메뉴 건너뛰기




Volumn 81, Issue 3, 2005, Pages 697-704

Photophysical properties of tyrosine and its simple derivatives in organic solvents studied by time-resolved fluorescence spectroscopy and global analysis

Author keywords

[No Author keywords available]

Indexed keywords


EID: 21244478246     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2004-03-02-RA-095.1     Document Type: Conference Paper
Times cited : (7)

References (64)
  • 1
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem, J. M. and L. Brand (1985) Time-resolved fluorescence of proteins. Ann. Rev. Biochem. 54, 43-71.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 2
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Protein Structure Determination (Edited by C. H. Schulter), J. Wiley and Sons
    • Eftink, M. R. (1991) Fluorescence techniques for studying protein structure. In Methods in Biochemical Analysis, Vol. 35, Protein Structure Determination (Edited by C. H. Schulter), J. Wiley and Sons, pp. 127-205.
    • (1991) Methods in Biochemical Analysis , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 3
    • 0002482325 scopus 로고
    • Tyrosine fluorescence and phosphorescence from proteins and peptides
    • Biochemical Applications (Edited by J. R. Lakowicz), Plenum Press, New York
    • Ross, J. B. A., W. R. Laws, K. W. Rousslang and H. R. Wyssbrod (1992) Tyrosine fluorescence and phosphorescence from proteins and peptides. In Topics in Fluorescence Spectroscopy, Vol. 3, Biochemical Applications (Edited by J. R. Lakowicz), Plenum Press, New York, pp. 1-53.
    • (1992) Topics in Fluorescence Spectroscopy , vol.3 , pp. 1-53
    • Ross, J.B.A.1    Laws, W.R.2    Rousslang, K.W.3    Wyssbrod, H.R.4
  • 4
    • 0022774512 scopus 로고
    • Linkedfunction analysis of fluorescence decay kinetics: Resolution of sidechain rotamer populations of a single aromatic amino acid in small polypeptides
    • Ross, J. B. A., W. R. Laws, J. C. Sutherland, A. Buku, P. G. Katsoyannis, I. L. Schwartz and H. R. Wyssbrod (1986) Linkedfunction analysis of fluorescence decay kinetics: resolution of sidechain rotamer populations of a single aromatic amino acid in small polypeptides. Photochem. Photobiol. 44, 365-370.
    • (1986) Photochem. Photobiol. , vol.44 , pp. 365-370
    • Ross, J.B.A.1    Laws, W.R.2    Sutherland, J.C.3    Buku, A.4    Katsoyannis, P.G.5    Schwartz, I.L.6    Wyssbrod, H.R.7
  • 6
    • 0017876975 scopus 로고
    • Pulse fluorimetry of tyrosyl peptides
    • Gauduchon, P. and P. Wahl (1978) Pulse fluorimetry of tyrosyl peptides. Biophys. Chem. 8, 87-104.
    • (1978) Biophys. Chem. , vol.8 , pp. 87-104
    • Gauduchon, P.1    Wahl, P.2
  • 9
    • 0000594506 scopus 로고    scopus 로고
    • Influence of substituent on amide nitrogen atom on fluorescence efficiency quenching of Tyr(Me) by amide group
    • Lukomska, J., A. Rzeska, J. Malicka and W. Wiczk (2001) Influence of substituent on amide nitrogen atom on fluorescence efficiency quenching of Tyr(Me) by amide group. J. Photochem. Photobiol., A: Chem. 142, 135-139.
    • (2001) J. Photochem. Photobiol., A: Chem. , vol.142 , pp. 135-139
    • Lukomska, J.1    Rzeska, A.2    Malicka, J.3    Wiczk, W.4
  • 10
    • 0001701340 scopus 로고
    • On the mechanism of fluorescence quenching. Tyrosine and similar compounds
    • Feitelson, J. (1964) On the mechanism of fluorescence quenching. Tyrosine and similar compounds. J. Phys. Chem. 68, 391-397.
