585.
    • (2004) Annu. Rev. Microbiol , vol.58 , pp. 555-585
    • Brown, C.K.1    Vetting, M.W.2    Earhart, C.A.3    Ohlendorf, D.H.4
  • 39
    • 0019769046 scopus 로고
    • Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida-a new iron to subunit stoichiometry
    • Bull, C., and D. P. Ballou. 1981. Purification and properties of protocatechuate 3,4-dioxygenase from Pseudomonas putida-a new iron to subunit stoichiometry. J. Biol. Chem. 256:2673-2680.
    • (1981) J. Biol. Chem , vol.256 , pp. 2673-2680
    • Bull, C.1    Ballou, D.P.2
  • 40
    • 58649112617 scopus 로고
    • Nonheme iron intradiol catechol dioxygenases-structural and mechanistic studies
    • Ballou, D. P., C. Bull, and T. Walsh. 1981. Nonheme iron intradiol catechol dioxygenases-structural and mechanistic studies. Fed. Proc. 40:1554-1554
    • (1981) Fed. Proc , vol.40 , pp. 1554-1554
    • Ballou, D.P.1    Bull, C.2    Walsh, T.3
  • 41
    • 0034669323 scopus 로고    scopus 로고
    • The use of protocatechuate dioxygenase for maintaining anaerobic conditions in biochemical experiments
    • Patil, P. V., and D. P. Ballou. 2000. The use of protocatechuate dioxygenase for maintaining anaerobic conditions in biochemical experiments. Anal. Biochem. 286:187-192.
    • (2000) Anal. Biochem , vol.286 , pp. 187-192
    • Patil, P.V.1    Ballou, D.P.2
  • 42
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase
    • Ha, T., I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu. 2002. Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase. Nature. 419:638-641.
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1    Rasnik, I.2    Cheng, W.3    Babcock, H.P.4    Gauss, G.H.5    Lohman, T.M.6    Chu, S.7
  • 43
    • 0033567060 scopus 로고    scopus 로고
    • A comparison between the sulfhydryl reductants Tris(2-carboxyethyl) phosphine and dithiothreitol for use in protein biochemistry
    • Getz, E. B., M. Xiao, T. Chakrabarty, R. Cooke, and P. R. Selvin. 1999. A comparison between the sulfhydryl reductants Tris(2-carboxyethyl) phosphine and dithiothreitol for use in protein biochemistry. Anal. Biochem. 273:73-80.
    • (1999) Anal. Biochem , vol.273 , pp. 73-80
    • Getz, E.B.1    Xiao, M.2    Chakrabarty, T.3    Cooke, R.4    Selvin, P.R.5
  • 44
    • 0001153517 scopus 로고
    • Selective reduction of disulfides by Tris(2-carboxyethyl)phosphine
    • Burns, J. A., J. C. Butler, J. Moran, and G. M. Whitesides. 1991. Selective reduction of disulfides by Tris(2-carboxyethyl)phosphine. J. Org. Chem. 56:2648-2650.
    • (1991) J. Org. Chem , vol.56 , pp. 2648-2650
    • Burns, J.A.1    Butler, J.C.2    Moran, J.3    Whitesides, G.M.4
  • 45
    • 0023082770 scopus 로고
    • Chemical-reduction of disulfides
    • Jocelyn, P. C. 1987. Chemical-reduction of disulfides. Methods Enzymol. 143:246-256.
    • (1987) Methods Enzymol , vol.143 , pp. 246-256
    • Jocelyn, P.C.1
  • 46
    • 33947482089 scopus 로고
    • Dithiothreitol new protective reagent for SH groups
    • Cleland, W. W. 1964. Dithiothreitol new protective reagent for SH groups. Biochemistry. 3:480-182.
    • (1964) Biochemistry , vol.3 , pp. 480-182
    • Cleland, W.W.1
  • 47
    • 0029153356 scopus 로고
    • Rigidity of microtubules is increased by stabilizing agents
    • Mickey, B., and J. Howard. 1995. Rigidity of microtubules is increased by stabilizing agents. J. Cell Biol. 130:909-917.
    • (1995) J. Cell Biol , vol.130 , pp. 909-917
    • Mickey, B.1    Howard, J.2
  • 48
    • 0008767941 scopus 로고    scopus 로고
    • Singlet oxygen and dyetriplet-state quenching in solid-state dye lasers consisting of pyrromethene 567-doped poly(methyl methacrylate)
    • Ahmad, M., M. D. Rahn, andT. A. King. 1999. Singlet oxygen and dyetriplet-state quenching in solid-state dye lasers consisting of pyrromethene 567-doped poly(methyl methacrylate). Appl. Opt. 38:6337-6342.
    • (1999) Appl. Opt , vol.38 , pp. 6337-6342
    • Ahmad, M.M.D.1    Rahn2    andT3    King, A.4
  • 49
    • 0019943371 scopus 로고
    • Fluorescence microscopy-reduced photobleaching of rhodamine and fluorescein protein conjugates by normal-propyl gallate
    • Giloh, H., and J. W. Sedat. 1982. Fluorescence microscopy-reduced photobleaching of rhodamine and fluorescein protein conjugates by normal-propyl gallate. Science. 217:1252-1255.
    • (1982) Science , vol.217 , pp. 1252-1255
    • Giloh, H.1    Sedat, J.W.2
  • 50
    • 0014144495 scopus 로고
    • Studies on ascorbic acid. II. Physical changes in catalase following incubation with ascorbate or ascorbate and copper (II)
    • Orr, C. W. M. 1967. Studies on ascorbic acid. II. Physical changes in catalase following incubation with ascorbate or ascorbate and copper (II). Biochemistry. 6:3000-3006.
