메뉴 건너뛰기




Volumn 17, Issue 1, 2002, Pages 19-42

The red-edge effects: 30 years of exploration

Author keywords

Dielectric relaxation; Fluorescence; Molecular disorder; Red edge effects; Site selection spectroscopy

Indexed keywords

AMINO ACIDS; ENERGY TRANSFER; EXCITED STATES; MOLECULAR BIOLOGY; PROTON TRANSFER; SITE SELECTION; TIME DOMAIN ANALYSIS;

EID: 0036363969     PISSN: 15227235     EISSN: None     Source Type: Journal    
DOI: 10.1002/bio.671     Document Type: Review
Times cited : (412)

References (232)
  • 1
    • 0001498520 scopus 로고
    • Role of heterogeneity of the solvation site in electronic spectra in solution
    • Galley WC and Purkey RM. Role of heterogeneity of the solvation site in electronic spectra in solution. Proc. Natl Acad. Sci. USA 1970; 67: 1116-1121.
    • (1970) Proc. Natl Acad. Sci. USA , vol.67 , pp. 1116-1121
    • Galley, W.C.1    Purkey, R.M.2
  • 2
    • 0013321397 scopus 로고
    • Bathochromic luminescence of organic dyes at low temperatures
    • Rubinov AN and Tomin VI. Bathochromic luminescence of organic dyes at low temperatures. Opt. Spektr. 1970; 29: 1082-1086.
    • (1970) Opt. Spektr. , vol.29 , pp. 1082-1086
    • Rubinov, A.N.1    Tomin, V.I.2
  • 3
    • 0000893996 scopus 로고
    • Failure of energy transfer between identical aromatic molecules on excitation at the long wave edge of the absorption spectrum
    • Weber G and Shinitzky M. Failure of energy transfer between identical aromatic molecules on excitation at the long wave edge of the absorption spectrum. Proc. Natl Acad. Sci. USA 1970; 65: 823-830.
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 823-830
    • Weber, G.1    Shinitzky, M.2
  • 4
    • 0000944228 scopus 로고
    • Fluorescence-polarization spectrum and electronic energy transfer in tyrosine, tryptophan and related compounds
    • Weber G. Fluorescence-polarization spectrum and electronic energy transfer in tyrosine, tryptophan and related compounds. Biochem. J. 1960; 75: 335-345.
    • (1960) Biochem. J. , vol.75 , pp. 335-345
    • Weber, G.1
  • 5
    • 0039430448 scopus 로고
    • On the influence of exciting light on fluorescence specra of phthalimide solutions
    • Rudik KI and Pikulik LG. On the influence of exciting light on fluorescence specra of phthalimide solutions. Opt. Spektr. 1971; 30: 275-278.
    • (1971) Opt. Spektr. , vol.30 , pp. 275-278
    • Rudik, K.I.1    Pikulik, L.G.2
  • 6
    • 0038804793 scopus 로고
    • Dependence of excitation spectra of solutions of dipolar molecules on registration wavelength
    • Pavlovich VS. Dependence of excitation spectra of solutions of dipolar molecules on registration wavelength. Zh. Prikl. Spektr. 1976; 25: 480-487.
    • (1976) Zh. Prikl. Spektr. , vol.25 , pp. 480-487
    • Pavlovich, V.S.1
  • 7
    • 0000703459 scopus 로고
    • Shift of emission band upon the excitation at the long wavelength absorption edge. 3. Temperature dependence of the shift and correlation with the time-dependent spectral shift
    • Azumi T, Itoh K and Shiraishi H. Shift of emission band upon the excitation at the long wavelength absorption edge. 3. Temperature dependence of the shift and correlation with the time-dependent spectral shift. J. Chem. Phys. 1976; 65: 2550-2555.
    • (1976) J. Chem. Phys. , vol.65 , pp. 2550-2555
    • Azumi, T.1    Itoh, K.2    Shiraishi, H.3
  • 8
    • 0040022721 scopus 로고
    • Peculiarities of inductive-resonance energy transfer in the conditions of organic molecule electronic levels inhomogeneous broadening
    • Gulis IM and Komyak AI. Peculiarities of inductive-resonance energy transfer in the conditions of organic molecule electronic levels inhomogeneous broadening. Zh. Prikl. Spektr. 1977; 27: 841-845.
    • (1977) Zh. Prikl. Spektr. , vol.27 , pp. 841-845
    • Gulis, I.M.1    Komyak, A.I.2
  • 9
    • 84909712317 scopus 로고
    • Intermolecular up-relaxation in phthalimide solutions at excitation by frequency tuned dye laser
    • Nemkovich NA, Matseyko VI and Tomin VI. Intermolecular up-relaxation in phthalimide solutions at excitation by frequency tuned dye laser. Opt. Spektr. 1980; 49: 274-283.
    • (1980) Opt. Spektr. , vol.49 , pp. 274-283
    • Nemkovich, N.A.1    Matseyko, V.I.2    Tomin, V.I.3
  • 12
    • 0012035638 scopus 로고
    • Theory of the absorption band shape and a fluorescence band shape of an impurity center in the Condon approximation
    • Osad'ko IS. Theory of the absorption band shape and a fluorescence band shape of an impurity center in the Condon approximation. Sov. Phys. JETP 1977; 45: 827-833.
    • (1977) Sov. Phys. JETP , vol.45 , pp. 827-833
    • Osad'ko, I.S.1
  • 13
    • 0038127826 scopus 로고
    • The studies of electronic-vibrational interactions in structurized optical centers of impurity centers
    • Osad'ko IS. The studies of electronic-vibrational interactions in structurized optical centers of impurity centers. Usp. Phys. Nauk. USSR 1979; 128: 31-68.
    • (1979) Usp. Phys. Nauk. USSR , vol.128 , pp. 31-68
    • Osad'ko, I.S.1
  • 14
    • 84985437487 scopus 로고
    • Fluorophores in polar media: Structural effects of the Langevin distribution of electrostatic interactions
    • Macgregor RB and Weber G. Fluorophores in polar media: Structural effects of the Langevin distribution of electrostatic interactions. Ann. N. Y. Acad. Sci. 1981; 366: 140-154.
    • (1981) Ann. N. Y. Acad. Sci. , vol.366 , pp. 140-154
    • Macgregor, R.B.1    Weber, G.2
  • 15
    • 0040615718 scopus 로고
    • Statistics of solvation and solvatochromy
    • Mazurenko YuT. Statistics of solvation and solvatochromy. Opt. Spektr. 1983; 55: 471-478.
    • (1983) Opt. Spektr. , vol.55 , pp. 471-478
    • Mazurenko, Y.T.1
  • 16
    • 0038837748 scopus 로고
    • Calculation of distribution function on the frequency of 0-0 transition in polar solutions
    • Gorbatsevich SK, Gulis IM and Komyak AI. Calculation of distribution function on the frequency of 0-0 transition in polar solutions. Zh. Prikl. Spektr. 1982; 36: 460-466.
    • (1982) Zh. Prikl. Spektr. , vol.36 , pp. 460-466
    • Gorbatsevich, S.K.1    Gulis, I.M.2    Komyak, A.I.3
  • 17
    • 85034931515 scopus 로고
    • Spectroscopy of the solvent cage. Generation and properties of the excited states
    • DeLucca M. McElroy WD (eds) Academic Press: New York
    • Kasha M, Dellinger B and Brown CW. Spectroscopy of the solvent cage. Generation and properties of the excited states. In: International Conference on Bioluminescence and Chemiluminescence. DeLucca M. McElroy WD (eds) Academic Press: New York 1981; 3-16.
    • (1981) International Conference on Bioluminescence and Chemiluminescence , pp. 3-16
    • Kasha, M.1    Dellinger, B.2    Brown, C.W.3
  • 18
    • 0019568556 scopus 로고
    • Dependence of human serum albumin fluorescence spectrum on excitation wavelength
    • Demchenko AP. Dependence of human serum albumin fluorescence spectrum on excitation wavelength. Ukr. Biochim. Zh. 1981; 53(3): 22-27.
    • (1981) Ukr. Biochim. Zh. , vol.53 , Issue.3 , pp. 22-27
    • Demchenko, A.P.1
  • 19
    • 0020131082 scopus 로고
    • On the nanosecond mobility in proteins. Edge excitation fluorescence red shift of protein-bound 2-(p-toluidinylnaphthalene)-6-sulfonate
    • Demchenko AP. On the nanosecond mobility in proteins. Edge excitation fluorescence red shift of protein-bound 2-(p-toluidinylnaphthalene)-6-sulfonate. Biophys. Chem. 1982; 15: 101-109.
    • (1982) Biophys. Chem. , vol.15 , pp. 101-109
    • Demchenko, A.P.1
  • 20
    • 0024259064 scopus 로고
    • Red-edge-excitation fluorescence spectroscopy of single-tryptophan proteins
    • Demchenko AP. Red-edge-excitation fluorescence spectroscopy of single-tryptophan proteins. Eur. Biophvs. J. 1988; 16: 121-129.
    • (1988) Eur. Biophvs. J. , vol.16 , pp. 121-129
    • Demchenko, A.P.1
  • 21
    • 0039430447 scopus 로고
    • Non-exponential kinetics of polarization in liquid polar solutions of phthalimide derivatives
    • Gakamsky DM, Nemkovich NA, Rubinov AI and Tomin VI. Non-exponential kinetics of polarization in liquid polar solutions of phthalimide derivatives. Opt. Spektr. 1983; 54: 567-568.
    • (1983) Opt. Spektr. , vol.54 , pp. 567-568
    • Gakamsky, D.M.1    Nemkovich, N.A.2    Rubinov, A.I.3    Tomin, V.I.4
  • 22
    • 0019608120 scopus 로고
    • Kinetics of luminescence spectra of rigid dye solutions due to directed electronic energy transfer
    • Nemkovich NA, Rubinov AN and Tomin VI. Kinetics of luminescence spectra of rigid dye solutions due to directed electronic energy transfer. J. Lumin. 1981; 23: 349-361.
    • (1981) J. Lumin. , vol.23 , pp. 349-361
    • Nemkovich, N.A.1    Rubinov, A.N.2    Tomin, V.I.3
  • 23
    • 0025944109 scopus 로고
    • Solvent-reorganizational red-edge effect in intramolecular electron transfer
    • Demchenko AP and Sytnik AS. Solvent-reorganizational red-edge effect in intramolecular electron transfer. Proc. Natl Acad. Sci. USA 1991; 88: 9311-9314.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9311-9314
    • Demchenko, A.P.1    Sytnik, A.S.2
  • 24
    • 0007876562 scopus 로고
    • Site-selectivity in excited-state reactions in solutions
    • Demchenko AP and Sytnik AS. Site-selectivity in excited-state reactions in solutions. J. Phys. Chem. 1991; 95: 10518-10524.
    • (1991) J. Phys. Chem. , vol.95 , pp. 10518-10524
    • Demchenko, A.P.1    Sytnik, A.S.2
  • 25
    • 0028670491 scopus 로고
    • Protein fluorescence, dynamics and function: Exploration of analogy between electronically excited and biocatalytic transition states
    • Demchenko AP. Protein fluorescence, dynamics and function: exploration of analogy between electronically excited and biocatalytic transition states. Biochim. Biophys. Acta 1994; 1209: 149-164.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 149-164
    • Demchenko, A.P.1
  • 26
    • 0001551138 scopus 로고
    • Hole-burning in a contour of a pure electronic line in a Spolskii system
    • Gorokhovskii AA, Kaarli RK and Rebane RA. Hole-burning in a contour of a pure electronic line in a Spolskii system. Sov. Phys. JETP Lett. 1974; 20: 216-218.
    • (1974) Sov. Phys. JETP Lett. , vol.20 , pp. 216-218
    • Gorokhovskii, A.A.1    Kaarli, R.K.2    Rebane, R.A.3
  • 27
    • 0016116113 scopus 로고
    • Stable 'gap' in absorption spectra in solid solutions of organic molecules by laser irradiation
    • Kharlamov BM. Personov RI and Bykovskaja LA. Stable 'gap' in absorption spectra in solid solutions of organic molecules by laser irradiation. Opt. Commun. 1974; 12: 191-193.
    • (1974) Opt. Commun. , vol.12 , pp. 191-193
    • Kharlamov, B.M.1    Personov, R.I.2    Bykovskaja, L.A.3
  • 28
    • 0015418624 scopus 로고
    • The effect of fine structure appearance in laser-excited fluorescence spectra of organic compounds in solid solutions
    • Personov RI, Al'shits LA and Bykovskaja LA. The effect of fine structure appearance in laser-excited fluorescence spectra of organic compounds in solid solutions. Opt. Commun. 1972; 6: 169-173.
    • (1972) Opt. Commun. , vol.6 , pp. 169-173
    • Personov, R.I.1    Al'shits, L.A.2    Bykovskaja, L.A.3
  • 29
    • 0001226819 scopus 로고
    • Laser induced fluorescence line narrowing in ruby
    • Szabo A. Laser induced fluorescence line narrowing in ruby. Phys. Rev. Lett. 1970; 25: 924-926.