    • (1964) J. Phys. Chem. , vol.68 , pp. 391-397
    • Feitelson, J.1
  • 15
    • 1842687496 scopus 로고    scopus 로고
    • Photophysical properties of tyrosine and its simple derivatives studied by time-resolved fluorescence spectroscopy, global analysis and theoretical calculations
    • Guzow, K., R. Ganzynkowicz, A. Rzeska, J. Mrozek, M. Szabelski, J. Karolczak, A. Liwo and W. Wiczk (2004) Photophysical properties of tyrosine and its simple derivatives studied by time-resolved fluorescence spectroscopy, global analysis and theoretical calculations. J. Phys. Chem. B 108, 3879-3889.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3879-3889
    • Guzow, K.1    Ganzynkowicz, R.2    Rzeska, A.3    Mrozek, J.4    Szabelski, M.5    Karolczak, J.6    Liwo, A.7    Wiczk, W.8
  • 16
    • 0023652246 scopus 로고
    • Picosecond resolution of tyrosine fluorescence and anisotropy decays by 2 GHz frequency-domain fluorometry
    • Lakowicz, J. R., G. Laczko and I. Gryczynski (1987) Picosecond resolution of tyrosine fluorescence and anisotropy decays by 2 GHz frequency-domain fluorometry. Biochemistry 26, 82-90.
    • (1987) Biochemistry , vol.26 , pp. 82-90
    • Lakowicz, J.R.1    Laczko, G.2    Gryczynski, I.3
  • 17
    • 0038808798 scopus 로고    scopus 로고
    • Tyrosyl fluorescence decays and rotational dynamics in tyrosine monomers and in peptides
    • Harms, G. S., S. W. Paulus, J. F. Hendstrom and C. K. Johnson (1997) Tyrosyl fluorescence decays and rotational dynamics in tyrosine monomers and in peptides. J. Fluoresc. 7, 273-282.
    • (1997) J. Fluoresc. , vol.7 , pp. 273-282
    • Harms, G.S.1    Paulus, S.W.2    Hendstrom, J.F.3    Johnson, C.K.4
  • 18
    • 0000544692 scopus 로고
    • Some aspect of steady state and time resolved fluorescence of tyrosine and related compounds
    • Pal, H., D. K. Palit, D. Mukherjee and J. P. Mittal (1990) Some aspect of steady state and time resolved fluorescence of tyrosine and related compounds. J. Photochem. Photobiol., A: Chem. 52, 391-409.
    • (1990) J. Photochem. Photobiol., A: Chem. , vol.52 , pp. 391-409
    • Pal, H.1    Palit, D.K.2    Mukherjee, D.3    Mittal, J.P.4
  • 19
    • 21244482310 scopus 로고
    • Variation avec le pH du rendement quantique et du déclin de la fluorescence de la tyrosine
    • Fayet, M. and P. Wahl (1971) Variation avec le pH du rendement quantique et du déclin de la fluorescence de la tyrosine. Biochim. Biophys. Acta 229, 192-212.
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 192-212
    • Fayet, M.1    Wahl, P.2
  • 20
    • 0000866947 scopus 로고
    • Excited-state acid-base equilibrium of tyrosine
    • Rayner, D. M., D. T. Krajcarski and A. G. Szabo (1977) Excited-state acid-base equilibrium of tyrosine. Can. J. Chem. 56, 1238-1245.
    • (1977) Can. J. Chem. , vol.56 , pp. 1238-1245
    • Rayner, D.M.1    Krajcarski, D.T.2    Szabo, A.G.3
  • 21
    • 0001253507 scopus 로고
    • Fluorescence decay kinetics of tyrosinate and tyrosine hydrogen-bonded complexes
    • Willis, J. K. and A. G. Szabo (1991) Fluorescence decay kinetics of tyrosinate and tyrosine hydrogen-bonded complexes. J. Phys. Chem. 95, 1585-1589.
    • (1991) J. Phys. Chem. , vol.95 , pp. 1585-1589
    • Willis, J.K.1    Szabo, A.G.2
  • 22
    • 0001801596 scopus 로고
    • Retainer-specific fluorescence quenching in tyrosineamide: Dynamic and static interactions
    • Contino, P. B. and W. R. Laws (1991) Retainer-specific fluorescence quenching in tyrosineamide: dynamic and static interactions. J. Fluoresc. 1, 5-13.
    • (1991) J. Fluoresc. , vol.1 , pp. 5-13
    • Contino, P.B.1    Laws, W.R.2
  • 23
    • 0037144757 scopus 로고    scopus 로고
    • Acidity of carboxyl group of tyrosine and its analogues and derivatives studied by steady-state fluorescence spectroscopy
    • Szabelski, M., K. Guzow, A. Rzeska, J. Malicka, M. Przyborowska and W. Wiczk (2002) Acidity of carboxyl group of tyrosine and its analogues and derivatives studied by steady-state fluorescence spectroscopy. J. Photochem. Photobiol., A:Chem. 152, 73-78.
