메뉴 건너뛰기




Volumn 450, Issue , 2008, Pages 159-183

Chapter 8 Ultrafast Fluorescence Spectroscopy via Upconversion. Applications to Biophysics

Author keywords

[No Author keywords available]

Indexed keywords

TRYPTOPHAN; NUCLEIC ACID; PEPTIDE; PROTEIN;

EID: 58249130415     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)03408-3     Document Type: Review
Times cited : (37)

References (82)
  • 1
    • 34547551083 scopus 로고    scopus 로고
    • Measurement of solvation responses at multiple sites in a globular protein
    • Abbyad P., Shi X., Childs W., McAnaney T., Cohen B., and Boxer S. Measurement of solvation responses at multiple sites in a globular protein. J. Phys. Chem. B 111 (2007) 8269
    • (2007) J. Phys. Chem. B , vol.111 , pp. 8269
    • Abbyad, P.1    Shi, X.2    Childs, W.3    McAnaney, T.4    Cohen, B.5    Boxer, S.6
  • 2
    • 0023357309 scopus 로고
    • Interpretation of fluorescence decays in proteins using continuous lifetime distributions
    • Alcala J.R., Gratton E., and Prendergast F.G. Interpretation of fluorescence decays in proteins using continuous lifetime distributions. Biophys. J. 51 (1987) 925
    • (1987) Biophys. J. , vol.51 , pp. 925
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 5
    • 14144250730 scopus 로고    scopus 로고
    • Design and characterization of a femtosecond fluorescence spectrometer based on optical Kerr gating
    • Arzhantsev S., and Maroncelli M. Design and characterization of a femtosecond fluorescence spectrometer based on optical Kerr gating. Appl. Spectrosc. 59 (2005) 206
    • (2005) Appl. Spectrosc. , vol.59 , pp. 206
    • Arzhantsev, S.1    Maroncelli, M.2
  • 6
    • 4043074486 scopus 로고
    • Picosecond time-resolved fluorescence study of s-tetrazine vibrational-relaxation in solution
    • Barbara P.F., Brus L.E., and Reutzepis P.P. Picosecond time-resolved fluorescence study of s-tetrazine vibrational-relaxation in solution. Chem. Phys. Lett. 69 (1980) 447
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 447
    • Barbara, P.F.1    Brus, L.E.2    Reutzepis, P.P.3
  • 8
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem J.M., and Brand L. Time-resolved fluorescence of proteins. Annu. Rev. Biochem. 54 (1985) 43
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 43
    • Beechem, J.M.1    Brand, L.2
  • 9
    • 0019025130 scopus 로고
    • Intensity dependent time resolution and dynamic-range of photochron picosecond streak cameras to linear photoelectric recording
    • Bradley D.J., Bryant S.F., and Sibbett W. Intensity dependent time resolution and dynamic-range of photochron picosecond streak cameras to linear photoelectric recording. Rev. Sci. Instrum. 51 (1980) 824
    • (1980) Rev. Sci. Instrum. , vol.51 , pp. 824
    • Bradley, D.J.1    Bryant, S.F.2    Sibbett, W.3
  • 10
    • 0020704054 scopus 로고
    • A new synchroscan streak-camera readout system for use with CW mode-locked lasers
    • Bradley D.J., Mcinerney J., Dennis W.M., and Taylor J.R. A new synchroscan streak-camera readout system for use with CW mode-locked lasers. Opt. Commun. 44 (1983) 357
    • (1983) Opt. Commun. , vol.44 , pp. 357
    • Bradley, D.J.1    Mcinerney, J.2    Dennis, W.M.3    Taylor, J.R.4
  • 11
    • 0002983460 scopus 로고
    • Time-domain fluorescence spectroscopy using time-correlated single-photon counting
    • Lakowicz J.R. (Ed), Plenum Press, New York
    • Birch D.J., and Imhof R.E. Time-domain fluorescence spectroscopy using time-correlated single-photon counting. In: Lakowicz J.R. (Ed). Topics in fluorescence spectroscopy Vol. 1 (1991), Plenum Press, New York 1-95