    • (1970) Phys. Rev. Lett. , vol.25 , pp. 924-926
    • Szabo, A.1
  • 30
    • 4243860207 scopus 로고
    • Site-selection spectroscopy of polyatomic molecules: Principles, applications and possibilities
    • Personov RI. Site-selection spectroscopy of polyatomic molecules: principles, applications and possibilities. Spectrochim. Acta B 1983; 38: 1533-1544.
    • (1983) Spectrochim. Acta B , vol.38 , pp. 1533-1544
    • Personov, R.I.1
  • 31
    • 3743067950 scopus 로고
    • Photochemical hole burning: A spectroscopic study of relaxation processes in polymers and glasses
    • Friedrich J and Haarer D. Photochemical hole burning: a spectroscopic study of relaxation processes in polymers and glasses. Angew. Chem. Int. Eng. Ed. 1984; 23: 118-140.
    • (1984) Angew. Chem. Int. Eng. Ed. , vol.23 , pp. 118-140
    • Friedrich, J.1    Haarer, D.2
  • 33
    • 0001407774 scopus 로고
    • Theory of transient hole-burning spectrum for molecules in solution
    • Kinosita S. Theory of transient hole-burning spectrum for molecules in solution. J. Chem. Phys. 1989; 91: 5175-5181.
    • (1989) J. Chem. Phys. , vol.91 , pp. 5175-5181
    • Kinosita, S.1
  • 34
    • 4244084400 scopus 로고
    • Optical detection and spectroscopy of single molecules in solid
    • Moerner WE and Kador L. Optical detection and spectroscopy of single molecules in solid. Phys. Rev. Lett. 1989; 62: 2535-2538.
    • (1989) Phys. Rev. Lett. , vol.62 , pp. 2535-2538
    • Moerner, W.E.1    Kador, L.2
  • 35
    • 0025920682 scopus 로고
    • Fluorescence spectroscopy and spectral diffusion of single molecule in a crystal
    • Ambrose WP and Moerner WE. Fluorescence spectroscopy and spectral diffusion of single molecule in a crystal. Nature 1991; 349: 225-227.
    • (1991) Nature , vol.349 , pp. 225-227
    • Ambrose, W.P.1    Moerner, W.E.2
  • 36
    • 85153315504 scopus 로고    scopus 로고
    • Imaging individual green fluorescent protein
    • Pierce DW and Holm-Booker RD. Imaging individual green fluorescent protein. Nature 1997; 328: 338.
    • (1997) Nature , vol.328 , pp. 338
    • Pierce, D.W.1    Holm-Booker, R.D.2
  • 38
    • 0030928573 scopus 로고    scopus 로고
    • Conformational fluctuations in single DNA molecules
    • Wennmalm S, Edman L and Rigler R. Conformational fluctuations in single DNA molecules. Proc. Natl Acad. Sci. USA 1997; 94: 10641-10646.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10641-10646
    • Wennmalm, S.1    Edman, L.2    Rigler, R.3
  • 39
    • 0037639180 scopus 로고
    • Spectroscopy of inhomogeneous configurational broadening in dye solutions
    • Tomin VI and Rubinov AN. Spectroscopy of inhomogeneous configurational broadening in dye solutions. Zh. Prikl. Spektr. 1981; 35: 237-251.
    • (1981) Zh. Prikl. Spektr. , vol.35 , pp. 237-251
    • Tomin, V.I.1    Rubinov, A.N.2
  • 40
    • 0022824205 scopus 로고
    • Fluorescence analysis of protein dynamics
    • Demchenko AP. Fluorescence analysis of protein dynamics. Essays Biochem. 1986; 22: 120-157.
    • (1986) Essays Biochem. , vol.22 , pp. 120-157
    • Demchenko, A.P.1
  • 41
    • 0023688789 scopus 로고
    • Site-selective excitation: A new dimension in protein and membrane spectroscopy
    • Demchenko AP. Site-selective excitation: a new dimension in protein and membrane spectroscopy. Trends Biochem. Sci. 1989; 10: 374-377.
    • (1989) Trends Biochem. Sci. , vol.10 , pp. 374-377
    • Demchenko, A.P.1
  • 42
    • 0000449341 scopus 로고
    • Inhomogeneous broadening of electronic spectra of dye molecules in solutions
    • Lakowicz JR (ed.). Plenum: New York
    • Nemkovich NA, Rubinov AN and Tomin VI. Inhomogeneous broadening of electronic spectra of dye molecules in solutions. In Topics in Fluorescence Spectroscopy, vol. 2, Lakowicz JR (ed.). Plenum: New York 1991; 367-128.
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 367-1128
    • Nemkovich, N.A.1    Rubinov, A.N.2    Tomin, V.I.3
  • 43
    • 0002482325 scopus 로고
    • Fluorescence and dynamics in proteins
    • Lakowicz JR (ed.). Plenum: New York
    • Demchenko AP. Fluorescence and dynamics in proteins. In Topics in Fluorescence Spectroscopy, vol. 3, Lakowicz JR (ed.). Plenum: New York 1991; 61-111.
    • (1991) Topics in Fluorescence Spectroscopy , vol.3 , pp. 61-111
    • Demchenko, A.P.1
  • 44
    • 0001527174 scopus 로고
    • Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems
    • Mukherjee S and Chattopadhyay A. Wavelength-selective fluorescence as a novel tool to study organization and dynamics in complex biological systems. J. Fluoresc. 1995; 5: 237-246.
    • (1995) J. Fluoresc. , vol.5 , pp. 237-246
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 48
    • 0039430445 scopus 로고
    • Inhomogeneous broadening of the spectra of dye solutions due to intermolecular hydrogen bond
    • Bushuk BA, Rubinov AN and Stupak AP. Inhomogeneous broadening of the spectra of dye solutions due to intermolecular hydrogen bond. Zh Prikl. Spektr. 1987; 47: 934-938.
    • (1987) Zh Prikl. Spektr. , vol.47 , pp. 934-938
    • Bushuk, B.A.1    Rubinov, A.N.2    Stupak, A.P.3
  • 49
    • 33751155037 scopus 로고
    • Structural changes and internal fields in proteins: A hole burning Stark effect study of horseradish peroxidase
    • Gafert J, Friedrich J, Vanderkooi JM and Fidy J. Structural changes and internal fields in proteins: a hole burning Stark effect study of horseradish peroxidase. J. Phys. Chem. 1995; 99: 5223-5227.
    • (1995) J. Phys. Chem. , vol.99 , pp. 5223-5227
    • Gafert, J.1    Friedrich, J.2    Vanderkooi, J.M.3    Fidy, J.4
  • 50
    • 0027411844 scopus 로고
    • Native and denatured Zn cytochrome c studied by fluorescence line narrowing spectroscopy
    • Logovinsky V, Kaposi AD and Vanderkooi JM. Native and denatured Zn cytochrome c studied by fluorescence line narrowing spectroscopy. Biochim. Biophys. Acta 1993; 1161: 149-160.
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 149-160
    • Logovinsky, V.1    Kaposi, A.D.2    Vanderkooi, J.M.3
  • 51
    • 0000777551 scopus 로고
    • Investigations of spectral broadening mechanisms in biomolecules: Cytochrome c
    • Schomaker KT and Champion PM. Investigations of spectral broadening mechanisms in biomolecules: cytochrome c. J. Chem. Phys. 1986; 84: 5314-5325.
    • (1986) J. Chem. Phys. , vol.84 , pp. 5314-5325
    • Schomaker, K.T.1    Champion, P.M.2
  • 52
    • 0038466894 scopus 로고
    • Some effects in inhomogeneous level broadening at excitation energy transfer conditions
    • Voropay ES, Koyava VT, Saechnikov VA and Sarjevsky AM. Some effects in inhomogeneous level broadening at excitation energy transfer conditions. Zh. Prikl. Spektr. 1980; 32: 457-463.
    • (1980) Zh. Prikl. Spektr. , vol.32 , pp. 457-463
    • Voropay, E.S.1    Koyava, V.T.2    Saechnikov, V.A.3    Sarjevsky, A.M.4
  • 53
    • 0000436771 scopus 로고
    • The influence of orientational dipolar relaxation on spectral, temporal and polarization properties of luminescence in solutions
    • Mazurenko YuT and Bakhshiev NG. The influence of orientational dipolar relaxation on spectral, temporal and polarization properties of luminescence in solutions. Opt. Spektr. 1970; 28: 905-913.
    • (1970) Opt. Spektr. , vol.28 , pp. 905-913
    • Mazurenko, Yu.T.1    Bakhshiev, N.G.2
  • 54
    • 33845280671 scopus 로고
    • Time-resolved studies of solvation in polar media
    • Simon JD. Time-resolved studies of solvation in polar media. Ace. Chem. Res. 1988; 21: 128-134.
    • (1988) Ace. Chem. Res. , vol.21 , pp. 128-134
    • Simon, J.D.1
  • 55
    • 0001292293 scopus 로고
    • Dynamics of fluorescence of a dye molecule in solution
    • Kinoshita S and Nishi N. Dynamics of fluorescence of a dye molecule in solution. J. Chem. Phys. 1988; 89: 6612-6622.
    • (1988) J. Chem. Phys. , vol.89 , pp. 6612-6622
    • Kinoshita, S.1    Nishi, N.2
  • 56
    • 33646102263 scopus 로고    scopus 로고
    • Dipole solvation in non-dipolar solvents: Experimental studies of reorganization energies and solvation dynamics
    • Reynolds L, Gardecki JA, Frankland SJV, Horng ML and Maroncelli M. Dipole solvation in non-dipolar solvents: experimental studies of reorganization energies and solvation dynamics. J. Phys. Chem. 1996; 100: 10337-10354.
    • (1996) J. Phys. Chem. , vol.100 , pp. 10337-10354
    • Reynolds, L.1    Gardecki, J.A.2    Frankland, S.J.V.3    Horng, M.L.4    Maroncelli, M.5
  • 57
    • 0040022720 scopus 로고    scopus 로고
    • Ultrafast solvation processes in polar liquids probed with large organic molecules
    • Bardeen CJ, Rosenthal SJ and Shank CV. Ultrafast solvation processes in polar liquids probed with large organic molecules. J. Phys. Chem. A 193: 10506-10516.
    • J. Phys. Chem. A , vol.193 , pp. 10506-10516
    • Bardeen, C.J.1    Rosenthal, S.J.2    Shank, C.V.3
  • 58
    • 0026623214 scopus 로고
    • Fluorescence decay time distribution for polar dye solutions with time-dependent fluorescent shift
    • Gakamsky DM, Goldin AA, Petrov EP and Rubinov AN. Fluorescence decay time distribution for polar dye solutions with time-dependent fluorescent shift. Biophys. Chem. 1992; 44: 47-60.
    • (1992) Biophys. Chem. , vol.44 , pp. 47-60
    • Gakamsky, D.M.1    Goldin, A.A.2    Petrov, E.P.3    Rubinov, A.N.4
  • 59
    • 0012866115 scopus 로고    scopus 로고
    • Energy relaxation dynamics in the optical excited state of myoglobin
    • Murakami H and Kushida T. Energy relaxation dynamics in the optical excited state of myoglobin. Phys. Rev. B 1996; 54: 978-985.
    • (1996) Phys. Rev. B , vol.54 , pp. 978-985
    • Murakami, H.1    Kushida, T.2
  • 60
    • 0012778108 scopus 로고    scopus 로고
    • Fast structural relaxation of polyvinyl alcohol below the glass transition temperature
    • Murakami H, Kushida T and Tashiro H. Fast structural relaxation of polyvinyl alcohol below the glass transition temperature. J. Chem. Phys. 1998; 108: 10309-10318.
    • (1998) J. Chem. Phys. , vol.108 , pp. 10309-10318
    • Murakami, H.1    Kushida, T.2    Tashiro, H.3
  • 61
    • 0001488471 scopus 로고    scopus 로고
    • Red edge photophysics of ethanolic rhodamine 101 and the observation of laser cooling in the condensed phase
    • Clark JL, Miller PF and Rumbles G. Red edge photophysics of ethanolic rhodamine 101 and the observation of laser cooling in the condensed phase. J. Phys. Chem. A 1998; 102: 4428-4437.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 4428-4437
    • Clark, J.L.1    Miller, P.F.2    Rumbles, G.3
  • 62
    • 0023679312 scopus 로고
    • Red-edge-excitation fluorescence spectroscopy of indole and tryptophan
    • Demchenko AP and Ladokhin AS. Red-edge-excitation fluorescence spectroscopy of indole and tryptophan. Eur. Biophys J. 1988; 15: 369-379.