    • (2002) J. Photochem. Photobiol., A:Chem. , vol.152 , pp. 73-78
    • Szabelski, M.1    Guzow, K.2    Rzeska, A.3    Malicka, J.4    Przyborowska, M.5    Wiczk, W.6
  • 24
    • 0027651401 scopus 로고
    • Electronic effects on the fluorescence of tyrosine in small peptides
    • Seidel, C., A. Orth and K. O. Greulich (1990) Electronic effects on the fluorescence of tyrosine in small peptides. Photochem. Photobiol. 58, 178-184.
    • (1990) Photochem. Photobiol. , vol.58 , pp. 178-184
    • Seidel, C.1    Orth, A.2    Greulich, K.O.3
  • 25
    • 0017407836 scopus 로고
    • Tyrosine fluorescence of two tryptophan-free proteins: Histones H1 and H5
    • Giancotti, V., M. Fonda and C. Crane-Robinson (1977) Tyrosine fluorescence of two tryptophan-free proteins: histones H1 and H5. Biophys. Chem. 6, 379-383.
    • (1977) Biophys. Chem. , vol.6 , pp. 379-383
    • Giancotti, V.1    Fonda, M.2    Crane-Robinson, C.3
  • 27
    • 0001581707 scopus 로고
    • Time resolved fluorescence of aqueous tryptophan
    • Rayner, D. M. and A. G. Szabo (1977) Time resolved fluorescence of aqueous tryptophan. Can. J. Chem. 56, 743-745.
    • (1977) Can. J. Chem. , vol.56 , pp. 743-745
    • Rayner, D.M.1    Szabo, A.G.2
  • 28
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo, A. G. and D. M. Rayner (1980) Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102, 554-563.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 29
    • 0001225219 scopus 로고
    • Conformational dynamics of tryptophan: A proposal for the origin of the nonexponential fluorescence decay
    • Engh, R. A., L. X.-Q. Chen and G. R. Fleming (1986) Conformational dynamics of tryptophan: a proposal for the origin of the nonexponential fluorescence decay. Chem. Phys. Lett. 126, 365-372.
    • (1986) Chem. Phys. Lett. , vol.126 , pp. 365-372
    • Engh, R.A.1    Chen, L.X.-Q.2    Fleming, G.R.3
  • 30
    • 0001116890 scopus 로고
    • Molecular dynamics simulations of the conformational dynamics of tryptophan
    • Gordon, H. R., H. C. Jarrell, A. G. Szabo, K. J. Willis and R. L. Somorjai (1992) Molecular dynamics simulations of the conformational dynamics of tryptophan. J. Phys. Chem. 96, 1915-1921.
    • (1992) J. Phys. Chem. , vol.96 , pp. 1915-1921
    • Gordon, H.R.1    Jarrell, H.C.2    Szabo, A.G.3    Willis, K.J.4    Somorjai, R.L.5
  • 31
    • 0014209817 scopus 로고
    • Fluorescence and protein structure X. Reappraisal of solvent and structural effects
    • Cowgill, R. W. (1967) Fluorescence and protein structure X. Reappraisal of solvent and structural effects. Biochim. Biophys. Acta 133, 6-18.
    • (1967) Biochim. Biophys. Acta , vol.133 , pp. 6-18
    • Cowgill, R.W.1
  • 32
    • 4644361550 scopus 로고
    • Fluorescence and the structure of protein I. Effects of substituents on the fluorescence of indole and phenol compounds
    • Cowgill, R. W. (1963) Fluorescence and the structure of protein I. Effects of substituents on the fluorescence of indole and phenol compounds. Arch. Biochem. Biophys. 100, 36-44.
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 36-44
    • Cowgill, R.W.1
  • 33
    • 0015432277 scopus 로고
    • Fluorescence quenching in phenylalanine and model compounds
    • Tournon, J. E., E. Kuntz and M. A. El Bayoumi (1972) Fluorescence quenching in phenylalanine and model compounds. Photochem. Photobiol. 16, 425-433.
    • (1972) Photochem. Photobiol. , vol.16 , pp. 425-433
    • Tournon, J.E.1    Kuntz, E.2    El Bayoumi, M.A.3
  • 35
    • 33947313965 scopus 로고
    • Solvent effects on aromatic chromophores and their relation to ultraviolet difference spectra of proteins
    • Chingell, D. A. and W. B. Gratzer (1968) Solvent effects on aromatic chromophores and their relation to ultraviolet difference spectra of proteins. J. Phys. Chem. 72, 2934-2941.