    • (1991) Topics in fluorescence spectroscopy , vol.1 , pp. 1-95
    • Birch, D.J.1    Imhof, R.E.2
  • 12
    • 0032535874 scopus 로고    scopus 로고
    • Subpicosecond fluorescence upconversion measurements of primary events in yellow proteins
    • Changenet P., Zhang H., and Van der Meer M.J. Subpicosecond fluorescence upconversion measurements of primary events in yellow proteins. Chem. Phys. Lett. 282 (1998) 276
    • (1998) Chem. Phys. Lett. , vol.282 , pp. 276
    • Changenet, P.1    Zhang, H.2    Van der Meer, M.J.3
  • 13
    • 0025830305 scopus 로고
    • Fluorescence of tryptophan dipeptides-correlations with the rotamer model
    • Chen R.F., Knutson J.R., Ziffer H., and Porter D. Fluorescence of tryptophan dipeptides-correlations with the rotamer model. Biochemistry 30 (1991) 5184
    • (1991) Biochemistry , vol.30 , pp. 5184
    • Chen, R.F.1    Knutson, J.R.2    Ziffer, H.3    Porter, D.4
  • 14
    • 0038672775 scopus 로고    scopus 로고
    • Picosecond dynamics of a peptide from the acetylcholine receptor interacting with a neurotoxin probed by tailored tryptophan fluorescence
    • Chowdhury P., Gondry M., Genet R., Martin J.L., Menez A., Negrerie M., and Petrich J.W. Picosecond dynamics of a peptide from the acetylcholine receptor interacting with a neurotoxin probed by tailored tryptophan fluorescence. Photochem. Photobiol. 77 (2003) 151
    • (2003) Photochem. Photobiol. , vol.77 , pp. 151
    • Chowdhury, P.1    Gondry, M.2    Genet, R.3    Martin, J.L.4    Menez, A.5    Negrerie, M.6    Petrich, J.W.7
  • 15
    • 0033002410 scopus 로고    scopus 로고
    • Tryptophan rotamer distributions in amphipathic peptides at a lipid surface
    • Clayton A., and Sawyer W. Tryptophan rotamer distributions in amphipathic peptides at a lipid surface. Biophys. J. 76 (1999) 3235
    • (1999) Biophys. J. , vol.76 , pp. 3235
    • Clayton, A.1    Sawyer, W.2
  • 16
    • 0037204951 scopus 로고    scopus 로고
    • Probing protein electrostatics with a synthetic fluorescent amino acid
    • Cohen B., McAnaney T., Park E., Jan Y., Boxer S., and Jan L. Probing protein electrostatics with a synthetic fluorescent amino acid. Science 296 (2002) 1700
    • (2002) Science , vol.296 , pp. 1700
    • Cohen, B.1    McAnaney, T.2    Park, E.3    Jan, Y.4    Boxer, S.5    Jan, L.6
  • 17
    • 15544379587 scopus 로고    scopus 로고
    • Tryptophan interactions with glycerol/water and trehalose/sucrose cryosolvents: Infrared and fluorescence spectroscopy and ab initio calculations
    • Dashnau J.L., Zelent B., and Vanderkooi J.M. Tryptophan interactions with glycerol/water and trehalose/sucrose cryosolvents: Infrared and fluorescence spectroscopy and ab initio calculations. Biophys. Chem. 114 (2005) 71
    • (2005) Biophys. Chem. , vol.114 , pp. 71
    • Dashnau, J.L.1    Zelent, B.2    Vanderkooi, J.M.3
  • 18
    • 0344028031 scopus 로고
    • Optical sampling of subnanosecond light pulses
    • Duguay M.A., and Hansen J.W. Optical sampling of subnanosecond light pulses. Appl. Phys. Lett. 13 (1968) 178
    • (1968) Appl. Phys. Lett. , vol.13 , pp. 178
    • Duguay, M.A.1    Hansen, J.W.2
  • 19
    • 84954718626 scopus 로고
    • Electrooptic, linear, and nonliner optical-properties of KDP and its isomorphs
    • Eimerl D. Electrooptic, linear, and nonliner optical-properties of KDP and its isomorphs. Ferroelectrics 72 (1987) 397
    • (1987) Ferroelectrics , vol.72 , pp. 397
    • Eimerl, D.1
  • 20
    • 33748194569 scopus 로고    scopus 로고