    • (1967) Biochemistry , vol.6 , pp. 3000-3006
    • Orr, C.W.M.1
  • 51
    • 0014144310 scopus 로고
    • Studies on ascorbic acid. I. Factors influencing ascorbate-mediated inhibition of catalase
    • Orr, C. W. M. 1967. Studies on ascorbic acid. I. Factors influencing ascorbate-mediated inhibition of catalase. Biochemistry. 6:2995-3000.
    • (1967) Biochemistry , vol.6 , pp. 2995-3000
    • Orr, C.W.M.1
  • 52
    • 0001266770 scopus 로고
    • Purification and partial characterization of three genetically defined classes of maize
    • Chandlee, J. M., A. S. Tsaftaris, and J. G. Scandalios. 1983. Purification and partial characterization of three genetically defined classes of maize. Plant Sci. Lett. 29:117-131.
    • (1983) Plant Sci. Lett , vol.29 , pp. 117-131
    • Chandlee, J.M.1    Tsaftaris, A.S.2    Scandalios, J.G.3
  • 53
    • 0032006806 scopus 로고    scopus 로고
    • Hemoglobin-oxygen equilibrium curvs measured during enzymatic oxygen consumption
    • Vandegriff, K. D., R. J. Rohlfs, M. D. Magde, and R. M. Winslow. 1998. Hemoglobin-oxygen equilibrium curvs measured during enzymatic oxygen consumption. Anal. Biochem. 256:107-116.
    • (1998) Anal. Biochem , vol.256 , pp. 107-116
    • Vandegriff, K.D.1    Rohlfs, R.J.2    Magde, M.D.3    Winslow, R.M.4
  • 55
    • 0242684545 scopus 로고    scopus 로고
    • Identification of an antioxidant, ethyl protocatechuate, in peanut seed testa
    • Huang, S. C., G. C. Yen, L. W. Chang, W. J. Yen, and P. D. Duh. 2003. Identification of an antioxidant, ethyl protocatechuate, in peanut seed testa. J. Agric. Food Chem. 51:2380-2383.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 2380-2383
    • Huang, S.C.1    Yen, G.C.2    Chang, L.W.3    Yen, W.J.4    Duh, P.D.5
  • 56
    • 12244260059 scopus 로고    scopus 로고
    • Spectroscopic study and evaluation of red-absorbing fluorescent dyes
    • Buschmann, V., K. D. Weston, and M. Sauer. 2003. Spectroscopic study and evaluation of red-absorbing fluorescent dyes. Bioconjug. Chem. 14:195-204.
    • (2003) Bioconjug. Chem , vol.14 , pp. 195-204
    • Buschmann, V.1    Weston, K.D.2    Sauer, M.3
  • 57
    • 33645678319 scopus 로고    scopus 로고
    • Analysis of photobleaching in single-molecule multicolor excitation and Forster resonance energy transfer measurement
    • Eggeling, C., J. Widengren, L. Brand, J. Schaffer, S. Felekyan, and C. A. M. Seidel. 2006. Analysis of photobleaching in single-molecule multicolor excitation and Forster resonance energy transfer measurement. J. Phys. Chem. A. 110:2979-2995.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 2979-2995
    • Eggeling, C.1    Widengren, J.2    Brand, L.3    Schaffer, J.4    Felekyan, S.5    Seidel, C.A.M.6
  • 58
    • 85003238673 scopus 로고    scopus 로고
    • Photodestruction intermediates probed by an adjacent reporter molecule
    • Ha, T., and J. Xu. 2003. Photodestruction intermediates probed by an adjacent reporter molecule. Phys. Rev. Lett. 90:223002.
    • (2003) Phys. Rev. Lett , vol.90 , pp. 223002
    • Ha, T.1    Xu, J.2
  • 59
    • 15744396330 scopus 로고    scopus 로고
    • Carbocyanine dyes as efficient reversible single-molecule optical switch
    • Heilemann, M., E. Margeat, R. Kasper, M. Sauer, and P. Tinnefeld.2005. Carbocyanine dyes as efficient reversible single-molecule optical switch. J. Am. Chem. Soc. 127:3801-3806.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 3801-3806
    • Heilemann, M.1    Margeat, E.2    Kasper, R.3    Sauer, M.4    Tinnefeld, P.5
  • 60
    • 31144474579 scopus 로고    scopus 로고
    • Spectral identification of specific photophysics of Cy5 by means of ensemble and single-molecule measurements
    • Huang, Z. X., D. M. Ji, S. F. Wang, A. D. Xia, F. Koberling, M. Patting, and R. Erdmann. 2006. Spectral identification of specific photophysics of Cy5 by means of ensemble and single-molecule measurements. J. Phys. Chem. A. 110:45-50.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 45-50
    • Huang, Z.X.1    Ji, D.M.2    Wang, S.F.3    Xia, A.D.4    Koberling, F.5    Patting, M.6    Erdmann, R.7
  • 61
    • 20444373042 scopus 로고    scopus 로고
    • Direct observation of delayed fluorescence from a remarkable back- isomerization in Cy5
    • Huang, Z. X., D. M. Ji, A. D. Xia, F. Koberling, M. Patting, and R. Erdmann. 2005. Direct observation of delayed fluorescence from a remarkable back- isomerization in Cy5. J. Am. Chem. Soc. 127:8064-8066.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 8064-8066
    • Huang, Z.X.1    Ji, D.M.2    Xia, A.D.3    Koberling, F.4    Patting, M.5    Erdmann, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.