메뉴 건너뛰기




Volumn 4626, Issue , 2002, Pages 493-501

Biochemical diagnostics by excited state absorption spectroscopy

Author keywords

Electron Transfer; ESA; Excited State Spectroscopy; Fluorescein Isothiocyanate; Fluorescent Probes; Laser Spectroscopy; Myoglobin; Protein Conformation; Transient Spectra

Indexed keywords

ABSORPTION SPECTROSCOPY; AROMATIC COMPOUNDS; BIOCHEMISTRY; BIOSENSORS; ELECTRON TRANSITIONS; FLUORESCENCE;

EID: 0036406720     PISSN: 0277786X     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1117/12.472116     Document Type: Conference Paper
Times cited : (3)

References (34)
  • 1
    • 0034383950 scopus 로고    scopus 로고
    • Protein folding: Progress made and promises ahead
    • S. Radford, "Protein folding: progress made and promises ahead", Trends Biochem. Sci. 25, pp. 611-618, 2000.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 611-618
    • Radford, S.1
  • 2
    • 0032011350 scopus 로고    scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • M.R. Eftink, "The use of fluorescence methods to monitor unfolding transitions in proteins" Biochemistry (Moscow) 63, pp. 276-284, 1998.
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 276-284
    • Eftink, M.R.1
  • 3
    • 0028290491 scopus 로고
    • Use of nonradiative decays of extrinsic fluorophores as structural and dynamic probes in protein environments: Fluorescence quenching
    • C. Viappiani, "Use of nonradiative decays of extrinsic fluorophores as structural and dynamic probes in protein environments: fluorescence quenching", Biophys. Chem. 50, pp. 293-304, 1994.
    • (1994) Biophys. Chem. , vol.50 , pp. 293-304
    • Viappiani, C.1
  • 4
    • 0033778182 scopus 로고    scopus 로고
    • New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay
    • M. Collini, L. D'Alfonso and G. Baldini "New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay", Protein Sci. 9, pp. 1968-1974, 2000.
    • (2000) Protein Sci. , vol.9 , pp. 1968-1974
    • Collini, M.1    D'Alfonso, L.2    Baldini, G.3
  • 5
    • 0001333352 scopus 로고
    • Excited singlet- and triplet-absorption of pentaphene
    • R. Menzel, and W. Rapp, "Excited singlet- and triplet-absorption of pentaphene", Chem. Phys. 89, pp. 445-455, 1984.
    • (1984) Chem. Phys. , vol.89 , pp. 445-455
    • Menzel, R.1    Rapp, W.2
  • 6
    • 0004153561 scopus 로고    scopus 로고
    • Springer Verlag, Heidelberg, New York, Berlin
    • R. Menzel, Photonics, Springer Verlag, Heidelberg, New York, Berlin, 2001.
    • (2001) Photonics
    • Menzel, R.1
  • 8
    • 0030580838 scopus 로고    scopus 로고
    • Diffuse reflectance laser photolytic studies of pyrene included in zeolites. Formation of prene anion radicals via excited state electron transfer between guest molecules
    • S. Hashimoto, "Diffuse reflectance laser photolytic studies of pyrene included in zeolites. Formation of prene anion radicals via excited state electron transfer between guest molecules", Chem. Phys. Lett. 252, pp. 236-242, 1996.
    • (1996) Chem. Phys. Lett. , vol.252 , pp. 236-242
    • Hashimoto, S.1
  • 10
    • 0000658827 scopus 로고
    • Solvent effects on intermolecular electron transfer processes
    • C.M. Previtali, "Solvent effects on intermolecular electron transfer processes", Pure & Appl. Chem. 67, pp. 27-134, 1995.
    • (1995) Pure & Appl. Chem. , vol.67 , pp. 27-134
    • Previtali, C.M.1
  • 11
    • 0031251589 scopus 로고    scopus 로고
    • Photoinduced charge-transfer reaction between pyrene and n,n'-dimethylaniline on silca gel surfaces