    • Ultrafast photoisomerization of photoactive yellow protein chromophore analogues in solution: Influence of the protonation state
    • Espagne A., Paik D.H., Changenet-Barret P., Martin M.M., and Zewail A.H. Ultrafast photoisomerization of photoactive yellow protein chromophore analogues in solution: Influence of the protonation state. Chem. Phys. Lett. 7 (2006) 1717
    • (2006) Chem. Phys. Lett. , vol.7 , pp. 1717
    • Espagne, A.1    Paik, D.H.2    Changenet-Barret, P.3    Martin, M.M.4    Zewail, A.H.5
  • 23
    • 84975659967 scopus 로고
    • Compression of optical pulses to 6 femtoseconds by using cubic phase compensation
    • Fork R.L., Brito C.H., Becker P.C., and Shank C.V. Compression of optical pulses to 6 femtoseconds by using cubic phase compensation. Opt. Lett. 12 (1987) 483
    • (1987) Opt. Lett. , vol.12 , pp. 483
    • Fork, R.L.1    Brito, C.H.2    Becker, P.C.3    Shank, C.V.4
  • 24
    • 34147207323 scopus 로고    scopus 로고
    • The partially unfolded state of beta-momorcharin characterized with steady-state and time-resolved fluorescence studies
    • Fukunaga Y., Nishimoto E., Yamashita K., Otosu T., and Yamashita S. The partially unfolded state of beta-momorcharin characterized with steady-state and time-resolved fluorescence studies. J. Biochem. 141 (2007) 9
    • (2007) J. Biochem. , vol.141 , pp. 9
    • Fukunaga, Y.1    Nishimoto, E.2    Yamashita, K.3    Otosu, T.4    Yamashita, S.5
  • 25
    • 0029478993 scopus 로고
    • Temperature dispersion of refractive-indexes in beta-bab2o4 and lib3o5 crystals for nonlinear-optical devices
    • Ghosh G. Temperature dispersion of refractive-indexes in beta-bab2o4 and lib3o5 crystals for nonlinear-optical devices. J. Appl. Phys. 78 (1995) 6752
    • (1995) J. Appl. Phys. , vol.78 , pp. 6752
    • Ghosh, G.1
  • 26
    • 34249012748 scopus 로고    scopus 로고
    • Ab initio study of the excited-state deactivation pathways of protonated tryptophan and tyrosine
    • Gregoire G., Jouvet C., Dedonder C., and Sobolewski A. Ab initio study of the excited-state deactivation pathways of protonated tryptophan and tyrosine. J. Am. Chem. Soc. 129 (2007) 6223
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6223
    • Gregoire, G.1    Jouvet, C.2    Dedonder, C.3    Sobolewski, A.4
  • 27
    • 0016075864 scopus 로고
    • Analysis of fluorescence decay kinetics by method of least-squares
    • Grinvald A., and Steinberg I.Z. Analysis of fluorescence decay kinetics by method of least-squares. Anal. Biochem. 59 (1974) 583
    • (1974) Anal. Biochem. , vol.59 , pp. 583
    • Grinvald, A.1    Steinberg, I.Z.2
  • 28
    • 16244370128 scopus 로고    scopus 로고
    • Incorporation of highly dispersed gold nanoparticles into the pore channels of mesoporous silica thin films and their ultrafast nonlinear optical response
    • Gu J.L., Shi J.L., You G.J., Xiong L.M., Qian S.X., Hua Z.L., and Chen H.R. Incorporation of highly dispersed gold nanoparticles into the pore channels of mesoporous silica thin films and their ultrafast nonlinear optical response. Adv. Mater. 17 (2005) 557
    • (2005) Adv. Mater. , vol.17 , pp. 557
    • Gu, J.L.1    Shi, J.L.2    You, G.J.3    Xiong, L.M.4    Qian, S.X.5    Hua, Z.L.6    Chen, H.R.7
  • 29
    • 31544440193 scopus 로고    scopus 로고
    • Singlet excited-state behavior of uracil and thymine in aqueous solution: A combined experimental and computational study of 11 uracil derivatives