    • (1968) J. Phys. Chem. , vol.72 , pp. 2934-2941
    • Chingell, D.A.1    Gratzer, W.B.2
  • 36
    • 0014936646 scopus 로고
    • Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of tyrosine derivatives and ribonuclease-A at 77 K
    • Horwitz, J., E. H. Strickland and C. Billups (1970) Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of tyrosine derivatives and ribonuclease-A at 77 K. J. Am. Chem. Soc. 92, 2119-2129.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 2119-2129
    • Horwitz, J.1    Strickland, E.H.2    Billups, C.3
  • 37
    • 84981760198 scopus 로고
    • An analysis of perturbations in the ultraviolet absorption spectra of proteins and model compounds
    • Bailey, J. E., G. H. Beaven, D. A. Chignell and W. B. Gratzer (1968) An analysis of perturbations in the ultraviolet absorption spectra of proteins and model compounds. Eur. J. Biochim. 7, 8-14.
    • (1968) Eur. J. Biochim. , vol.7 , pp. 8-14
    • Bailey, J.E.1    Beaven, G.H.2    Chignell, D.A.3    Gratzer, W.B.4
  • 38
    • 0013038994 scopus 로고
    • Optical rotatory power in the ground state and electronically excited state of diketopiperazines containing aromatic side chains
    • Schlessinger, J., A. Gafni and I. Z. Steinberg (1974) Optical rotatory power in the ground state and electronically excited state of diketopiperazines containing aromatic side chains. J. Am. Chem. Soc. 96, 7396-7400.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 7396-7400
    • Schlessinger, J.1    Gafni, A.2    Steinberg, I.Z.3
  • 39
    • 0014962538 scopus 로고
    • Low temperature circular dichroism of tyrosyl and tryptophanyl diketopiperazines
    • Strickland, E. H., M. Wilchek, J. Horwitz and C. Billups (1970) Low temperature circular dichroism of tyrosyl and tryptophanyl diketopiperazines. J. Biol. Chem. 245, 4168-4177.
    • (1970) J. Biol. Chem. , vol.245 , pp. 4168-4177
    • Strickland, E.H.1    Wilchek, M.2    Horwitz, J.3    Billups, C.4
  • 40
    • 0345265151 scopus 로고    scopus 로고
    • Chiroptical properties of the benzene chromophores. A method for the determination of the absolute configurations of benzene compounds by application of the benzene sector and benzene chirality rules
    • Smith, H. E. (1998) Chiroptical properties of the benzene chromophores. A method for the determination of the absolute configurations of benzene compounds by application of the benzene sector and benzene chirality rules. Chem. Rev. 98, 1709-1740.
    • (1998) Chem. Rev. , vol.98 , pp. 1709-1740
    • Smith, H.E.1
  • 41
    • 0014516559 scopus 로고
    • Environmental effects on the fluorescence of tyrosine and its homologues
    • Feitelson, J. (1969) Environmental effects on the fluorescence of tyrosine and its homologues. Photochem. Photobiol. 9, 401-410.
    • (1969) Photochem. Photobiol. , vol.9 , pp. 401-410
    • Feitelson, J.1
  • 42
    • 0017020544 scopus 로고
    • The effect of mixed aqueous solvent systems on the fluorescence of indoles and aromatic amino acids and their metabolites
    • Froehlich, P. M. and M. Yeats (1976) The effect of mixed aqueous solvent systems on the fluorescence of indoles and aromatic amino acids and their metabolites. Anal. Chim. Acta 87, 185-189.
    • (1976) Anal. Chim. Acta , vol.87 , pp. 185-189
    • Froehlich, P.M.1    Yeats, M.2
  • 45
    • 84945799762 scopus 로고
    • Fluorescence quantum yields of tryptophan and tyrosine
    • Chen, R. F. (1967) Fluorescence quantum yields of tryptophan and tyrosine. Anal. Lett. 1, 35-42.
    • (1967) Anal. Lett. , vol.1 , pp. 35-42
    • Chen, R.F.1
  • 47
    • 0000060559 scopus 로고
    • Simultaneous analysis of multiple fluorescence decay curves: A global approach
    • Knutson, R. J., J. M. Bechem and L. Brand (1983) Simultaneous analysis of multiple fluorescence decay curves: a global approach. Chem. Phys. Lett. 102, 501-507.