    • (1988) Eur. Biophys J. , vol.15 , pp. 369-379
    • Demchenko, A.P.1    Ladokhin, A.S.2
  • 63
    • 0015217633 scopus 로고
    • Nanosecond time-resolved fluorescence spectra of a protein-dye complex BSA + TNS
    • Brand L and Gohlike JR. Nanosecond time-resolved fluorescence spectra of a protein-dye complex BSA + TNS. J. Biol. Chem. 1971; 246: 2317-2324.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2317-2324
    • Brand, L.1    Gohlike, J.R.2
  • 65
    • 33751156520 scopus 로고
    • Solvent relaxation around the excited state of indole: Analysis of fluorescence lifetime distributions and time-dependent spectral shifts
    • Vincent M and Gallay J. Demchenko AP. Solvent relaxation around the excited state of indole: analysis of fluorescence lifetime distributions and time-dependent spectral shifts. J. Phys. Chem. 1995; 99: 34931-34941.
    • (1995) J. Phys. Chem. , vol.99 , pp. 34931-34941
    • Vincent, M.1    Gallay, J.2    Demchenko, A.P.3
  • 66
    • 85153194466 scopus 로고    scopus 로고
    • Photophysics of indole in polar solvent: Analysis of fluorescence lifetime distributions and time-dependent spectral shifts
    • Woodburry: New York
    • Vincent M and Gallay J. Demchenko AP. Photophysics of indole in polar solvent: analysis of fluorescence lifetime distributions and time-dependent spectral shifts. In: Fast Elementary Processes in Chemical and Biological Systems. Woodburry: New York, 1996: 496-506.
    • (1996) Fast Elementary Processes in Chemical and Biological Systems , pp. 496-506
    • Vincent, M.1    Gallay, J.2    Demchenko, A.P.3
  • 67
    • 33751294164 scopus 로고    scopus 로고
    • Red-edge excitation fluorescence study of the inhomogeneous broadening of electronic transitions in solutions
    • Morgenthaler MJE, Yoshihara K and Meech SR. Red-edge excitation fluorescence study of the inhomogeneous broadening of electronic transitions in solutions. J. Chem. Soc. Faraday Trans. 1996; 92: 629-635.
    • (1996) J. Chem. Soc. Faraday Trans. , vol.92 , pp. 629-635
    • Morgenthaler, M.J.E.1    Yoshihara, K.2    Meech, S.R.3
  • 68
    • 0040022718 scopus 로고
    • The influence of relaxation processes on temporal and polarization characteristics of fluorescence of rhodamine 6G in glycerol
    • Levshin LB, Struganova IA and Toleutaev BN. The influence of relaxation processes on temporal and polarization characteristics of fluorescence of rhodamine 6G in glycerol. Zh. Prikl. Spektr. 1986; 44: 769-776.
    • (1986) Zh. Prikl. Spektr. , vol.44 , pp. 769-776
    • Levshin, L.B.1    Struganova, I.A.2    Toleutaev, B.N.3
  • 69
    • 0000366551 scopus 로고
    • Spectral diffusion in liquids
    • Stein AD and Fayer MD. Spectral diffusion in liquids. J. Chem. Phys. 1992; 97: 2948-2962.
    • (1992) J. Chem. Phys. , vol.97 , pp. 2948-2962
    • Stein, A.D.1    Fayer, M.D.2
  • 70
    • 33748919686 scopus 로고
    • Kinetic spectroscopy of orientational states of solvated dye molecules in polar solution
    • Rubinov AN, Tomin VI and Bushuk BA. Kinetic spectroscopy of orientational states of solvated dye molecules in polar solution. J. Lumin. 1982; 26: 377-391.
    • (1982) J. Lumin. , vol.26 , pp. 377-391
    • Rubinov, A.N.1    Tomin, V.I.2    Bushuk, B.A.3
  • 71
    • 0039430444 scopus 로고
    • Spectral dependence of the degree of rotational depolarization of the fluorescence of complex molecules in viscous solutions
    • Mazurenko YuT, Bakhshiev NG and Piterskaya IV. Spectral dependence of the degree of rotational depolarization of the fluorescence of complex molecules in viscous solutions. Opt. Spektr. 1968; 25: 92-97.
    • (1968) Opt. Spektr. , vol.25 , pp. 92-97
    • Mazurenko, Y.T.1    Bakhshiev, N.G.2    Piterskaya, I.V.3
  • 72
    • 0040615715 scopus 로고
    • Wavelength-dependent rotation of dye molecules in a polar solution
    • Gakamsky DM, Nemkovich NA and Rubinov AN. Wavelength-dependent rotation of dye molecules in a polar solution. J. Fluorescence 1992; 2: 81-92.
    • (1992) J. Fluorescence , vol.2 , pp. 81-92
    • Gakamsky, D.M.1    Nemkovich, N.A.2    Rubinov, A.N.3
  • 74
    • 0000353745 scopus 로고
    • Directed energy transport due to orientational broadening of energy levels in photosynthetic pigment solutions
    • Rubinov AN, Zenkevich EI, Nemkovich NA and Tomin VI. Directed energy transport due to orientational broadening of energy levels in photosynthetic pigment solutions. J. Lumin. 1982; 26: 367-376.
    • (1982) J. Lumin. , vol.26 , pp. 367-376
    • Rubinov, A.N.1    Zenkevich, E.I.2    Nemkovich, N.A.3    Tomin, V.I.4
  • 75
    • 0040615714 scopus 로고
    • Directed excitation energy transfer in solid polar solutions of dyes
    • Koyava VT and Popechitz VI. Directed excitation energy transfer in solid polar solutions of dyes. Zh. Prikl. Spektr. 1979; 31: 982-986.
    • (1979) Zh. Prikl. Spektr. , vol.31 , pp. 982-986
    • Koyava, V.T.1    Popechitz, V.I.2
  • 76
    • 0039430443 scopus 로고
    • Concentrational depolarization of fluorescence in systems with inhomogeneously broadened electronic levels
    • Koyava VT, Popechitz VI and Sarjevsky AM. Concentrational depolarization of fluorescence in systems with inhomogeneously broadened electronic levels. Zh. Prikl. Spektr. 1980; 32: 1023-1029.
    • (1980) Zh. Prikl. Spektr. , vol.32 , pp. 1023-1029
    • Koyava, V.T.1    Popechitz, V.I.2    Sarjevsky, A.M.3
  • 77
    • 0038127813 scopus 로고
    • The influence of directed energy transfer on kinetics of emission spectra of solid solutions of complex molecules
    • Nemkovich NA, Gulis IM and Tomin VI. The influence of directed energy transfer on kinetics of emission spectra of solid solutions of complex molecules. Zh. Prikl. Spektr. 1981; 33: 1080-1084.
    • (1981) Zh. Prikl. Spektr. , vol.33 , pp. 1080-1084
    • Nemkovich, N.A.1    Gulis, I.M.2    Tomin, V.I.3
  • 78
    • 36749118729 scopus 로고
    • The kinetics of solvent reorientation in hydroxylated solvents from the exciting-wavelength dependence of chromophore emission spectra
    • Milton JC, Purkey RM and Galley WC. The kinetics of solvent reorientation in hydroxylated solvents from the exciting-wavelength dependence of chromophore emission spectra. J. Chem. Phys. 1978; 68: 5396-5404.
    • (1978) J. Chem. Phys. , vol.68 , pp. 5396-5404
    • Milton, J.C.1    Purkey, R.M.2    Galley, W.C.3
  • 79
    • 0007329044 scopus 로고
    • Instantanous phosphorescence spectra of glassy polar solutions of acetyl phthalamide derivatives
    • Pavlovich VS, Pershukevich PP and Pikulik LG. Instantanous phosphorescence spectra of glassy polar solutions of acetyl phthalamide derivatives. Zh. Prikl. Spektr. 1983; 39: 779-785.
    • (1983) Zh. Prikl. Spektr. , vol.39 , pp. 779-785
    • Pavlovich, V.S.1    Pershukevich, P.P.2    Pikulik, L.G.3
  • 81
    • 0033660958 scopus 로고    scopus 로고
    • Time-domain observation of conformational fluctuation of protein by time-resolved hole-burning spectroscopy
    • Shibata Y. Time-domain observation of conformational fluctuation of protein by time-resolved hole-burning spectroscopy. Sci. Prog. 2000; 83(Pt 2): 193-208.
    • (2000) Sci. Prog. , vol.83 , Issue.2 PART , pp. 193-208
    • Shibata, Y.1
  • 82
    • 0033044711 scopus 로고    scopus 로고
    • Conformational fluctuation of native-like and molten-globule-like cytochrome c observed by time-resolved hole burning
    • Shibata Y, Takahashi H, Kaneko R, Kurita A and Kushida T. Conformational fluctuation of native-like and molten-globule-like cytochrome c observed by time-resolved hole burning. Biochemistry 1999; 38: 1802-1810.
    • (1999) Biochemistry , vol.38 , pp. 1802-1810
    • Shibata, Y.1    Takahashi, H.2    Kaneko, R.3    Kurita, A.4    Kushida, T.5
  • 83
    • 0032972964 scopus 로고    scopus 로고
    • Solvent effects on conformational dynamics of Zn-substituted myoglobin observed by time-resolved hole-burning spectroscopy
    • Shibata Y, Kurita A and Kushida T. Solvent effects on conformational dynamics of Zn-substituted myoglobin observed by time-resolved hole-burning spectroscopy. Biochemistry 1999; 38: 1789-1801.
    • (1999) Biochemistry , vol.38 , pp. 1789-1801
    • Shibata, Y.1    Kurita, A.2    Kushida, T.3
  • 84
    • 0031836879 scopus 로고    scopus 로고
    • Real-time observation of conformational fluctuations in Zn-substituted myoglobin by time-resolved transient hole-burning spectroscopy
    • Shibata Y, Kurita A and Kushida T. Real-time observation of conformational fluctuations in Zn-substituted myoglobin by time-resolved transient hole-burning spectroscopy. Biophys. J. 1998; 75: 521-527.
    • (1998) Biophys. J. , vol.75 , pp. 521-527
    • Shibata, Y.1    Kurita, A.2    Kushida, T.3
  • 85
    • 0030680984 scopus 로고    scopus 로고
    • Solvent accessibility of the phycocyanobilin chromophore in the alpha subunit of C-phycocyanin: Implications for a molecular mechanism for internal protein-matrix solvation dynamics
    • Homoelle BJ and Beck WF. Solvent accessibility of the phycocyanobilin chromophore in the alpha subunit of C-phycocyanin: implications for a molecular mechanism for internal protein-matrix solvation dynamics. Biochemistry 1997; 36: 12970-12975.
    • (1997) Biochemistry , vol.36 , pp. 12970-12975
    • Homoelle, B.J.1    Beck, W.F.2
  • 86
    • 0030671072 scopus 로고    scopus 로고
    • Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: Direct evidence for the functional significance of a hierarchy of dynamical processes
    • Huang J, Ridsdale A, Wang J and Friedman JM. Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: direct evidence for the functional significance of a hierarchy of dynamical processes. Biochemistry 1997; 36: 14353-14365.
    • (1997) Biochemistry , vol.36 , pp. 14353-14365
    • Huang, J.1    Ridsdale, A.2    Wang, J.3    Friedman, J.M.4
  • 87
    • 33750109348 scopus 로고
    • Polar solvent dynamics and electron-transfer reactions
    • Maroncelli M, McInnis J and Fleming GR. Polar solvent dynamics and electron-transfer reactions. Science 1989; 243: 1674-1681.
    • (1989) Science , vol.243 , pp. 1674-1681
    • Maroncelli, M.1    McInnis, J.2    Fleming, G.R.3
  • 88
    • 4243271260 scopus 로고
    • Free volume sensing fluorescent probes
    • Al-Hassan KA and Rettig W. Free volume sensing fluorescent probes. Chem. Phys. Lett. 1986; 126: 273-279.
    • (1986) Chem. Phys. Lett. , vol.126 , pp. 273-279
    • Al-Hassan, K.A.1    Rettig, W.2
  • 89
    • 0031552260 scopus 로고    scopus 로고
    • Excitation energy dependence of the kinetics of charge-transfer formation
    • Braun D and Rettig W. Excitation energy dependence of the kinetics of charge-transfer formation Chem. Phys. Lett. 1997; 268: 110-116.
    • (1997) Chem. Phys. Lett. , vol.268 , pp. 110-116
    • Braun, D.1    Rettig, W.2
  • 90
    • 0024735941 scopus 로고
    • Low-temperature dual fluorescence in 9-morpholinoacridine
    • Herbich J, Dobkowski J, Rulliere C and Nowacki J. Low-temperature dual fluorescence in 9-morpholinoacridine. J. Lumin. 1989; 44: 87-95.
    • (1989) J. Lumin. , vol.44 , pp. 87-95
    • Herbich, J.1    Dobkowski, J.2    Rulliere, C.3    Nowacki, J.4
  • 91
    • 0000023905 scopus 로고
    • Excitedstate s-cis rotamers produced by extreme red edge excitation of all-trans-1,4-diphenyl-1,3-butadiene
    • Wallace-Williams SE, Moller S and Goldbeck RA et al. Excitedstate s-cis rotamers produced by extreme red edge excitation of all-trans-1,4-diphenyl-1,3-butadiene. J. Phys. Chem. 1993; 97: 9587-9592.