    • Gustavsson T., Banyasz A., Lazzarotto E., Markovitsi D., Scalmani G., Frisch M., Barone V., and Improta R. Singlet excited-state behavior of uracil and thymine in aqueous solution: A combined experimental and computational study of 11 uracil derivatives. J. Am. Chem. Soc. 128 (2006) 607
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 607
    • Gustavsson, T.1    Banyasz, A.2    Lazzarotto, E.3    Markovitsi, D.4    Scalmani, G.5    Frisch, M.6    Barone, V.7    Improta, R.8
  • 30
    • 33748894317 scopus 로고    scopus 로고
    • Singlet excited state dynamics of uracil and thymine derivatives: A femtosecond fluorescence upconversion study in acetonitrile
    • Gustavsson T., Sarkar N., Lazzarotto E., Markovitsi D., Scalmani G., Frisch M., and Improta R. Singlet excited state dynamics of uracil and thymine derivatives: A femtosecond fluorescence upconversion study in acetonitrile. Chem. Phys. Lett. 429 (2006) 551
    • (2006) Chem. Phys. Lett. , vol.429 , pp. 551
    • Gustavsson, T.1    Sarkar, N.2    Lazzarotto, E.3    Markovitsi, D.4    Scalmani, G.5    Frisch, M.6    Improta, R.7
  • 31
    • 0003504720 scopus 로고
    • Picosecond luminescence detection using type-2 phase-matched frequency-conversion
    • Halliday L., and Topp M. Picosecond luminescence detection using type-2 phase-matched frequency-conversion. Chem. Phys. Lett. 46 (1977) 8
    • (1977) Chem. Phys. Lett. , vol.46 , pp. 8
    • Halliday, L.1    Topp, M.2
  • 32
    • 33947093414 scopus 로고
    • Picosecond optical pulse sampling by frequency-conversion - studies of solvent-induced molecular relaxation
    • Halliday L., and Topp M. Picosecond optical pulse sampling by frequency-conversion - studies of solvent-induced molecular relaxation. J. Phys. Chem. 82 (1978) 2273
    • (1978) J. Phys. Chem. , vol.82 , pp. 2273
    • Halliday, L.1    Topp, M.2
  • 33
    • 0017868544 scopus 로고
    • Picosecond flash-photolysis in biology and biophysics
    • Holten D., and Windsor M.W. Picosecond flash-photolysis in biology and biophysics. Annu. Rev. Biophys. 7 (1978) 189
    • (1978) Annu. Rev. Biophys. , vol.7 , pp. 189
    • Holten, D.1    Windsor, M.W.2
  • 34
    • 28144457206 scopus 로고    scopus 로고
    • Excitation decay pathways of Lhca proteins: A time-resolved fluorescence study
    • Ihalainen J.A., Croce R., and Morosiuotto T. Excitation decay pathways of Lhca proteins: A time-resolved fluorescence study. J. Phys. Chem. B 109 (2005) 21150
    • (2005) J. Phys. Chem. B , vol.109 , pp. 21150
    • Ihalainen, J.A.1    Croce, R.2    Morosiuotto, T.3
  • 35
    • 0010179173 scopus 로고    scopus 로고
    • Quartic phase compensation with a standard grating compressor
    • Inchauspe C.M.G., and Martinez O.E. Quartic phase compensation with a standard grating compressor. Opt. Lett. 22 (1997) 1186
    • (1997) Opt. Lett. , vol.22 , pp. 1186
    • Inchauspe, C.M.G.1    Martinez, O.E.2
  • 36
    • 58249132090 scopus 로고
    • Sub-picosecond spectroscopy
    • Ippen E.P., and Shank C.V. Sub-picosecond spectroscopy. Phys. Today 31 (1978) 41
    • (1978) Phys. Today , vol.31 , pp. 41
    • Ippen, E.P.1    Shank, C.V.2
  • 38
    • 84975655083 scopus 로고
    • Prism-pair dispersive delay-lines in optical pulse-compression
    • Kafka J.D., and Baer T. Prism-pair dispersive delay-lines in optical pulse-compression. Opt. Lett. 12 (1987) 401
    • (1987) Opt. Lett. , vol.12 , pp. 401
    • Kafka, J.D.1    Baer, T.2
  • 39
    • 33645916355 scopus 로고
    • Ultrafast emission-spectroscopy in the ultraviolet by time-gated upconversion
