메뉴 건너뛰기




Volumn 111, Issue 2, 2004, Pages 105-113

Influence of alkyl group on amide nitrogen atom on fluorescence quenching of tyrosine amide and N-acetyltyrosine amide

Author keywords

Flourescence; Rotamers; Tyrosine

Indexed keywords

AMIDE; N ACETYLTYROSINAMIDE; NITROGEN; PHENOL; TYROSINAMIDE; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 4644264946     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.05.002     Document Type: Article
Times cited : (12)

References (32)
  • 1
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem J.M., Brand L. Time-resolved fluorescence of proteins. Ann. Rev. Biochem. 54:1985;43-71
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 4
    • 0022774512 scopus 로고
    • Linked-function analysis of fluorescence decay kinetics: Resolution of side-chain rotamer populations of a single aromatic amino acid in small polypeptides
    • Ross J.B.A., Laws W.R., Sutherl J.C., Buku A., Katsoyannis P.G., Schwartz I.L., Wyssbrod H.R. Linked-function analysis of fluorescence decay kinetics: resolution of side-chain rotamer populations of a single aromatic amino acid in small polypeptides. Photochem. Photobiol. 44:1986;365-370
    • (1986) Photochem. Photobiol. , vol.44 , pp. 365-370
    • Ross, J.B.A.1    Laws, W.R.2    Sutherl, 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., Whal P. Pulse fluorimetry of tyrosyl peptides. Biophys. Chem. 8:1978;87-104
    • (1978) Biophys. Chem. , vol.8 , pp. 87-104
    • Gauduchon, P.1    Whal, 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., Rzeska A., Malicka J., Wiczk W. Influence of substituent on amide nitrogen atom on fluorescence efficiency quenching of Tyr(Me) by amide group. J. Photochem. Photobiol., A Chem. 142:2001;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. On the mechanism of fluorescence quenching. Tyrosine and similar compounds. J. Phys. Chem. 68:1964;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., Ganzynkowicz R., Rzeska A., Mrozek J., Szabelski M., Karolczak J., Liwo A., Wiczk W. Photophysical properties of tyrosine and its simple derivatives studied by time-resolved fluorescence spectroscopy, global analysis and theoretical calculations. J. Phys. Chem. B. 108:2004;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., Laczko G., Gryczynski I. Picosecond resolution of tyrosine fluorescence and anisotropy decays by 2 Ghz frequency-domain fluorometry. Biochemistry. 26:1987;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., Paulus S.W., Hendstrom J.F., Johnson C.K. Tyrosyl fluorescence decays and rotational dynamics in tyrosine monomers and in peptides. J. Fluoresc. 7:1997;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 spectroscopy of tyrosine and related compounds
    • Pal H., Palit D.K., Mukherjee D., Mittal J.P. Some aspect of steady state and time resolved fluorescence spectroscopy of tyrosine and related compounds. J. Photochem. Photobiol., A Chem. 523:1990;391-409
    • (1990) J. Photochem. Photobiol., a Chem. , vol.523 , pp. 391-409
    • Pal, H.1    Palit, D.K.2    Mukherjee, D.3    Mittal, J.P.4
  • 19
    • 0015231805 scopus 로고
    • Variation avec le pH du rendement quantique et du déclin de la fluorescence de la tyrosine
    • Fayet M., Whal P. Variation avec le pH du rendement quantique et du déclin de la fluorescence de la tyrosine. Biochim. Biophys. Acta. 229:1971;102-112
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 102-112
    • Fayet, M.1    Whal, P.2
  • 20
    • 0000866947 scopus 로고
    • Excited-state acid-base equilibrium of tyrosine