    • (1983) Chem. Phys. Lett. , vol.102 , pp. 501-507
    • Knutson, R.J.1    Bechem, J.M.2    Brand, L.3
  • 48
    • 0000335117 scopus 로고
    • The global analysis of fluorescence intensity and anisotropy decay data: Second-generation theory and programs
    • Principles (Edited by J. R. Lakowicz). Plenum Press, New York
    • Beechem, J. M., E. Gratton, M. Ameloot, R. J. Knutson and L. Brand (1991) The global analysis of fluorescence intensity and anisotropy decay data: second-generation theory and programs. In Topics in Fluorescence Spectroscopy, Vol 2; Principles (Edited by J. R. Lakowicz), pp. 241-305. Plenum Press, New York.
    • (1991) Topics in Fluorescence Spectroscopy , vol.2 , pp. 241-305
    • Beechem, J.M.1    Gratton, E.2    Ameloot, M.3    Knutson, R.J.4    Brand, L.5
  • 49
    • 0020482353 scopus 로고
    • Decay associated spectra and the heterogeneous emission of alcohol dehydrogenase
    • Knutson, R. J., D. G. Waldbridge and L. Brand (1982) Decay associated spectra and the heterogeneous emission of alcohol dehydrogenase. Biochemistry 21, 4671-4619.
    • (1982) Biochemistry , vol.21 , pp. 4671-14619
    • Knutson, R.J.1    Waldbridge, D.G.2    Brand, L.3
  • 50
    • 0025190991 scopus 로고
    • Resolution of heterogeneous fluorescence into component decay-associated excitation spectra
    • Willis, K. J., A. G. Szabo, J. Drew, M. Zuker and J. M. Ridgewey (1990) Resolution of heterogeneous fluorescence into component decay-associated excitation spectra. Biophys. J. 57, 183-189.
    • (1990) Biophys. J. , vol.57 , pp. 183-189
    • Willis, K.J.1    Szabo, A.G.2    Drew, J.3    Zuker, M.4    Ridgewey, J.M.5
  • 51
    • 0000841686 scopus 로고    scopus 로고
    • Absorption and fluorescence of tyrosine hydrogen-bonded to amide-like ligands
    • Lee, J. K. and R. T. Ross (1998) Absorption and fluorescence of tyrosine hydrogen-bonded to amide-like ligands. J. Phys. Chem. B 102, 4612-4618.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 4612-4618
    • Lee, J.K.1    Ross, R.T.2
  • 52
    • 36449006885 scopus 로고
    • Combined neutron diffraction and computer simulation study of liquid dimethyl sulfoxide
    • A. Lazur, A. K. Soper and D. Chandler (1993) Combined neutron diffraction and computer simulation study of liquid dimethyl sulfoxide. J. Chem. Phys. 99, 6836-6847.
    • (1993) J. Chem. Phys. , vol.99 , pp. 6836-6847
    • Lazur, A.1    Soper, A.K.2    Chandler, D.3
  • 53
    • 0037075407 scopus 로고    scopus 로고
    • A flexible all-atom model of dimethyl sulfoxide for molecular dynamics simulation
    • Strader, M. L. and S. E. Feller (2002) A flexible all-atom model of dimethyl sulfoxide for molecular dynamics simulation. J. Phys. Chem. A 106, 1074-1080.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 1074-1080
    • Strader, M.L.1    Feller, S.E.2
  • 55
    • 0028327178 scopus 로고
    • Conformational dynamic of bovine Cu, Zn Superoxide dismutase revealed by time-resolved fluorescence spectroscopy of the single tyrosine residue
    • Ferreira, S. T., L. Stella and E. Gratton (1994) Conformational dynamic of bovine Cu, Zn Superoxide dismutase revealed by time-resolved fluorescence spectroscopy of the single tyrosine residue. Biophys. J. 66, 1185-1196.
    • (1994) Biophys. J. , vol.66 , pp. 1185-1196
    • Ferreira, S.T.1    Stella, L.2    Gratton, E.3
  • 56
    • 0033084091 scopus 로고    scopus 로고
    • Conformational landscapes in flexible organic molecules: 4-hydroxy phenyl ethanol (p-tyrosol) and its singly hydrated complex
    • Hockridge, M. R., S. M. Knight, E. G. Robertson, J. P. Simons, J. McCombir and M. Walker (1999) Conformational landscapes in flexible organic molecules: 4-hydroxy phenyl ethanol (p-tyrosol) and its singly hydrated complex. Phys. Chem. Chem. Phys. 1, 407-413.