    • Kahlow M.A., Jarzeba W., Dubruil T.P., and Barbara P.F. Ultrafast emission-spectroscopy in the ultraviolet by time-gated upconversion. Rev. Sci. Instrum. 59 (1988) 1098
    • (1988) Rev. Sci. Instrum. , vol.59 , pp. 1098
    • Kahlow, M.A.1    Jarzeba, W.2    Dubruil, T.P.3    Barbara, P.F.4
  • 40
    • 0035902395 scopus 로고    scopus 로고
    • Light harvesting by chlorophylls and carotenoids in the photosystem I core complex of synechococcus elongatus: A fluorescence upconversion study
    • Kennis J.T.M., Gobets B., van Stokkum I.H.M., Dekker J.P., van Grondelle R., and Fleming G.R. Light harvesting by chlorophylls and carotenoids in the photosystem I core complex of synechococcus elongatus: A fluorescence upconversion study. J. Phys. Chem. B 105 (2001) 4485
    • (2001) J. Phys. Chem. B , vol.105 , pp. 4485
    • Kennis, J.T.M.1    Gobets, B.2    van Stokkum, I.H.M.3    Dekker, J.P.4    van Grondelle, R.5    Fleming, G.R.6
  • 41
    • 13444271832 scopus 로고    scopus 로고
    • Photophysics of tryptophan fluorescence: Link with the catalytic strategy of the citrate synthase from thermoplasma acidophilum
    • Kurz L.C., Fite B., Jean J., Park J., Erpelding T., and Callis P. Photophysics of tryptophan fluorescence: Link with the catalytic strategy of the citrate synthase from thermoplasma acidophilum. Biochemistry 44 (2005) 1394
    • (2005) Biochemistry , vol.44 , pp. 1394
    • Kurz, L.C.1    Fite, B.2    Jean, J.3    Park, J.4    Erpelding, T.5    Callis, P.6
  • 43
    • 0034309767 scopus 로고    scopus 로고
    • On spectral relaxation in proteins
    • Lakowicz J.R. On spectral relaxation in proteins. Photochem. Photobiol. 72 (2000) 421
    • (2000) Photochem. Photobiol. , vol.72 , pp. 421
    • Lakowicz, J.R.1
  • 44
    • 4344608081 scopus 로고    scopus 로고
    • Excited-state axial-ligand photodissociation and nonpolar protein-matrix reorganization in zn(II)-substituted cytochrome c
    • Lampa-Pastrk S., Lafuente R.C., and Beck W.F. Excited-state axial-ligand photodissociation and nonpolar protein-matrix reorganization in zn(II)-substituted cytochrome c. J. Phys. Chem. B 108 (2004) 12602
    • (2004) J. Phys. Chem. B , vol.108 , pp. 12602
    • Lampa-Pastrk, S.1    Lafuente, R.C.2    Beck, W.F.3
  • 45
    • 33947425139 scopus 로고    scopus 로고
    • Hydration dynamics and time scales of coupled water-protein fluctuations
    • Li T., Hassanali A.A., Kao Y., Zhong D., and Singer S.J. Hydration dynamics and time scales of coupled water-protein fluctuations. J. Am. Chem. Soc. 129 (2007) 3376
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3376
    • Li, T.1    Hassanali, A.A.2    Kao, Y.3    Zhong, D.4    Singer, S.J.5
  • 46
    • 0033321570 scopus 로고    scopus 로고
    • Optimum phase matching and effective nonlinear coefficients of lbo and ktp for continuously changing wavelength
    • Liu L.Q., and Nagashima K. Optimum phase matching and effective nonlinear coefficients of lbo and ktp for continuously changing wavelength. Opt. Laser Technol. 31 (1999) 283
    • (1999) Opt. Laser Technol. , vol.31 , pp. 283
    • Liu, L.Q.1    Nagashima, K.2
  • 47
    • 1842525751 scopus 로고    scopus 로고
    • Femtosecond studies of tryptophan solvation: Correlation function and water dynamics at lipid surfaces
    • Lu W., Kim J., Qiu W., and Zhong D. Femtosecond studies of tryptophan solvation: Correlation function and water dynamics at lipid surfaces. Chem. Phys. Lett. 388 (2004) 120
    • (2004) Chem. Phys. Lett. , vol.388 , pp. 120
    • Lu, W.1    Kim, J.2    Qiu, W.3    Zhong, D.4
  • 48
    • 0016470126 scopus 로고
    • Optical up-conversion light gate with picosecond resolution