    • (1993) J. Phys. Chem. , vol.97 , pp. 9587-9592
    • Wallace-Williams, S.E.1    Moller, S.2    Goldbeck, R.A.3
  • 92
    • 0030602557 scopus 로고    scopus 로고
    • Femtosecond dynamics of intramolecular charge transfer in 4-dimethylamino-4′-cyanostilbene in polar solvents
    • Eilers-Konig N, Kuhne T, Schwarzer D, Vohringer P and Schroeder J. Femtosecond dynamics of intramolecular charge transfer in 4-dimethylamino-4′-cyanostilbene in polar solvents. Chem. Phys. Lett. 1996; 263: 69-76.
    • (1996) Chem. Phys. Lett. , vol.263 , pp. 69-76
    • Eilers-Konig, N.1    Kuhne, T.2    Schwarzer, D.3    Vohringer, P.4    Schroeder, J.5
  • 93
    • 14844350856 scopus 로고    scopus 로고
    • Subpicosecond solvation relaxation of 4-(dicyanomethylene)-2-methyl-6-(p-(dimethylamino)styryl)-4-H-pyran in polar liquids
    • van der Meulen P, Zhang H, Jonkman AM and Glasbeek M. Subpicosecond solvation relaxation of 4-(dicyanomethylene)-2-methyl-6-(p-(dimethylamino)styryl)-4-H-pyran in polar liquids. J. Phys. Chem. 1996; 100: 5367-5373.
    • (1996) J. Phys. Chem. , vol.100 , pp. 5367-5373
    • Van Der Meulen, P.1    Zhang, H.2    Jonkman, A.M.3    Glasbeek, M.4
  • 94
    • 1642425739 scopus 로고
    • About dynamic and stochastic approaches in the theory of elementary act of charge transfer in condensed media
    • Kuznetsov AM. About dynamic and stochastic approaches in the theory of elementary act of charge transfer in condensed media. Electrochemistry (Moscow) 1984; 20: 1069-1074.
    • (1984) Electrochemistry (Moscow) , vol.20 , pp. 1069-1074
    • Kuznetsov, A.M.1
  • 95
    • 0000654754 scopus 로고
    • Reversal of excitation behavior of proton transfer vs. Charge-transfer by dielectric perturbation of electronic manifolds
    • Chou P-T, Martinez MM and Clements JH. Reversal of excitation behavior of proton transfer vs. charge-transfer by dielectric perturbation of electronic manifolds. J. Phys. Chem. 1993; 97: 2618-2622.
    • (1993) J. Phys. Chem. , vol.97 , pp. 2618-2622
    • Chou, P.-T.1    Martinez, M.M.2    Clements, J.H.3
  • 96
    • 0346510946 scopus 로고    scopus 로고
    • Excited-state proton transfer and dual fluorescence of robinetin in different environments
    • Guharay J, Sengupta PK and Pradeep K. Excited-state proton transfer and dual fluorescence of robinetin in different environments. Spectrochim. Acta A 1997; 53: 905-912.
    • (1997) Spectrochim. Acta A , vol.53 , pp. 905-912
    • Guharay, J.1    Sengupta, P.K.2    Pradeep, K.3
  • 97
    • 4143065388 scopus 로고    scopus 로고
    • Intramolecular excited-state proton transfer and charge transfer fluorescence of a 3-hydroxyflavone derivative in micellar media
    • Dennison S, Guharay J and Sengupta PK. Intramolecular excited-state proton transfer and charge transfer fluorescence of a 3-hydroxyflavone derivative in micellar media. Spectrochim. Acta A 1999; 55: 903-909.
    • (1999) Spectrochim. Acta A , vol.55 , pp. 903-909
    • Dennison, S.1    Guharay, J.2    Sengupta, P.K.3
  • 98
    • 0001401520 scopus 로고    scopus 로고
    • Influence of different environments on the excited-state proton transfer and dual fluorescence of fisetin
    • Guharay J, Dennison SM and Sengupta PK. Influence of different environments on the excited-state proton transfer and dual fluorescence of fisetin. Spectrochim. Acta A 1999; 55: 1091-1099.
    • (1999) Spectrochim. Acta A , vol.55 , pp. 1091-1099
    • Guharay, J.1    Dennison, S.M.2    Sengupta, P.K.3
  • 99
    • 0000186835 scopus 로고    scopus 로고
    • Excited-state intramolecular proton transfer (ESIPT) and charge transfer (CT) fluorescence probe for model membranes
    • Dennison SM, Guharay J and Sengupta PK. Excited-state intramolecular proton transfer (ESIPT) and charge transfer (CT) fluorescence probe for model membranes. Spectrochim. Acta A 1999; 55: 1127-1132.
    • (1999) Spectrochim. Acta A , vol.55 , pp. 1127-1132
    • Dennison, S.M.1    Guharay, J.2    Sengupta, P.K.3
  • 100
    • 0035342444 scopus 로고    scopus 로고
    • Protein-flavonol interaction: Fluorescence spectroscopic studies
    • Guharay J, Sengupta B and Sengupta PK. Protein-flavonol interaction: fluorescence spectroscopic studies. Proteins 2001; 43: 75-81.
    • (2001) Proteins , vol.43 , pp. 75-81
    • Guharay, J.1    Sengupta, B.2    Sengupta, P.K.3
  • 103
    • 48749136758 scopus 로고
    • A unique excitation wavelength dependence of excited-state proton transfer in para-N,N′-aminosalicylic acid
    • Shabestary N and El-Bayoumi MA. A unique excitation wavelength dependence of excited-state proton transfer in para-N,N′-aminosalicylic acid. Chem. Phys. Lett. 1984; 106: 107-110.
    • (1984) Chem. Phys. Lett. , vol.106 , pp. 107-110
    • Shabestary, N.1    El-Bayoumi, M.A.2
  • 104
    • 33751267463 scopus 로고
    • Inhomogeneous decay kinetics and apparent solvent relaxation at low temperatures
    • Fee RS, Milsom JA and Maroncelli M. Inhomogeneous decay kinetics and apparent solvent relaxation at low temperatures. J. Phys. Chem. 1991; 95: 5170-5182.
    • (1991) J. Phys. Chem. , vol.95 , pp. 5170-5182
    • Fee, R.S.1    Milsom, J.A.2    Maroncelli, M.3
  • 105
    • 30344434220 scopus 로고
    • Dynamic Stokes shift in coumarin: Is it only relaxation?
    • Agmon N. Dynamic Stokes shift in coumarin: is it only relaxation? J. Phys. Chem. 1990; 94: 2959-2963.
    • (1990) J. Phys. Chem. , vol.94 , pp. 2959-2963
    • Agmon, N.1
  • 106
    • 0001153441 scopus 로고
    • Picosecond Stokes shift studies of solvent friction: Experimental measurements of time-dependent band shape and integrated intensity
    • Simon JD and Su S-G. Picosecond Stokes shift studies of solvent friction: experimental measurements of time-dependent band shape and integrated intensity. Chem. Phys. 1991; 152: 143-152.
    • (1991) Chem. Phys. , vol.152 , pp. 143-152
    • Simon, J.D.1    Su, S.-G.2
  • 107
    • 2642605136 scopus 로고
    • Solvation dynamics of dye molecules in polar solvents studied by hole-burning spectroscopy
    • Nishiyama K, Asano Y, Hashimoto N and Okada T. Solvation dynamics of dye molecules in polar solvents studied by hole-burning spectroscopy. J. Mol. Liquids 1995; 65/66: 41-48.
    • (1995) J. Mol. Liquids , vol.65-66 , pp. 41-48
    • Nishiyama, K.1    Asano, Y.2    Hashimoto, N.3    Okada, T.4
  • 109
  • 110
    • 0023310468 scopus 로고
    • Large edge-excitation red shift for a merocyanine dye in poly(vinyl alcohol) polymer matrix
    • Al-Hassan KA and El-Bayoumi MA. Large edge-excitation red shift for a merocyanine dye in poly(vinyl alcohol) polymer matrix. J. Polymer Sci. B 1987; 25: 495-500.
    • (1987) J. Polymer Sci. B , vol.25 , pp. 495-500
    • Al-Hassan, K.A.1    El-Bayoumi, M.A.2
  • 111
    • 0002475040 scopus 로고
    • Red edge effect (REE) phenomena of flexible solute molecules as a probe for polymer rigidity and/or free volume
    • Al-Hassan KA and Azumi T. Red edge effect (REE) phenomena of flexible solute molecules as a probe for polymer rigidity and/or free volume. Chem. Phys. Lett. 1988; 145: 49-54.
    • (1988) Chem. Phys. Lett. , vol.145 , pp. 49-54
    • Al-Hassan, K.A.1    Azumi, T.2
  • 112
    • 0347718494 scopus 로고    scopus 로고
    • Edge excitation red shift and micro environmental effects on the photophysics of quinine bisulfate diacation
    • Joshi HC, Upadhyay A, Mishra H, Tripathi HB and Pant DD. Edge excitation red shift and micro environmental effects on the photophysics of quinine bisulfate diacation. J. Photochem. Photobiol. A: Chem. 1999; 122: 185-189.
    • (1999) J. Photochem. Photobiol. A: Chem. , vol.122 , pp. 185-189
    • Joshi, H.C.1    Upadhyay, A.2    Mishra, H.3    Tripathi, H.B.4    Pant, D.D.5
  • 113
    • 0039430442 scopus 로고
    • The red edge effect as a tool for investigating the origin of the anomalous fluorescence band of 9,9′-bianthryl in rigid polar polymer matrices
    • Al-Hassan KA and Azumi T. The red edge effect as a tool for investigating the origin of the anomalous fluorescence band of 9,9′-bianthryl in rigid polar polymer matrices. Chem. Phys. Lett. 1988; 150: 344-348.
    • (1988) Chem. Phys. Lett. , vol.150 , pp. 344-348
    • Al-Hassan, K.A.1    Azumi, T.2
  • 114
    • 0040022715 scopus 로고    scopus 로고
    • Fluorescence probes as molecular weight indicators in polymers
    • Al-Hassan KA, Meetani MA and Said ZFM. Fluorescence probes as molecular weight indicators in polymers. J. Fluorescence 1998; 8: 93-100.
    • (1998) J. Fluorescence , vol.8 , pp. 93-100
    • Al-Hassan, K.A.1    Meetani, M.A.2    Said, Z.F.M.3
  • 115
    • 0030244590 scopus 로고    scopus 로고
    • Excited-state relaxation processes in polymethine dye molecules in polymeric media
    • Przhonska O, Slominsky Yu, Stahl U and Daehne S. Excited-state relaxation processes in polymethine dye molecules in polymeric media. J. Lumin. 1996; 69: 105-113.
    • (1996) J. Lumin. , vol.69 , pp. 105-113
    • Przhonska, O.1    Slominsky, Yu.2    Stahl, U.3    Daehne, S.4
  • 116
    • 0033428904 scopus 로고    scopus 로고
    • Photophysics of dimethylaminosubstituted polymethine dye in polymeric media
    • Przhonska O, Bondar M and Gallay J et al. Photophysics of dimethylaminosubstituted polymethine dye in polymeric media. J. Photochem. Photobiol. B. Biol. 1999; 52: 19-29.
    • (1999) J. Photochem. Photobiol. B. Biol. , vol.52 , pp. 19-29
    • Przhonska, O.1    Bondar, M.2    Gallay, J.3
  • 117
    • 0031647320 scopus 로고    scopus 로고
    • Influence of the attachment of chromophores to a polymer chain on their twisted intramolecular charge transfer in dilute solution
    • Bajorek A and Paczkowski J. Influence of the attachment of chromophores to a polymer chain on their twisted intramolecular charge transfer in dilute solution. Macromolecules 1998; 31: 86-95.
    • (1998) Macromolecules , vol.31 , pp. 86-95
    • Bajorek, A.1    Paczkowski, J.2
  • 118
    • 0031331268 scopus 로고    scopus 로고
    • Fluorescence monitoring of polyacrylamide hydrogel using 4-aminophthalimide
    • Datta A, Das S, Mandai D, Pal SK and Bhattacharyya K. Fluorescence monitoring of polyacrylamide hydrogel using 4-aminophthalimide. Langmuir 1997; 13: 6922-6926.
    • (1997) Langmuir , vol.13 , pp. 6922-6926
    • Datta, A.1    Das, S.2    Mandai, D.3    Pal, S.K.4    Bhattacharyya, K.5
  • 119
    • 33748392395 scopus 로고    scopus 로고
    • Solvation dynamics of Coumarin 480 in micelles
    • Sarkar N, Datta A, Das S and Bhattacharyya K. Solvation dynamics of Coumarin 480 in micelles. J. Phys. Chem. 1996; 100: 15483-15486.