    • Rayner D.M., Krajcarski D.T., Szabo A.G. Excited-state acid-base equilibrium of tyrosine. Can. J. Chem. 56:1977;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., Szabo A.G. Fluorescence decay kinetics of tyrosinate and tyrosine hydrogen-bonded complexes. J. Phys. Chem. 95:1991;1585-1589
    • (1991) J . Phys. Chem. , vol.95 , pp. 1585-1589
    • Willis, J.K.1    Szabo, A.G.2
  • 22
    • 0001801596 scopus 로고
    • Rotamer-specific fluorescence quenching in tyrosineamide: Dynamic and static interactions
    • Contino P.B., Laws W.R. Rotamer-specific fluorescence quenching in tyrosineamide: dynamic and static interactions. J. Fluoresc. 1:1991;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., Guzow K., Rzeska A., Malicka J., Przyborowska M., Wiczk W. Acidity of carboxyl group of tyrosine and its analogues and derivatives studied by steady-state fluorescence spectroscopy. J. Photochem. Photobiol., A Chem. 152:2002;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., Orth A., Greulich K.O. Electronic effects on the fluorescence of tyrosine in small peptides. Photochem. Photobiol. 58:1990;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., Fonda M., Crane-Robinson C. Tyrosine fluorescence of two tryptophan-free proteins: histones H1 and H5. Biophys. Chem. 6:1977;379-383
    • (1977) Biophys. Chem. , vol.6 , pp. 379-383
    • Giancotti, V.1    Fonda, M.2    Crane-Robinson, C.3
  • 26
    • 0014209817 scopus 로고
    • Fluorescence and protein structure: X. Reappraisal of solvent and structural effects
    • Cowgill R.W. Fluorescence and protein structure: X. Reappraisal of solvent and structural effects. Biochim. Biophys. Acta. 133:1967;6-18
    • (1967) Biochim. Biophys. Acta , vol.133 , pp. 6-18
    • Cowgill, R.W.1
  • 27
    • 4644361550 scopus 로고
    • Fluorescence and the structure of protein: I. Effects of substituents on the fluorescence of indole and phenol compounds
    • Cowgill R.W. Fluorescence and the structure of protein: I. Effects of substituents on the fluorescence of indole and phenol compounds. Arch. Biochem. Biophys. 100:1963;3644
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 3644
    • Cowgill, R.W.1
  • 28
    • 0015432277 scopus 로고
    • Fluorescence quenching in phenylalanine and model compounds
    • Tournon J.E., Kuntz E., El-Bayoumi M.A. Fluorescence quenching in phenylalanine and model compounds. Photochem. Photobiol. 16:1972;425-433
    • (1972) Photochem. Photobiol. , vol.16 , pp. 425-433
    • Tournon, J.E.1    Kuntz, E.2    El-Bayoumi, M.A.3
  • 29
    • 84945799762 scopus 로고
    • Fluorescence quantum yields of tryptophan and tyrosine
    • Chen R.F. Fluorescence quantum yields of tryptophan and tyrosine. Anal. Lett. 1:1967;35-42
    • (1967) Anal. Lett. , vol.1 , pp. 35-42
    • Chen, R.F.1
  • 31
    • 0019553521 scopus 로고
    • Nuclear magnetic resonance study on solvent dependence of side chain conformations of tyrosine and tryptophan derivatives
    • Kobayashi J., Higashijima T., Sekido S., Miyazawa T. Nuclear magnetic resonance study on solvent dependence of side chain conformations of tyrosine and tryptophan derivatives. Int. J. Protein Res. 17:1981;486-494
    • (1981) Int. J. Protein Res. , vol.17 , pp. 486-494
    • Kobayashi, J.1    Higashijima, T.2    Sekido, S.3    Miyazawa, T.4
  • 32
    • 0018180320 scopus 로고
    • A solvent effect on the side-chain conformation of phenylalanine derivatives and phenylalanine residues in peptides
    • Kobayashi J., Nagai U. A solvent effect on the side-chain conformation of phenylalanine derivatives and phenylalanine residues in peptides. Biopolymers. 17:1978;2265-2277
    • (1978) Biopolymers , vol.17 , pp. 2265-2277
    • Kobayashi, J.1    Nagai, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.