    • Mahr H., and Hirsch M.D. Optical up-conversion light gate with picosecond resolution. Opt. Commun. 13 (1975) 96
    • (1975) Opt. Commun. , vol.13 , pp. 96
    • Mahr, H.1    Hirsch, M.D.2
  • 49
    • 0027415480 scopus 로고
    • Monitoring conformational change in the human erythrocyte glucose carrier - use of a fluorescent-probe attached to an exofacial carrier sulfhydryl
    • May J.M., and Beechem J.M. Monitoring conformational change in the human erythrocyte glucose carrier - use of a fluorescent-probe attached to an exofacial carrier sulfhydryl. Biochemistry 32 (1993) 2907
    • (1993) Biochemistry , vol.32 , pp. 2907
    • May, J.M.1    Beechem, J.M.2
  • 51
    • 36749084541 scopus 로고    scopus 로고
    • Ultrafast excited-state deactivation and energy transfer in guanine-cytosine DNA double helices
    • Miannay F., Bányász A., Gustavsson T., and Markovitsi D. Ultrafast excited-state deactivation and energy transfer in guanine-cytosine DNA double helices. J. Am. Chem. Soc. 129 (2007) 14574
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14574
    • Miannay, F.1    Bányász, A.2    Gustavsson, T.3    Markovitsi, D.4
  • 52
    • 36449007809 scopus 로고
    • Hybrid simulations of solvation effects on electronic-spectra - indoles in water
    • Muino P.L., and Callis P.R. Hybrid simulations of solvation effects on electronic-spectra - indoles in water. J. Chem. Phys. 100 (1994) 4093
    • (1994) J. Chem. Phys. , vol.100 , pp. 4093
    • Muino, P.L.1    Callis, P.R.2
  • 53
    • 0030576368 scopus 로고    scopus 로고
    • Primary charge separation processes in reaction centers of an antenna-free mutant of Rhodobacter capsulatus
    • Muller M.G., Drews G., and Holzwarth A. Primary charge separation processes in reaction centers of an antenna-free mutant of Rhodobacter capsulatus. Chem. Phys. Lett. 258 (1996) 194
    • (1996) Chem. Phys. Lett. , vol.258 , pp. 194
    • Muller, M.G.1    Drews, G.2    Holzwarth, A.3
  • 54
    • 84975571164 scopus 로고
    • Applicability of a microchannel plate photo-multiplier to the time-correlated photon-counting technique
    • Murao T., Yamazaki I., and Yoshihara K. Applicability of a microchannel plate photo-multiplier to the time-correlated photon-counting technique. Appl. Opt. 21 (1982) 2297
    • (1982) Appl. Opt. , vol.21 , pp. 2297
    • Murao, T.1    Yamazaki, I.2    Yoshihara, K.3
  • 56
    • 33646369664 scopus 로고    scopus 로고
    • Dependence of tryptophan emission wavelength on conformation in cyclic hexapeptides
    • Pan C.P., Callis P.R., and Barkley M.D. Dependence of tryptophan emission wavelength on conformation in cyclic hexapeptides. J. Phys. Chem. B 110 (2006) 7009
    • (2006) J. Phys. Chem. B , vol.110 , pp. 7009
    • Pan, C.P.1    Callis, P.R.2    Barkley, M.D.3
  • 57
    • 33745470061 scopus 로고    scopus 로고
    • Ultrafast solvation dynamics of human serum albumin: Correlations with conformational transitions and site-selected recognition
    • Qiu W., Zhang L., Okobiah O., Yang Y., Wang L., Zhong D., and Zewail A.H. Ultrafast solvation dynamics of human serum albumin: Correlations with conformational transitions and site-selected recognition. J. Phys. Chem. B 110 (2006) 10540
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10540
    • Qiu, W.1    Zhang, L.2    Okobiah, O.3    Yang, Y.4    Wang, L.5    Zhong, D.6    Zewail, A.H.7
  • 58
    • 0026552305 scopus 로고
    • Correlation of tryptophan fluorescence intensity decay parameters with H-1 NMR-determined rotamer conformations-[tryptophan2]oxytocin