    • (1996) J. Phys. Chem. , vol.100 , pp. 15483-15486
    • Sarkar, N.1    Datta, A.2    Das, S.3    Bhattacharyya, K.4
  • 121
    • 0000058811 scopus 로고    scopus 로고
    • Micellar organization and dynamics: A wavelength-selective fluorescence approach
    • Rawat S, Mukherjee S and Chattopadhyay A. Micellar organization and dynamics: a wavelength-selective fluorescence approach. J. Phys. Chem. B 1997; 101: 1922-1929.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1922-1929
    • Rawat, S.1    Mukherjee, S.2    Chattopadhyay, A.3
  • 122
    • 0000736542 scopus 로고    scopus 로고
    • Structural transition in micellar assembly - A fluorescence study
    • Rawat S and Chattopadhyay A. Structural transition in micellar assembly - a fluorescence study. J. Fluoresc. 1999; 9: 233-244.
    • (1999) J. Fluoresc. , vol.9 , pp. 233-244
    • Rawat, S.1    Chattopadhyay, A.2
  • 123
    • 0001073292 scopus 로고    scopus 로고
    • An amphiphilic hemicyanine dye employed as a sensitive probe of water in reverse AOT micelles
    • Hof M, Lianos P and Laschevsky A. An amphiphilic hemicyanine dye employed as a sensitive probe of water in reverse AOT micelles. Langmuir 1997; 13: 2181-2183.
    • (1997) Langmuir , vol.13 , pp. 2181-2183
    • Hof, M.1    Lianos, P.2    Laschevsky, A.3
  • 124
    • 0030596387 scopus 로고    scopus 로고
    • Luminescence behavior of 7-hydroxyflavone in aerosol OT reverse micelles: Excited-state proton transfer and red-edge excitation effects
    • Sarkar M, Ray JG and Sengupta PK. Luminescence behavior of 7-hydroxyflavone in aerosol OT reverse micelles: excited-state proton transfer and red-edge excitation effects. J. Photochem. Phoiobiol. A. Chem. 1996; 95: 157-160.
    • (1996) J. Photochem. Phoiobiol. A. Chem. , vol.95 , pp. 157-160
    • Sarkar, M.1    Ray, J.G.2    Sengupta, P.K.3
  • 125
    • 0009764489 scopus 로고    scopus 로고
    • Structural studies of thin AOT films by using the polarity fluorescent probe Coumarin-153
    • Hof M and Lianos P. Structural studies of thin AOT films by using the polarity fluorescent probe Coumarin-153. Langmuir 1997; 13: 290-294.
    • (1997) Langmuir , vol.13 , pp. 290-294
    • Hof, M.1    Lianos, P.2
  • 126
    • 0033624316 scopus 로고    scopus 로고
    • The role of molecular size in the excited-state behavior of aminocoumarine dyes in restricted media. 2: Study of BC1 in AOT-formaldehyde reversed micelles
    • Raju BB and Costa SM. The role of molecular size in the excited-state behavior of aminocoumarine dyes in restricted media. 2: Study of BC1 in AOT-formaldehyde reversed micelles. Spectrochim. Acta A 2000; 56: 1703-1710.
    • (2000) Spectrochim. Acta A , vol.56 , pp. 1703-1710
    • Raju, B.B.1    Costa, S.M.2
  • 127
    • 0021766889 scopus 로고
    • Red-edge excitation of fluorescence and dynamic properties of proteins and membranes
    • Lakowicz JR and Keating-Nakamoto S. Red-edge excitation of fluorescence and dynamic properties of proteins and membranes. Biochemistry 1984; 23: 3013-3021.
    • (1984) Biochemistry , vol.23 , pp. 3013-3021
    • Lakowicz, J.R.1    Keating-Nakamoto, S.2
  • 128
    • 0021968028 scopus 로고
    • Nanosecond dynamics of charged fluorescent probes at the polar interface of a membrane phospholipid bilayer
    • Demchenko AP and Shcherbatska NV. Nanosecond dynamics of charged fluorescent probes at the polar interface of a membrane phospholipid bilayer. Biophys Chem. 1985; 22: 131-143.
    • (1985) Biophys Chem. , vol.22 , pp. 131-143
    • Demchenko, A.P.1    Shcherbatska, N.V.2
  • 129
    • 0040615711 scopus 로고
    • Segmentary mobility of phospholipid in bilayer membrane in the binding site of uncharged fluorescent probes
    • Scherbatska NV and Demchenko AP. Segmentary mobility of phospholipid in bilayer membrane in the binding site of uncharged fluorescent probes. Biofizika 1989; 31: 574-578.
    • (1989) Biofizika , vol.31 , pp. 574-578
    • Scherbatska, N.V.1    Demchenko, A.P.2
  • 130
    • 0017143855 scopus 로고
    • Nanosecond time-resolved emission spectroscopy of a fluorescent probe adsorbed to L-α-egg lecithin vesicles
    • Easter JH, DeToma RP and Brand L, Nanosecond time-resolved emission spectroscopy of a fluorescent probe adsorbed to L-α-egg lecithin vesicles. Biophys. J. 1976; 16: 571-583.
    • (1976) Biophys. J. , vol.16 , pp. 571-583
    • Easter, J.H.1    DeToma, R.P.2    Brand, L.3
  • 132
    • 0027174080 scopus 로고
    • Fluorophore environment in membrane-bound probes: A red edge excitation shift study
    • Chattopadhyay A and Mukherjee S. Fluorophore environment in membrane-bound probes: a red edge excitation shift study. Biochemistry 1993; 32: 3804-3811.
    • (1993) Biochemistry , vol.32 , pp. 3804-3811
    • Chattopadhyay, A.1    Mukherjee, S.2
  • 133
    • 0001158157 scopus 로고    scopus 로고
    • Red edge excitation shift of deeply imbedded membrane probe-implication in water penetration in the bilayer
    • Chattopadhyay A and Mukherjee S. Red edge excitation shift of deeply imbedded membrane probe-implication in water penetration in the bilayer. J. Phys. Chem B 1999; 103: 8180-8185.
    • (1999) J. Phys. Chem B , vol.103 , pp. 8180-8185
    • Chattopadhyay, A.1    Mukherjee, S.2
  • 134
    • 0344927570 scopus 로고    scopus 로고
    • Depth-dependent solvent relaxation in membranes - Wavelength-selective fluorescence as a membrane dipstick
    • Chattopadhyay A and Mukherjee S. Depth-dependent solvent relaxation in membranes - wavelength-selective fluorescence as a membrane dipstick. Langmuir 1999; 15: 2142-2148.
    • (1999) Langmuir , vol.15 , pp. 2142-2148
    • Chattopadhyay, A.1    Mukherjee, S.2
  • 135
    • 0030749502 scopus 로고    scopus 로고
    • Ionization, partitioning and dynamics of tryptophan octyl ester: Implications for membrane-bound tryptophan residues
    • Chattopadhyay A, Mukherjee S, Rukmini R, Rwatt SS and Sudha S. Ionization, partitioning and dynamics of tryptophan octyl ester: implications for membrane-bound tryptophan residues. Biophys. J. 1997; 73: 839-849.
    • (1997) Biophys. J. , vol.73 , pp. 839-849
    • Chattopadhyay, A.1    Mukherjee, S.2    Rukmini, R.3    Rwatt, S.S.4    Sudha, S.5
  • 136
    • 0027508011 scopus 로고
    • Intramolecular dynamics in the environment of the single tryptophan residue in staphylococcal nuclease
    • Demchenko AP, Gryczynski I, Gryczynski Z, Wiczk W, Malak H and Fishman M. Intramolecular dynamics in the environment of the single tryptophan residue in staphylococcal nuclease. Biophys. Chem. 1993; 48: 39-18.
    • (1993) Biophys. Chem. , vol.48 , pp. 39-118
    • Demchenko, A.P.1    Gryczynski, I.2    Gryczynski, Z.3    Wiczk, W.4    Malak, H.5    Fishman, M.6
  • 137
    • 0023334542 scopus 로고
    • Structural-dynamic properties of the tryptophan residue environment in melittin
    • Demchenko AP, Ladokhin AS and Kostrzhevska EG. Structural-dynamic properties of the tryptophan residue environment in melittin. Mol. Biol. (Moscow) 1987; 21: 663-671.
    • (1987) Mol. Biol. (Moscow) , vol.21 , pp. 663-671
    • Demchenko, A.P.1    Ladokhin, A.S.2    Kostrzhevska, E.G.3
  • 138
    • 0024283409 scopus 로고
    • Temperature-dependent shift of fluorescence spectra without conformational changes in protein: Studies of dipole relaxations in melittin molecule
    • Demchenko AP and Ladohin AS. Temperature-dependent shift of fluorescence spectra without conformational changes in protein: studies of dipole relaxations in melittin molecule. Biochim. Biophys. Acra 1989; 955: 352-360.
    • (1989) Biochim. Biophys. Acra , vol.955 , pp. 352-360
    • Demchenko, A.P.1    Ladohin, A.S.2
  • 139
    • 0347173726 scopus 로고    scopus 로고
    • Assignment of log-normal components of protein fluorescence spectra to individual tryptophan residues using their microenvironment properties in three-dimensional structure
    • Reshetnyak YAK and Burstein EA. Assignment of log-normal components of protein fluorescence spectra to individual tryptophan residues using their microenvironment properties in three-dimensional structure. Biofizika 1997; 42: 293-300.
    • (1997) Biofizika , vol.42 , pp. 293-300
    • Reshetnyak, Y.A.K.1    Burstein, E.A.2
  • 140
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem JM and Brand L. Time-resolved fluorescence of proteins. Ann. Rev. Biochtm. 1985; 54: 43-71.
    • (1985) Ann. Rev. Biochtm. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 141
    • 0026505882 scopus 로고
    • Red-edge excitation fluorescence measurements of several two-tryptophan-containing proteins
    • Wasylewski Z, Koloczek H, Wasniowska A and Slizowska K. Red-edge excitation fluorescence measurements of several two-tryptophan-containing proteins. Eur. J. Biochem. 1992; 206: 235-242.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 235-242
    • Wasylewski, Z.1    Koloczek, H.2    Wasniowska, A.3    Slizowska, K.4
  • 142
    • 0029841539 scopus 로고    scopus 로고
    • Tubulin conformation and dynamics: A red edge excitation shift study
    • Guha S, Rawat SS, Chattopadhyay A and Bhattacharyya B. Tubulin conformation and dynamics: a red edge excitation shift study. Biochemistry 1996; 35: 13426-13433.
    • (1996) Biochemistry , vol.35 , pp. 13426-13433
    • Guha, S.1    Rawat, S.S.2    Chattopadhyay, A.3    Bhattacharyya, B.4
  • 143
    • 0019885903 scopus 로고
    • Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase
    • Ross JB and Schmidt CJ and Brand L. Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry 1981; 20: 4369-4377.
    • (1981) Biochemistry , vol.20 , pp. 4369-4377
    • Ross, J.B.1    Schmidt, C.J.2    Brand, L.3
  • 144
    • 0032532547 scopus 로고    scopus 로고
    • Resolution of the heterogeneous fluorescence in multi-tryptophan proteins: Ascorbate oxydase
    • Di Venere A, Mei G and Gilardi G et al. Resolution of the heterogeneous fluorescence in multi-tryptophan proteins: ascorbate oxydase. Eur. J. Biochem. 1998; 257: 337-343.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 337-343
    • Di Venere, A.1    Mei, G.2    Gilardi, G.3
  • 145
    • 0035907114 scopus 로고    scopus 로고
    • On the excited-state energy transfer between tryptophan residues in proteins: The case of penicillin acylase
    • Ercelen S, Kazan D, Erarslan A and Demchenko AP. On the excited-state energy transfer between tryptophan residues in proteins: the case of penicillin acylase. Biophys. Chem. 2001; 90: 203-217.
    • (2001) Biophys. Chem. , vol.90 , pp. 203-217
    • Ercelen, S.1    Kazan, D.2    Erarslan, A.3    Demchenko, A.P.4
  • 146
    • 0027731415 scopus 로고
    • Fluorescence spectroscopic studies on equilibrium dipole-relaxational dynamics of Na,K-ATPase
    • Demchenko AP, Apell HJ, Sturmer W and Feddersen B. Fluorescence spectroscopic studies on equilibrium dipole-relaxational dynamics of Na,K-ATPase. Biophys. Chem. 1993; 48: 135-147.
    • (1993) Biophys. Chem. , vol.48 , pp. 135-147
    • Demchenko, A.P.1    Apell, H.J.2    Sturmer, W.3    Feddersen, B.4
  • 147
    • 0032499727 scopus 로고    scopus 로고
    • Fluorescence heterogeneity of tryptophans in Na.K-ATPase: Evidences for temperature-dependent energy transfer
    • Demchenko AP, Gallay J, Vincent M and Apell HJ. Fluorescence heterogeneity of tryptophans in Na.K-ATPase: evidences for temperature-dependent energy transfer. Biophys. Chem. 1998; 72: 265-283.
    • (1998) Biophys. Chem. , vol.72 , pp. 265-283
    • Demchenko, A.P.1    Gallay, J.2    Vincent, M.3    Apell, H.J.4
  • 148
    • 0028932060 scopus 로고
    • Selective steady-state and time-resolved fluorescence spectroscopy of an HLA-A2-peptide complex
    • Gakamsky DM, Haas E, Robbins P, Strominger JL and Pecht I. Selective steady-state and time-resolved fluorescence spectroscopy of an HLA-A2-peptide complex. Immunol. Lett. 1995; 44: 195-201.