    • (1999) Phys. Chem. Chem. Phys. , vol.1 , pp. 407-413
    • Hockridge, M.R.1    Knight, S.M.2    Robertson, E.G.3    Simons, J.P.4    McCombir, J.5    Walker, M.6
  • 57
    • 21244499513 scopus 로고
    • Proton magnetic resonance spectra of amino-acids and peptides relevant to wool structure. Part IV. Relative residence times of dipeptides and tripeptides of phenylalanine and tyrosine
    • Dale, B. J. and D. W. Jones (1976) Proton magnetic resonance spectra of amino-acids and peptides relevant to wool structure. Part IV. Relative residence times of dipeptides and tripeptides of phenylalanine and tyrosine. J. Chem. Soc. Perkin Trans. II 1976, 91-96.
    • (1976) J. Chem. Soc. Perkin Trans. II , vol.1976 , pp. 91-96
    • Dale, B.J.1    Jones, D.W.2
  • 59
    • 0019553521 scopus 로고
    • Nuclear magnetic resonance study on solvent dependence of side-chain conformations of tyrosine and tryptophan derivatives
    • Kobayashi, J., T. Higashijama, S. Sekido and T. Miyazawa (1981) Nuclear magnetic resonance study on solvent dependence of side-chain conformations of tyrosine and tryptophan derivatives. Int. J. Protein Res. 17, 486-494.
    • (1981) Int. J. Protein Res. , vol.17 , pp. 486-494
    • Kobayashi, J.1    Higashijama, T.2    Sekido, S.3    Miyazawa, T.4
  • 60
    • 1642300619 scopus 로고
    • A nitrogen-14 magnetic resonance study of amino-acids, peptides, and other biologically interesting molecules
    • Richards, R. and N. A. Thomas (1974) A nitrogen-14 magnetic resonance study of amino-acids, peptides, and other biologically interesting molecules. J. Chem. Soc. Perkin II 1974, 368-374.
    • (1974) J. Chem. Soc. Perkin II , vol.1974 , pp. 368-374
    • Richards, R.1    Thomas, N.A.2
  • 61
    • 84970572066 scopus 로고
    • A luminescent probe study of water/acetonitrile mixtures
    • Easeal, A. J. (1979) A luminescent probe study of water/acetonitrile mixtures, Aust. J. Chem. 32, 271-275.
    • (1979) Aust. J. Chem. , vol.32 , pp. 271-275
    • Easeal, A.J.1
  • 62
    • 2542457898 scopus 로고
    • Preferential solvation in acetonitrile-water mixtures. Relationship between solvatochromic parameters and standard pH values
    • Barbosa, J. and V. Sanz-Nebot (1994) Preferential solvation in acetonitrile-water mixtures. Relationship between solvatochromic parameters and standard pH values. J. Chem. Faraday Trans. 90, 3287-3292.
    • (1994) J. Chem. Faraday Trans. , vol.90 , pp. 3287-3292
    • Barbosa, J.1    Sanz-Nebot, V.2
  • 63
    • 0030782254 scopus 로고    scopus 로고
    • Solvent effect on protonation equilibria of peptides and quinolones by factor analysis applied to the correlation between dissociation constants and solvatochromic parameters in acetonitrilewater mixtures
    • Barbosa, J., G. Fonrodona, I. Marques, V. Sanz-Nebot and I. Toro (1997) Solvent effect on protonation equilibria of peptides and quinolones by factor analysis applied to the correlation between dissociation constants and solvatochromic parameters in acetonitrilewater mixtures. Anal. Chim. Acta 351, 397-405.
    • (1997) Anal. Chim. Acta , vol.351 , pp. 397-405
    • Barbosa, J.1    Fonrodona, G.2    Marques, I.3    Sanz-Nebot, V.4    Toro, I.5
  • 64
    • 0011281436 scopus 로고
    • Thermodynamics in solvent mixtures. 1. A simple deviation function for summarizing thermodynamic data in mixed solvents
    • Hogfeldt, E. (1981) Thermodynamics in solvent mixtures. 1. A simple deviation function for summarizing thermodynamic data in mixed solvents. Acta Chim. Scand. A 35, 383-388.
    • (1981) Acta Chim. Scand. A , vol.35 , pp. 383-388
    • Hogfeldt, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.