    • Ross J.A., Wyssbrod H.R., Porter R.A., Schwartz G.P., Michaels C.A., and Laws W.R. Correlation of tryptophan fluorescence intensity decay parameters with H-1 NMR-determined rotamer conformations-[tryptophan2]oxytocin. Biochemistry 31 (1992) 1585
    • (1992) Biochemistry , vol.31 , pp. 1585
    • Ross, J.A.1    Wyssbrod, H.R.2    Porter, R.A.3    Schwartz, G.P.4    Michaels, C.A.5    Laws, W.R.6
  • 59
    • 0001253401 scopus 로고    scopus 로고
    • Vibrational coherence in electron donor-acceptor complexes
    • Rubtsov I.V., and Yoshihara K. Vibrational coherence in electron donor-acceptor complexes. J. Phys. Chem. A 103 (1999) 10202
    • (1999) J. Phys. Chem. A , vol.103 , pp. 10202
    • Rubtsov, I.V.1    Yoshihara, K.2
  • 60
    • 0025255660 scopus 로고
    • Subpicosecond fluorescence anisotropy studies of tryptophan in water
    • Ruggiero A.J., Todd D.C., and Fleming G.R. Subpicosecond fluorescence anisotropy studies of tryptophan in water. J. Am. Chem. Soc. 112 (1990) 1003
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1003
    • Ruggiero, A.J.1    Todd, D.C.2    Fleming, G.R.3
  • 62
    • 0029515093 scopus 로고
    • SHG phase matching conditions for undoped and doped lithium niobate
    • Schlarb U., Reichert A., and Betzler K. SHG phase matching conditions for undoped and doped lithium niobate. Radiat. Eff. Defects Solids 136 (1995) 1029
    • (1995) Radiat. Eff. Defects Solids , vol.136 , pp. 1029
    • Schlarb, U.1    Reichert, A.2    Betzler, K.3
  • 63
    • 28444473536 scopus 로고    scopus 로고
    • Simulation of fluorescence anisotropy experiments: Probing protein dynamics
    • Schroder G.F., Alexiev U., and Gubmuller H. Simulation of fluorescence anisotropy experiments: Probing protein dynamics. Biophys. J. 89 (2005) 3757
    • (2005) Biophys. J. , vol.89 , pp. 3757
    • Schroder, G.F.1    Alexiev, U.2    Gubmuller, H.3
  • 64
    • 34547681413 scopus 로고    scopus 로고
    • Ultrafast electronic relaxation in guanosine is promoted by hydrogen bonding with cytidine
    • Schwalb N., and Temps F. Ultrafast electronic relaxation in guanosine is promoted by hydrogen bonding with cytidine. J. Am. Chem. Soc. 129 (2007) 9272
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9272
    • Schwalb, N.1    Temps, F.2
  • 65
    • 53749094033 scopus 로고    scopus 로고
    • Base sequence and higher-order structure induce the complex excited-state dynamics in DNA
    • Schwalb N., and Temps F. Base sequence and higher-order structure induce the complex excited-state dynamics in DNA. Sciences 322 (2008) 243
    • (2008) Sciences , vol.322 , pp. 243
    • Schwalb, N.1    Temps, F.2
  • 67
    • 0001734289 scopus 로고    scopus 로고
    • Femtosecond internal conversion and reorientation of 5-methoxyindole in hexadecane
    • Shen X., and Knutson J.R. Femtosecond internal conversion and reorientation of 5-methoxyindole in hexadecane. Chem. Phys. Lett. 339 (2001) 191
    • (2001) Chem. Phys. Lett. , vol.339 , pp. 191
    • Shen, X.1    Knutson, J.R.2
  • 68
    • 0035812107 scopus 로고    scopus 로고
    • Subpicosecond fluorescence spectra of tryptophan in water
    • Shen X., and Knutson J.R. Subpicosecond fluorescence spectra of tryptophan in water. J. Phys. Chem. B 105 (2001) 6260
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6260
    • Shen, X.1    Knutson, J.R.2
  • 69
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous-solution
    • Szabo A.G., and Rayner D.M. Fluorescence decay of tryptophan conformers in aqueous-solution. J. Am. Chem. Soc. 102 (1980) 554