    • (1995) Immunol. Lett. , vol.44 , pp. 195-201
    • Gakamsky, D.M.1    Haas, E.2    Robbins, P.3    Strominger, J.L.4    Pecht, I.5
  • 149
    • 0040615712 scopus 로고    scopus 로고
    • A nanosecond time-resolved study of recombinant human myelin basic protein
    • Russo AT and Brand L. A nanosecond time-resolved study of recombinant human myelin basic protein. J. Fluoresc. 1999; 9: 333-342.
    • (1999) J. Fluoresc. , vol.9 , pp. 333-342
    • Russo, A.T.1    Brand, L.2
  • 150
  • 151
    • 0035743185 scopus 로고    scopus 로고
    • Tryptophan rotamers report the conformational dynamics of proteins
    • in press
    • Fidy J, Laberge M and Ullrich B et al. Tryptophan rotamers report the conformational dynamics of proteins. Pure Appl. Chem. 2001; 73 (in press).
    • (2001) Pure Appl. Chem. , vol.73
    • Fidy, J.1    Laberge, M.2    Ullrich, B.3
  • 152
    • 0034309767 scopus 로고    scopus 로고
    • On spectral relaxation in proteins
    • Lakowicz JR. On spectral relaxation in proteins. Photochem. Photobiol. 2000; 72: 421-437.
    • (2000) Photochem. Photobiol. , vol.72 , pp. 421-437
    • Lakowicz, J.R.1
  • 153
    • 0025857326 scopus 로고
    • The fluorescence quenching resolved spectra and red-edge excitation fluorescence measurements of human alpha 1-proteinase inhibitor
    • Koloczek H, Wasniowska A, Potempa J and Wasylewski Z. The fluorescence quenching resolved spectra and red-edge excitation fluorescence measurements of human alpha 1-proteinase inhibitor. Biochim. Biophys. Acta 1991; 1073: 619-625.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 619-625
    • Koloczek, H.1    Wasniowska, A.2    Potempa, J.3    Wasylewski, Z.4
  • 154
    • 0031217630 scopus 로고    scopus 로고
    • Red edge excitation shift emission spectroscopic investigation of serum albumins and serum albumin-bilirubin complexes
    • Patra SK and Pal MK. Red edge excitation shift emission spectroscopic investigation of serum albumins and serum albumin-bilirubin complexes. Spectrochim. Acta A 1997; 53: 1609-1614.
    • (1997) Spectrochim. Acta A , vol.53 , pp. 1609-1614
    • Patra, S.K.1    Pal, M.K.2
  • 155
    • 0030764465 scopus 로고    scopus 로고
    • Binding effect of progesterone on the dynamics of alpha 1-acid glycoprotein
    • Albani JR. Binding effect of progesterone on the dynamics of alpha 1-acid glycoprotein. Biochim. Biophys. Acta 1997; 1336: 349-359.
    • (1997) Biochim. Biophys. Acta , vol.1336 , pp. 349-359
    • Albani, J.R.1
  • 156
    • 0031612885 scopus 로고    scopus 로고
    • Correlation between dynamics, structure and spectral properties of human alpha 1-acid glycoprotein (orosomucoid): A fluorescence approach
    • Albani JR. Correlation between dynamics, structure and spectral properties of human alpha 1-acid glycoprotein (orosomucoid): a fluorescence approach. Spectrochim. Acta A 1998; 54: 175-183.
    • (1998) Spectrochim. Acta A , vol.54 , pp. 175-183
    • Albani, J.R.1
  • 157
    • 0029658224 scopus 로고    scopus 로고
    • Serpin alpha 1-proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy
    • Koloczek H, Banbula A, Salvesen GS and Potempa J. Serpin alpha 1-proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopy. Protein Sci. 1996; 5: 2226-2235.
    • (1996) Protein Sci. , vol.5 , pp. 2226-2235
    • Koloczek, H.1    Banbula, A.2    Salvesen, G.S.3    Potempa, J.4
  • 158
    • 0029938595 scopus 로고    scopus 로고
    • Conformation, stability and interactions of corneal keratan sulfate proteoglycan
    • Uma L, Sharma Y and Balasubramanian D. Conformation, stability and interactions of corneal keratan sulfate proteoglycan. Biochim. Biophys. Acta 1996; 1294: 8-14.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 8-14
    • Uma, L.1    Sharma, Y.2    Balasubramanian, D.3
  • 159
    • 0029146508 scopus 로고
    • Fluorescence of a tryptophan-bearing peptide from smooth muscle myosin light chain kinase upon binding to two closely related calmodulins
    • Chabbert M, Piemont E, Prendergast FG and Lami H. Fluorescence of a tryptophan-bearing peptide from smooth muscle myosin light chain kinase upon binding to two closely related calmodulins. Arch. Biochem. Biophys. 1995; 322: 429-436.
    • (1995) Arch. Biochem. Biophys. , vol.322 , pp. 429-436
    • Chabbert, M.1    Piemont, E.2    Prendergast, F.G.3    Lami, H.4
  • 160
    • 0028142742 scopus 로고
    • Effects of sialic acids and the beta-drug adrenergic blocker, propranolol, on the dynamics of human alpha 1-acid glycoprotein: A fluorescence study
    • Albani JR. Effects of sialic acids and the beta-drug adrenergic blocker, propranolol, on the dynamics of human alpha 1-acid glycoprotein: a fluorescence study. J. Biochem. (Tokyo) 1994; 116: 625-630.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 625-630
    • Albani, J.R.1
  • 161
    • 0034738907 scopus 로고    scopus 로고
    • Human pyridoxal kinase: Overexpression and properties of the recombinant enzyme
    • Lee HS, Moon BJ, Choi SY and Kwon OS. Human pyridoxal kinase: overexpression and properties of the recombinant enzyme. Mol. Cell. 2000; 10: 452-459.
    • (2000) Mol. Cell. , vol.10 , pp. 452-459
    • Lee, H.S.1    Moon, B.J.2    Choi, S.Y.3    Kwon, O.S.4
  • 162
    • 0026670154 scopus 로고
    • Molecular relaxation spectroscopy of flavin adenine dinucleotide in wild type and mutant lipoamide dehydrogenase from Azotobacter vinelandii
    • Bastiaens PI, van Hoek A, van Berkel WJ, de Kok A and Visser AJ. Molecular relaxation spectroscopy of flavin adenine dinucleotide in wild type and mutant lipoamide dehydrogenase from Azotobacter vinelandii. Biochemistry 1992; 31: 7061-7068.
    • (1992) Biochemistry , vol.31 , pp. 7061-7068
    • Bastiaens, P.I.1    Van Hoek, A.2    Van Berkel, W.J.3    De Kok, A.4    Visser, A.J.5
  • 163
    • 0026737642 scopus 로고
    • Conformational dynamics and intersubunit energy transfer in wild-type and mutant lipoamide dehydrogenase from Azotobacter vinelandii. A multidimensional time-resolved polarized fluorescence study
    • Bastiaens PI, van Hoek A, Benen JA, Brochon JC and Visser AJ. Conformational dynamics and intersubunit energy transfer in wild-type and mutant lipoamide dehydrogenase from Azotobacter vinelandii. A multidimensional time-resolved polarized fluorescence study. Biophys. J. 1992; 63: 839-853.
    • (1992) Biophys. J. , vol.63 , pp. 839-853
    • Bastiaens, P.I.1    Van Hoek, A.2    Benen, J.A.3    Brochon, J.C.4    Visser, A.J.5
  • 164
    • 0024441603 scopus 로고
    • Time-resolved fluorescence spectroscopy of NADPH-cytochrome P-450 reductase: Demonstration of energy transfer between the two prosthetic groups
    • Bastiaens PI, Bonants PJ, Muller F and Visser AJ. Time-resolved fluorescence spectroscopy of NADPH-cytochrome P-450 reductase: demonstration of energy transfer between the two prosthetic groups. Biochemistry 1989; 28: 8416-8425.
    • (1989) Biochemistry , vol.28 , pp. 8416-8425
    • Bastiaens, P.I.1    Bonants, P.J.2    Muller, F.3    Visser, A.J.4
  • 165
    • 0004382970 scopus 로고
    • Fluorescence molecular relaxation studies of protein dynamics. The TNS-binding site in melittin is rigid on nanosecond time scale
    • Demchenko AP. Fluorescence molecular relaxation studies of protein dynamics. The TNS-binding site in melittin is rigid on nanosecond time scale. FEBS Lett. 1985; 182: 99-102.
    • (1985) FEBS Lett. , vol.182 , pp. 99-102
    • Demchenko, A.P.1
  • 166
    • 0026727945 scopus 로고
    • Motions studies of the human alpha 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and polarization of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues
    • Albani J. Motions studies of the human alpha 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and polarization of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues. Biophys. Chem. 1992; 44: 129-137.
    • (1992) Biophys. Chem. , vol.44 , pp. 129-137
    • Albani, J.1
  • 167
    • 0022429034 scopus 로고
    • Interfacial properties of model membranes and plasma lipoproteins containing ether lipids
    • Massey JB, She HS and Pownall HJ. Interfacial properties of model membranes and plasma lipoproteins containing ether lipids. Biochemistry 1985; 24: 6973-6978.
    • (1985) Biochemistry , vol.24 , pp. 6973-6978
    • Massey, J.B.1    She, H.S.2    Pownall, H.J.3
  • 168
    • 0035795727 scopus 로고    scopus 로고
    • Interaction and structure induction of cell-permeant peptides in the presence of phospholipid vesicles
    • Magzoub M, Kilk K, Eriksson LE, Langel U and Graslund A. Interaction and structure induction of cell-permeant peptides in the presence of phospholipid vesicles. Biochim. Biophys. Acta 2001; 1512: 77-89.
    • (2001) Biochim. Biophys. Acta , vol.1512 , pp. 77-89
    • Magzoub, M.1    Kilk, K.2    Eriksson, L.E.3    Langel, U.4    Graslund, A.5
  • 169
    • 0027363792 scopus 로고
    • Restricted mobility of the sole tryptophan in membrane-bound melittin
    • Chattopadhyay A and Rukmini R. Restricted mobility of the sole tryptophan in membrane-bound melittin. FEBS Lett. 1993; 335: 341-344.
    • (1993) FEBS Lett. , vol.335 , pp. 341-344
    • Chattopadhyay, A.1    Rukmini, R.2
  • 170
    • 0030704248 scopus 로고    scopus 로고
    • Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: Implications in membrane organization and function
    • Ghosh AK, Rukmini R and Chattopadhyay A. Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function. Biochemistry 1997; 36: 14291-14305.
    • (1997) Biochemistry , vol.36 , pp. 14291-14305
    • Ghosh, A.K.1    Rukmini, R.2    Chattopadhyay, A.3
  • 171
    • 0032982573 scopus 로고    scopus 로고
    • Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus
    • Raja SM, Rawat SS, Chattopadhyay A and Lala AK. Localization and environment of tryptophans in soluble and membrane-bound states of a pore-forming toxin from Staphylococcus aureus. Biophys J. 1999; 76: 1469-1479.
    • (1999) Biophys J. , vol.76 , pp. 1469-1479
    • Raja, S.M.1    Rawat, S.S.2    Chattopadhyay, A.3    Lala, A.K.4
  • 172
    • 0028352135 scopus 로고
    • Motionally restricted tryptophan environments at the peptide-lipid interface of gramicidin channels
    • Mukherjee S and Chattopadhyay A. Motionally restricted tryptophan environments at the peptide-lipid interface of gramicidin channels. Biochemistry 1994; 33: 5089-5097.
    • (1994) Biochemistry , vol.33 , pp. 5089-5097
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 173
    • 0032537597 scopus 로고    scopus 로고
    • Interaction of the major epitope region of HIV protein gp41 with membrane model systems. A fluorescence spectroscopy study
    • Santos NC, Prieto M and Castanho MA. Interaction of the major epitope region of HIV protein gp41 with membrane model systems. A fluorescence spectroscopy study. Biochemistry 1998; 37: 8674-8682.
    • (1998) Biochemistry , vol.37 , pp. 8674-8682
    • Santos, N.C.1    Prieto, M.2    Castanho, M.A.3
  • 174
    • 0033578448 scopus 로고    scopus 로고
    • Helix-helix association of a lipid-bound amphipathic alpha-helix derived from apolipoprotein C-II
    • MacPhee CE, Hewlett GJ, Sawyer WH and Clayton AH. Helix-helix association of a lipid-bound amphipathic alpha-helix derived from apolipoprotein C-II. Biochemistry 1999; 38: 10878-10884.
    • (1999) Biochemistry , vol.38 , pp. 10878-10884
    • MacPhee, C.E.1    Hewlett, G.J.2    Sawyer, W.H.3    Clayton, A.H.4
  • 175
    • 0011301641 scopus 로고
    • Spectral inhomogeneity and wavelength-dependent rotation of probe molecules in membranes
    • Nemkovich NA and Rubinov AN. Spectral inhomogeneity and wavelength-dependent rotation of probe molecules in membranes. J. Fluoresc. 1995; 5: 285-294.