    • G. Zhang, J.K. Thomas, A. Eremenko, T. Kikteva, F. Wilkinson, "Photoinduced Charge-Transfer Reaction between Pyrene and N,N'-Dimethylaniline on Silca Gel Surfaces", J. Phys. Chem. B 101, pp. 8569-8577, 1997.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8569-8577
    • Zhang, G.1    Thomas, J.K.2    Eremenko, A.3    Kikteva, T.4    Wilkinson, F.5
  • 12
    • 0011011370 scopus 로고
    • Electronic and vibrational spectra of matrix-isolated pyrene radical cations: Theoretical and experimental aspects
    • M. Vala, J. Szczepanski, F. Pauzat, O. Parisel, D. Talbi, Y. Ellinger, "Electronic and Vibrational Spectra of Matrix-Isolated Pyrene Radical Cations: Theoretical and Experimental Aspects", J. Phys. Chem. 98, pp. 9187-9196, 1994.
    • (1994) J. Phys. Chem. , vol.98 , pp. 9187-9196
    • Vala, M.1    Szczepanski, J.2    Pauzat, F.3    Parisel, O.4    Talbi, D.5    Ellinger, Y.6
  • 13
    • 0003018251 scopus 로고
    • A flash photolysis study of fluorescein
    • L. Lindqvist, "A flash photolysis study of fluorescein", Arkiv för kemi 16, pp. 79-138, 1961.
    • (1961) Arkiv för kemi , vol.16 , pp. 79-138
    • Lindqvist, L.1
  • 14
    • 0016530989 scopus 로고
    • The pH dependence of fluorescein fluorescence
    • M.M. Martin, and L. Lindqvist, "The pH dependence of fluorescein fluorescence", J. Lumin. 10, pp. 381-390, 1975.
    • (1975) J. Lumin. , vol.10 , pp. 381-390
    • Martin, M.M.1    Lindqvist, L.2
  • 15
    • 0001616163 scopus 로고
    • pH correlation of the absorption, fluorescence and polarization spectra of fluoresceinisothyocianate
    • D.P. Dimitrov, "pH correlation of the absorption, fluorescence and polarization spectra of fluoresceinisothyocianate" Dokl. Bolgarsk. Akad. Nauk 35, pp. 1467-1470, 1982.
    • (1982) Dokl. Bolgarsk. Akad. Nauk , vol.35 , pp. 1467-1470
    • Dimitrov, D.P.1
  • 16
    • 0021366404 scopus 로고
    • Fluorescein conjugates as indicators of subcellular pH. A critical evaluation
    • M.J. Geisow, "Fluorescein conjugates as indicators of subcellular pH. A critical evaluation", Exp. Cell Res. 150, pp. 29-35, 1984.
    • (1984) Exp. Cell Res. , vol.150 , pp. 29-35
    • Geisow, M.J.1
  • 17
    • 0000498268 scopus 로고
    • Photochemistry of xanthene dyes
    • Edited by D.H. Volman et al., Wiley, New York, Chichester, Brisbane, Toronto, Singapore
    • D.C. Neckers, and O.M. Valdes-Aguilera, "Photochemistry of xanthene dyes", in Advances in photochemistry Vol. 18. (Edited by D.H. Volman et al.), pp. 315 - 386. Wiley, New York, Chichester, Brisbane, Toronto, Singapore. 1993.
    • (1993) Advances in photochemistry , vol.18 , pp. 315-386
    • Neckers, D.C.1    Valdes-Aguilera, O.M.2
  • 18
    • 34247489528 scopus 로고
    • Absorption and fluorescence properties of fluorescein
    • R. Sjöback, J. Nygren and M. Kubista, "Absorption and fluorescence properties of fluorescein", Spectrochim. Acta A 51, L7-L21, 1995.
    • (1995) Spectrochim. Acta A , vol.51
    • Sjöback, R.1    Nygren, J.2    Kubista, M.3
  • 20
    • 0000469474 scopus 로고    scopus 로고
    • Solvent dependence of the fluorescence lifetimes of xanthene dyes
    • D. Magde, G.E. Rojas and P.G. Seybold, "Solvent dependence of the fluorescence lifetimes of xanthene dyes", Photochem. Photobiol. 70, pp. 737-744, 1999.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 737-744
    • Magde, D.1    Rojas, G.E.2    Seybold, P.G.3
  • 21
    • 0033200126 scopus 로고    scopus 로고
    • Identification of fluorescein-5'-isothiocyanate-modification sites in proteins by electrospray-ionization mass spectrometry