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554
    • Szabo, A.G.1    Rayner, D.M.2
  • 70
    • 84973001389 scopus 로고
    • Pulsed laser spectroscopy
    • Topp M.R. Pulsed laser spectroscopy. Appl. Spectrosc. Rev. 14 (1979) 1
    • (1979) Appl. Spectrosc. Rev. , vol.14 , pp. 1
    • Topp, M.R.1
  • 71
    • 0035868719 scopus 로고    scopus 로고
    • Homogeneous spectrally- and time-resolved fluorescence emission from single-tryptophan mutants of IIA(Glc) protein
    • Toptygin D., Savtchenko R., Meadow D., and Brand L. Homogeneous spectrally- and time-resolved fluorescence emission from single-tryptophan mutants of IIA(Glc) protein. J. Phys. Chem. B 105 (2001) 2043
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2043
    • Toptygin, D.1    Savtchenko, R.2    Meadow, D.3    Brand, L.4
  • 72
    • 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. 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 (2006) 26292
    • (2006) J. Phys. Chem. B , vol.110 , pp. 26292
    • Toptygin, D.1    Gronenborn, A.M.2    Brand, L.3
  • 73
    • 33646251145 scopus 로고    scopus 로고
    • (Sub)-picosecond spectral evolution of fluorescence in photoactive proteins studied with a synchroscan streak camera system
    • Van Stokkum I.H.M., Gobets B., and Gensch T. (Sub)-picosecond spectral evolution of fluorescence in photoactive proteins studied with a synchroscan streak camera system. Photochem. Photobiol. 82 (2006) 380
    • (2006) Photochem. Photobiol. , vol.82 , pp. 380
    • Van Stokkum, I.H.M.1    Gobets, B.2    Gensch, T.3
  • 74
    • 33751156520 scopus 로고
    • Solvent relaxation around the excited-state of indole - analysis of fluorescence lifetime distributions and time-dependence spectral shifts
    • Vincent M., Gallay J., and Demchenko A.P. Solvent relaxation around the excited-state of indole - analysis of fluorescence lifetime distributions and time-dependence spectral shifts. J. Phys. Chem. 99 (1995) 14931
    • (1995) J. Phys. Chem. , vol.99 , pp. 14931
    • Vincent, M.1    Gallay, J.2    Demchenko, A.P.3
  • 77
    • 0037438846 scopus 로고    scopus 로고
    • Femtosecond optical Kerr shutter using lead-bismuth-gallium oxide glass
    • Yu B.L., Bykov A.B., and Qiu T. Femtosecond optical Kerr shutter using lead-bismuth-gallium oxide glass. Opt. Commun. 215 (2003) 407
    • (2003) Opt. Commun. , vol.215 , pp. 407
    • Yu, B.L.1    Bykov, A.B.2    Qiu, T.3
  • 78
    • 33751213387 scopus 로고    scopus 로고
    • Protonation of excited state pyrene-1-carboxylate by phosphate and organic acids in aqueous solution studied by fluorescence spectroscopy
    • Zelent B., Vanderkooi J.M., Coleman R.G., Gryczynski I., and Gryczynski Z. Protonation of excited state pyrene-1-carboxylate by phosphate and organic acids in aqueous solution studied by fluorescence spectroscopy. Biophys. J. 91 (2006) 3864
    • (2006) Biophys. J. , vol.91 , pp. 3864
    • Zelent, B.1    Vanderkooi, J.M.2    Coleman, R.G.3    Gryczynski, I.4    Gryczynski, Z.5
  • 80
    • 33749599714 scopus 로고    scopus 로고
    • Femtosecond studies of tryptophan fluorescence dynamics in proteins: Local solvation and electronic quenching
    • Zhang L., Kao Y., Qiu W., Wang L., and Zhong D. Femtosecond studies of tryptophan fluorescence dynamics in proteins: Local solvation and electronic quenching. J. Phys. Chem. Lett. B 110 (2006) 18097
    • (2006) J. Phys. Chem. Lett. B , vol.110 , pp. 18097
    • Zhang, L.1    Kao, Y.2    Qiu, W.3    Wang, L.4    Zhong, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.