    • (1995) J. Fluoresc. , vol.5 , pp. 285-294
    • Nemkovich, N.A.1    Rubinov, A.N.2
  • 176
    • 0029224117 scopus 로고
    • Spectral inhomogeneity and intramolecular relaxation in erythrocyte ghosts and phospholipid bilayer membranes
    • Nemkovich NA, Kozlovsky AS and Rubinov AN. Spectral inhomogeneity and intramolecular relaxation in erythrocyte ghosts and phospholipid bilayer membranes. Proc. SPIE Int. Soc. Opt. Eng. 1995; 2388: 389-399.
    • (1995) Proc. SPIE Int. Soc. Opt. Eng. , vol.2388 , pp. 389-399
    • Nemkovich, N.A.1    Kozlovsky, A.S.2    Rubinov, A.N.3
  • 177
    • 0034710250 scopus 로고    scopus 로고
    • Interaction between carbohydrate residues of alpha 1-acid glycoprotein (orosomucoid) and saturating concentrations of Calcofluor white. A fluorescence study
    • Albani JR, Sillen A, Plancke YD, Coddeville B and Engelborghs Y. Interaction between carbohydrate residues of alpha 1-acid glycoprotein (orosomucoid) and saturating concentrations of Calcofluor white. A fluorescence study. Carbohydr. Res. 2000; 327: 333-340.
    • (2000) Carbohydr. Res. , vol.327 , pp. 333-340
    • Albani, J.R.1    Sillen, A.2    Plancke, Y.D.3    Coddeville, B.4    Engelborghs, Y.5
  • 178
    • 0032755450 scopus 로고    scopus 로고
    • Dynamics of carbohydrate residues of alpha 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and emission anisotropy studies of Calcofluor White
    • Albani JR, Sillen A, Coddeville B, Plancke YD and Engelborghs Y. Dynamics of carbohydrate residues of alpha 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and emission anisotropy studies of Calcofluor White. Carbohydr. Res. 1999; 322: 87-94.
    • (1999) Carbohydr. Res. , vol.322 , pp. 87-94
    • Albani, J.R.1    Sillen, A.2    Coddeville, B.3    Plancke, Y.D.4    Engelborghs, Y.5
  • 179
    • 0029992307 scopus 로고    scopus 로고
    • Fluorescence studies of DNA and RNA structure and dynamics
    • Millar DP. Fluorescence studies of DNA and RNA structure and dynamics. Curr. Opinion Structural Biol. 1996; 6: 322-326.
    • (1996) Curr. Opinion Structural Biol. , vol.6 , pp. 322-326
    • Millar, D.P.1
  • 180
    • 0028832014 scopus 로고
    • Fluorescent d(CGCGAATTCGCG): Characterization of the major groove polarity and study of minor groove interactions through a major groove semantophore conjugate
    • Barawkar DA and Ganesh KN. Fluorescent d(CGCGAATTCGCG): characterization of the major groove polarity and study of minor groove interactions through a major groove semantophore conjugate. Nucleic Acids Res. 1995; 23: 159-164.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 159-164
    • Barawkar, D.A.1    Ganesh, K.N.2
  • 181
    • 33845551513 scopus 로고
    • Picosecond fluorescence anisotropy decay in the ethidium/DNA complex
    • Magde D, Zappala M, Knox WH and Nordlund TM. Picosecond fluorescence anisotropy decay in the ethidium/DNA complex. J. Phys. Chem. 1983; 87: 3286-3288.
    • (1983) J. Phys. Chem. , vol.87 , pp. 3286-3288
    • Magde, D.1    Zappala, M.2    Knox, W.H.3    Nordlund, T.M.4
  • 182
    • 0028341190 scopus 로고
    • Greenstock. Fluorescence lifetime analysis of DNA intercalated ethidium bromide and quenching by free dye
    • Heller DP. Greenstock. Fluorescence lifetime analysis of DNA intercalated ethidium bromide and quenching by free dye. Biophys. Chem. 1994; 50: 305-312.
    • (1994) Biophys. Chem. , vol.50 , pp. 305-312
    • Heller, D.P.1
  • 183
    • 0032486312 scopus 로고    scopus 로고
    • Taxol-DNA interactions: Fluorescence and CD studies of DNA groove binding properties of taxol
    • Krishna AG, Kumar DV, Khan BM, Rawal SK and Ganesh KN. Taxol-DNA interactions: fluorescence and CD studies of DNA groove binding properties of taxol. Biochim. Biophys. Acta 1998; 1381: 104-112.
    • (1998) Biochim. Biophys. Acta , vol.1381 , pp. 104-112
    • Krishna, A.G.1    Kumar, D.V.2    Khan, B.M.3    Rawal, S.K.4    Ganesh, K.N.5
  • 184
    • 0000879525 scopus 로고
    • Site-dependent fluorescence lifetimes of isolated dye molecules absorbed on organic single crystals and other substrates
    • Kemnitz K, Tamai N, Yamazaki I, Nakashima N and Yoshihara K. Site-dependent fluorescence lifetimes of isolated dye molecules absorbed on organic single crystals and other substrates. J. Phys. Chem. 1987; 91: 1423-1430.
    • (1987) J. Phys. Chem. , vol.91 , pp. 1423-1430
    • Kemnitz, K.1    Tamai, N.2    Yamazaki, I.3    Nakashima, N.4    Yoshihara, K.5
  • 185
    • 84912813327 scopus 로고
    • Low-temperature spectra of anthracene absorbed on silicone surface at selective laser irradiation
    • Bykovskaja LA, Kulikov SG, Eremenko AM and Yankovich BN. Low-temperature spectra of anthracene absorbed on silicone surface at selective laser irradiation. Opt. Spektr. 1988; 64: 320-323.
    • (1988) Opt. Spektr. , vol.64 , pp. 320-323
    • Bykovskaja, L.A.1    Kulikov, S.G.2    Eremenko, A.M.3    Yankovich, B.N.4
  • 186
    • 0004409031 scopus 로고    scopus 로고
    • Dynamics of Trp residues in crystals of human α 1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra
    • Albani JR. Dynamics of Trp residues in crystals of human α 1-acid
    • (1998) J. Fluoresc. , vol.8 , pp. 213-224
    • Albani, J.R.1
  • 187
    • 0032102452 scopus 로고    scopus 로고
    • Structure and topography of membrane binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles
    • Veeraraghavan S, Baleja JD and Gilbert GE. Structure and topography of membrane binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles. Biochem. J. 1998; 332: 549-555.
    • (1998) Biochem. J. , vol.332 , pp. 549-555
    • Veeraraghavan, S.1    Baleja, J.D.2    Gilbert, G.E.3
  • 188
    • 0028031342 scopus 로고
    • Red-edge excitation fluorescence spectroscopy of proteins in reversed micelles
    • Guz A and Wasylewski Z. Red-edge excitation fluorescence spectroscopy of proteins in reversed micelles. J. Protein Chem. 1994; 13: 393-399.
    • (1994) J. Protein Chem. , vol.13 , pp. 393-399
    • Guz, A.1    Wasylewski, Z.2
  • 189
    • 0031574008 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes in the serine proteinsase savinase - A tryptophan fluorescence and circular-dichroism study
    • Maste MCL, Norde W and Visser AJWC. Adsorption-induced conformational changes in the serine proteinsase savinase - a tryptophan fluorescence and circular-dichroism study. J. Colloid Interface Sci. 1997; 196: 224-230.
    • (1997) J. Colloid Interface Sci. , vol.196 , pp. 224-230
    • Maste, M.C.L.1    Norde, W.2    Ajwc, V.3
  • 190
    • 0031655462 scopus 로고    scopus 로고
    • The measurement of intrinsic fluorescence to probe the conformational flexibility and thermodynamic stability of a single tryptophan protein entrapped in a sol-gel derived glass matrix
    • Zheng I and Brennan JD. The measurement of intrinsic fluorescence to probe the conformational flexibility and thermodynamic stability of a single tryptophan protein entrapped in a sol-gel derived glass matrix. Analyst 1998; 123: 1735-1744.
    • (1998) Analyst , vol.123 , pp. 1735-1744
    • Zheng, I.1    Brennan, J.D.2
  • 191
    • 0032632382 scopus 로고    scopus 로고
    • Using intrinsic fluorescence to investigate proteins entrapped in sol-gel derived materials
    • Brennan JD. Using intrinsic fluorescence to investigate proteins entrapped in sol-gel derived materials. Appl. Spectr. 1999; 53: A106-121.
    • (1999) Appl. Spectr. , vol.53
    • Brennan, J.D.1
  • 192
    • 0024722578 scopus 로고
    • Red edge excitation effect in intact eye lens
    • Rao CM, Rao SC and Rao PB. Red edge excitation effect in intact eye lens. Photochem. Photobiol. 1989; 50: 399-402.
    • (1989) Photochem. Photobiol. , vol.50 , pp. 399-402
    • Rao, C.M.1    Rao, S.C.2    Rao, P.B.3
  • 193
    • 0028084943 scopus 로고
    • Red edge excitation shifts of crystallins and intact lenses. A study of segmental mobility and interprotein interactions
    • Rao SC and Rao CM. Red edge excitation shifts of crystallins and intact lenses. A study of segmental mobility and interprotein interactions. FEBS Lett. 1994; 337: 269-273.
    • (1994) FEBS Lett. , vol.337 , pp. 269-273
    • Rao, S.C.1    Rao, C.M.2
  • 194
    • 0038837741 scopus 로고
    • Application of spectrophotometry in ultraviolet and visible region
    • Springer-Verlag: Berlin. Heidelberg
    • Neubacher H and Lohmann W. Application of spectrophotometry in ultraviolet and visible region. In Biophysics. Springer-Verlag: Berlin. Heidelberg 1988; 100-108.
    • (1988) Biophysics , pp. 100-108
    • Neubacher, H.1    Lohmann, W.2
  • 195
    • 0038877839 scopus 로고    scopus 로고
    • Spectroscopic studies of solvation dynamics of fluoroprobe in liquid solutions
    • Middelhoek ER, Zhang H, Verhoeven JW and Glasbeek M. Spectroscopic studies of solvation dynamics of fluoroprobe in liquid solutions. Chem. Phys. 1996; 211: 489-497.
    • (1996) Chem. Phys. , vol.211 , pp. 489-497
    • Middelhoek, E.R.1    Zhang, H.2    Verhoeven, J.W.3    Glasbeek, M.4
  • 196
    • 0010715609 scopus 로고
    • Synthesis and spectroscopic studies of 4-formyl-4′-N,N-dimethylamino-1,1′-biphenyl: The unusual red edge effect and efficient laser generation
    • Chou P-T; Chang C-P, Clements JH and Kuo M-S. Synthesis and spectroscopic studies of 4-formyl-4′-N,N-dimethylamino-1,1′-biphenyl: the unusual red edge effect and efficient laser generation. J. Fluoresc. 1995; 5: 369-376.
    • (1995) J. Fluoresc. , vol.5 , pp. 369-376
    • Chou, P.-T.1    Chang, C.-P.2    Clements, J.H.3    Kuo, M.-S.4
  • 197
    • 5844252510 scopus 로고
    • Solvatochromic dyes as solvent polarity indicators
    • Reichardt C. Solvatochromic dyes as solvent polarity indicators. Chem. Rev. 1994; 94: 2319-2358.
    • (1994) Chem. Rev. , vol.94 , pp. 2319-2358
    • Reichardt, C.1
  • 198
    • 0031012421 scopus 로고    scopus 로고
    • Optical detection of membrane dipole potential: Avoidance of fluidity and dye-induced effects
    • Clarke RJ and Kane DJ. Optical detection of membrane dipole potential: avoidance of fluidity and dye-induced effects. Biochim. Biophys. Acta 1997; 1323: 223-239.
    • (1997) Biochim. Biophys. Acta , vol.1323 , pp. 223-239
    • Clarke, R.J.1    Kane, D.J.2
  • 199
    • 4244128229 scopus 로고
    • The influence of molecular geometry on the fluorescence spectra of biphenyl and the polyphenyls
    • Razi Naqvi K, Donatsch J and Wild UP. The influence of molecular geometry on the fluorescence spectra of biphenyl and the polyphenyls. Chem. Phys. Lett. 1975; 34: 285-288.
    • (1975) Chem. Phys. Lett. , vol.34 , pp. 285-288
    • Razi Naqvi, K.1    Donatsch, J.2    Wild, U.P.3
  • 200
    • 0038801459 scopus 로고
    • Biexponemial fluorescence decay of biphenylbutadiene rotational isomers after extreme red-edge excitation
    • Moeler S, Yee WA, Goldbeck RA and Wallace-Williams SE. Biexponemial fluorescence decay of biphenylbutadiene rotational isomers after extreme red-edge excitation. Chem. Phys. Lett. 1995; 243: 579-585.
    • (1995) Chem. Phys. Lett. , vol.243 , pp. 579-585
    • Moeler, S.1    Yee, W.A.2    Goldbeck, R.A.3    Wallace-Williams, S.E.4
  • 201
    • 0002286419 scopus 로고    scopus 로고
    • Red-edge excitation study of non-exponential fluorescence decay of indole in solution and in a protein
    • Ladokhin AS. Red-edge excitation study of non-exponential fluorescence decay of indole in solution and in a protein. J. Fluoresc. 1999; 9: 1-9.
    • (1999) J. Fluoresc. , vol.9 , pp. 1-9
    • Ladokhin, A.S.1
  • 202
    • 0033537022 scopus 로고    scopus 로고
    • Role of ground state structure in photoinduced tautomerization in bifunctional proton donor-acceptor molecules: Pyrolloquinoline and related compounds
    • Kyrychenko A, Herbich J, Izydorzak, Wu F, Thummel Rp and Waluk J. Role of ground state structure in photoinduced tautomerization in bifunctional proton donor-acceptor molecules: pyrolloquinoline and related compounds. J. Am. Chem. Soc. 1999; 121: 11179-11188.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11179-11188
    • Kyrychenko, A.1    Herbich, J.2    Wu, F.3    Thummel, Rp.4    Waluk, J.5
  • 203
    • 0033295175 scopus 로고    scopus 로고
    • Dual fluorescence of 2-4′-dimethylaminophenyl-pyrido-imidazole: Effect of solvents
    • Krishnamoorthy G and Dogra SK. Dual fluorescence of 2-4′-dimethylaminophenyl-pyrido-imidazole: effect of solvents. Spectrochim. Acta A 1999; 55: 2647-2658.
    • (1999) Spectrochim. Acta A , vol.55 , pp. 2647-2658
    • Krishnamoorthy, G.1    Dogra, S.K.2
  • 204
    • 0032560468 scopus 로고    scopus 로고
    • A coupled proton-transfer and twisting-motion fluorescence probe for lipid bilayer
    • Mateo CR and Douhal A. A coupled proton-transfer and twisting-motion fluorescence probe for lipid bilayer. Proc. Natl Acad. Sci. USA 1998; 95: 7245-7250.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7245-7250
    • Mateo, C.R.1    Douhal, A.2
  • 205
    • 0030610813 scopus 로고    scopus 로고
    • 1Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins
    • 1Lb transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Emymol. 1997; 278: 113-150.
    • (1997) Methods Emymol. , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 206
    • 0000517116 scopus 로고    scopus 로고
    • Ab initio investigations on the photophysics of indole
    • Sobolewski AL and Domcke W. Ab initio investigations on the photophysics of indole. Chem. Phys. Lett. 1999; 315: 293-298.
    • (1999) Chem. Phys. Lett. , vol.315 , pp. 293-298
    • Sobolewski, A.L.1    Domcke, W.2
  • 207
    • 0020482353 scopus 로고
    • Decay-associated fluorescence spectra and the heterogeneous emission of alcohol dehydrogenase
    • Knutson JR, Walbridge DG and Brand L. Decay-associated fluorescence spectra and the heterogeneous emission of alcohol dehydrogenase. Biochemistry 1982; 21: 4671-4679.
    • (1982) Biochemistry , vol.21 , pp. 4671-4679
    • Knutson, J.R.1    Walbridge, D.G.2    Brand, L.3
  • 208
    • 0023044635 scopus 로고
    • Anisotropy decay associated fluorescence spectra and analysis of rotational heterogeneity. 1. Theory and applications
    • Knutson JR, Davenport L and Brand L. Anisotropy decay associated fluorescence spectra and analysis of rotational heterogeneity. 1. Theory and applications. Biochemistry 1986; 25: 1805-1810.
    • (1986) Biochemistry , vol.25 , pp. 1805-1810
    • Knutson, J.R.1    Davenport, L.2    Brand, L.3
  • 209
    • 0040022714 scopus 로고
    • Genetically inserted tryptophans in protein spectroscopy
    • Clark RJH, Hester RE (eds). Wiley: New York
    • Hart KW, Halsall DJ and Holbrook JJ. Genetically inserted tryptophans in protein spectroscopy. In Biomolecular Spectroscopy, Clark RJH, Hester RE (eds). Wiley: New York 1993; 195-229.
    • (1993) Biomolecular Spectroscopy , pp. 195-229
    • Hart, K.W.1    Halsall, D.J.2    Holbrook, J.J.3
  • 210
    • 0000861904 scopus 로고    scopus 로고
    • Spectrally and time-resolved fluorescence emission of indole during solvent relaxation: A quantitative model
    • Toptygin D and Brand L. Spectrally and time-resolved fluorescence emission of indole during solvent relaxation: a quantitative model. Chem. Phys. Lett. 2000; 322: 496-502.
    • (2000) Chem. Phys. Lett. , vol.322 , pp. 496-502
    • Toptygin, D.1    Brand, L.2
  • 212
    • 0035868855 scopus 로고    scopus 로고
    • Time-resolved area-normalized emission spectroscopy (TRANES): A novel method confirming emission from two states
    • Koti ASR, Krishna MMG and Periasamy N. Time-resolved area-normalized emission spectroscopy (TRANES): a novel method confirming emission from two states. J. Phys. Chem. A 2001; 105: 1767-1771.
    • (2001) J. Phys. Chem. A , vol.105 , pp. 1767-1771
    • Koti, A.S.R.1    Krishna, M.M.G.2    Periasamy, N.3
  • 214
    • 0033515831 scopus 로고    scopus 로고
    • Simple lessons from complexity
    • Goldenfeld N and Kadanoff LP. Simple lessons from complexity. Science 1999; 284: 87-89.
    • (1999) Science , vol.284 , pp. 87-89
    • Goldenfeld, N.1    Kadanoff, L.P.2
  • 216
    • 0031708076 scopus 로고    scopus 로고
    • The energy landscape in non-biological and biological molecules
    • Frauenfelder H and Leeson DT. The energy landscape in non-biological and biological molecules. Nature Struct. Biol. 1998; 5: 757-759.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 757-759
    • Frauenfelder, H.1    Leeson, D.T.2
  • 217
    • 0038467725 scopus 로고
    • Experimental study of non-exponential relaxation processes in random organic solids
    • Richert R, Elschner A and Bassler H. Experimental study of non-exponential relaxation processes in random organic solids. Z. Phys. Chem. Neue Folge 1986; 149: 63-75.
    • (1986) Z. Phys. Chem. Neue Folge , vol.149 , pp. 63-75
    • Richert, R.1    Elschner, A.2    Bassler, H.3
  • 218
    • 0026512374 scopus 로고
    • Heterogeneous distributions and dispersive photodissociation rates of benzo[a]pvrene diol-epoxide enantiomerDNA and -poly(dG-dC).Poly(dG-dC) adducts
    • Jankowiak R. Heterogeneous distributions and dispersive photodissociation rates of benzo[a]pvrene diol-epoxide enantiomerDNA and -poly(dG-dC).poly(dG-dC) adducts. Biophys. Chem. 1992: 42: 133-146.
    • (1992) Biophys. Chem. , vol.42 , pp. 133-146
    • Jankowiak, R.1
  • 219
    • 0028460836 scopus 로고
    • Kinetic studies concerning the decay of nitronic acids in polymer matrices using a data evaluation method based on dispersive kinetics
    • Feldmann G, Winsauer A, Pfleger J and Schnabel W. Kinetic studies concerning the decay of nitronic acids in polymer matrices using a data evaluation method based on dispersive kinetics. Macromolecules 1994; 27: 4391-4396.
    • (1994) Macromolecules , vol.27 , pp. 4391-4396
    • Feldmann, G.1    Winsauer, A.2    Pfleger, J.3    Schnabel, W.4
  • 220
    • 21344495023 scopus 로고
    • Dual phosphorescence from 2-(2′-hydroxyphenyl)benzoxazole in amorphous solid solution - Temperature dependence of dispersive kinetics of non-exponential triplet decay
    • Nickel B and Ruth AA. Dual phosphorescence from 2-(2′-hydroxyphenyl)benzoxazole in amorphous solid solution - temperature dependence of dispersive kinetics of non-exponential triplet decay. Chem. Phys. 1994; 184: 261-271.
    • (1994) Chem. Phys. , vol.184 , pp. 261-271
    • Nickel, B.1    Ruth, A.A.2
  • 221
    • 0026757571 scopus 로고
    • Does biocatalysis involve inhomogenous kinetics?
    • Demchenko AP. Does biocatalysis involve inhomogenous kinetics?. FEBS Lett. 1992; 310: 211-215.
    • (1992) FEBS Lett. , vol.310 , pp. 211-215
    • Demchenko, A.P.1
  • 222
    • 0025190014 scopus 로고
    • Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin. The connection between spectral and functional heterogeneity
    • Orrmos P, Ansari A and Braunstein D et al. Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin. The connection between spectral and functional heterogeneity. Biophys. J. 1990; 57: 191-199.
    • (1990) Biophys. J. , vol.57 , pp. 191-199
    • Orrmos, P.1    Ansari, A.2    Braunstein, D.3
  • 223
    • 0034650106 scopus 로고    scopus 로고
    • Stretched exponentials and barrier distributions
    • Edholm O and Blomberg C. Stretched exponentials and barrier distributions. Chem. Phys. 2000; 252: 221-225.
    • (2000) Chem. Phys. , vol.252 , pp. 221-225
    • Edholm, O.1    Blomberg, C.2
  • 224
    • 0003179683 scopus 로고    scopus 로고
    • Breaks in Arrhenius plots for enzyme reactions: The switches between different protein dynamics regimes?
    • Demchenko AP. Breaks in Arrhenius plots for enzyme reactions: the switches between different protein dynamics regimes?. Comments Mol. Cell Biophys. 1996; 9: 87-112.
    • (1996) Comments Mol. Cell Biophys. , vol.9 , pp. 87-112
    • Demchenko, A.P.1
  • 225
    • 0027371191 scopus 로고
    • Dynamics of protein relaxation in site-specific mutants of human myoglobin
    • Lambright DG, Balasubramanian S and Boxer SG. Dynamics of protein relaxation in site-specific mutants of human myoglobin. Biochemistry 1993; 32: 10116-10124.
    • (1993) Biochemistry , vol.32 , pp. 10116-10124
    • Lambright, D.G.1    Balasubramanian, S.2    Boxer, S.G.3
  • 226
    • 0024463170 scopus 로고
    • Kinetics of the lactate dehydrogenase reaction in high-viscosity media
    • Demchenko AP, Rusyn OI and Saburova EA. Kinetics of the lactate dehydrogenase reaction in high-viscosity media. Biochim. Biophys. Acta 1989; 998: 196-203.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 196-203
    • Demchenko, A.P.1    Rusyn, O.I.2    Saburova, E.A.3
  • 227
    • 0028997570 scopus 로고
    • 2+)-HisF8 linkage in deoxymyoglobin probed by the Raman active Fe-N epsilon (HisF8) stretching vibration
    • 2+)-HisF8 linkage in deoxymyoglobin probed by the Raman active Fe-N epsilon (HisF8) stretching vibration. Biophys. J. 1995; 69: 214-227.
    • (1995) Biophys. J. , vol.69 , pp. 214-227
    • Gilch, H.1    Dreybrodt, W.2    Schweitzer-Stenner, R.3
  • 228
    • 11644297580 scopus 로고    scopus 로고
    • Anomalous dielectric relaxation of aqueous protein solutions
    • Nandi N and Bagchi B. Anomalous dielectric relaxation of aqueous protein solutions. J. Phys. Chem. A 1998; 102: 8217-8221.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 8217-8221
    • Nandi, N.1    Bagchi, B.2
  • 229
    • 0034682520 scopus 로고    scopus 로고
    • Memory landscapes of single-enzyme molecules
    • Edman L and Rigler R. Memory landscapes of single-enzyme molecules. Proc. Natl Acad. Sci. USA 2000; 97: 8266-8271.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8266-8271
    • Edman, L.1    Rigler, R.2
  • 230
    • 0033613185 scopus 로고    scopus 로고
    • Hierarchies and logarithmic oscillations in the temporal relaxation patterns of proteins and other complex systems
    • Metzler R, Klafter J and Jortner J. Hierarchies and logarithmic oscillations in the temporal relaxation patterns of proteins and other complex systems. Proc. Natl Acad. Sci. USA 1999; 96: 11085-11089.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11085-11089
    • Metzler, R.1    Klafter, J.2    Jortner, J.3
  • 231
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenko AP. Recognition between flexible protein molecules: induced and assisted folding. J. Mol. Recogn. 2001; 14: 42-61.
    • (2001) J. Mol. Recogn. , vol.14 , pp. 42-61
    • Demchenko, A.P.1
  • 232
    • 0035033781 scopus 로고    scopus 로고
    • Concepts and misconcepts in the science of protein folding
    • Demchenko AP. Concepts and misconcepts in the science of protein folding. Curr. Prot. Peptide Sci. 2001; 2: 73-98.
    • (2001) Curr. Prot. Peptide Sci. , vol.2 , pp. 73-98
    • Demchenko, A.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.