    • V. Schnaible, and M. Przybylski, "Identification of fluorescein-5'-isothiocyanate-modification sites in proteins by electrospray-ionization mass spectrometry", Bioconjugate Chem. 10, pp. 861-866, 1999.
    • (1999) Bioconjugate Chem. , vol.10 , pp. 861-866
    • Schnaible, V.1    Przybylski, M.2
  • 22
    • 0034672118 scopus 로고    scopus 로고
    • Preparation of Na,K-ATPase specifically modified on the anti-fluorescein antibody-inaccessible site by fluorescein 5'-isothiocyanate
    • S.-H. Lin, and L.D. Faller, "Preparation of Na,K-ATPase specifically modified on the anti-fluorescein antibody-inaccessible site by fluorescein 5'-isothiocyanate", Anal Biochem. 287, pp. 303-312, 2000.
    • (2000) Anal Biochem. , vol.287 , pp. 303-312
    • Lin, S.-H.1    Faller, L.D.2
  • 23
    • 0023869651 scopus 로고
    • Purification and characterization of four monofluorescein cobra alpha-toxin derivatives
    • D.A. Johnson, and R. Cushman, "Purification and characterization of four monofluorescein cobra alpha-toxin derivatives", J. Biol. Chem. 263, 2802-2807, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2802-2807
    • Johnson, D.A.1    Cushman, R.2
  • 24
    • 0026487591 scopus 로고
    • A brief survey of methods for preparing protein conjugates with dyes, haptens, and cross-linking reagents
    • M. Brinkley, "A brief survey of methods for preparing protein conjugates with dyes, haptens, and cross-linking reagents", Bioconjugate Chem. 3, pp. 2-13, 1992.
    • (1992) Bioconjugate Chem. , vol.3 , pp. 2-13
    • Brinkley, M.1
  • 25
    • 0028878752 scopus 로고
    • A fluorescence quench and dequench assay of fibrinogen polymerization, fibrinogenolysis, or fibrinolysis
    • J.-H. Wu, and S.L. Diamond, "A fluorescence quench and dequench assay of fibrinogen polymerization, fibrinogenolysis, or fibrinolysis", Anal. Biochem. 224, pp. 83-91, 1995.
    • (1995) Anal. Biochem. , vol.224 , pp. 83-91
    • Wu, J.-H.1    Diamond, S.L.2
  • 26
    • 0032573977 scopus 로고    scopus 로고
    • Emission quenching via intramolecular electron transfer for fluorescein conjugates. Dependences on driving force and medium
    • G. Jones, and X. Qian, "Emission quenching via intramolecular electron transfer for fluorescein conjugates. Dependences on driving force and medium", J. Photochem. Photobiol. A 113, pp. 125-134, 1998.
    • (1998) J. Photochem. Photobiol. A , vol.113 , pp. 125-134
    • Jones, G.1    Qian, X.2
  • 27
    • 0040960725 scopus 로고    scopus 로고
    • Identifying the site of initial tertiary structure disruption during apomyoglobin unfolding
    • Z. Feng, J.-H. Ha and S.N. Loh, "Identifying the site of initial tertiary structure disruption during apomyoglobin unfolding", Biochemistry 38, pp. 14433-14439, 1999.
    • (1999) Biochemistry , vol.38 , pp. 14433-14439
    • Feng, Z.1    Ha, J.-H.2    Loh, S.N.3
  • 28
    • 0034734278 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin
    • M. Brunori, "Structural dynamics of myoglobin", Biophys. Chem. 86, pp. 221-230, 2000.
    • (2000) Biophys. Chem. , vol.86 , pp. 221-230
    • Brunori, M.1
  • 29
    • 0001074064 scopus 로고    scopus 로고
    • The effect of tryptophanyl substitution on folding and structure of myoglobin
    • I. Sirangelo, S. Tavassi, P.L. Martelli and R. Casadio, "The effect of tryptophanyl substitution on folding and structure of myoglobin", Eur. J. Biochem. 267, pp. 3937-3945, 2000.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3937-3945
    • Sirangelo, I.1    Tavassi, S.2    Martelli, P.L.3    Casadio, R.4
  • 30
    • 0033968785 scopus 로고    scopus 로고
    • Tryptophanyl contributions to apomyoglobin fluorescence resolved by site-directed mutagenesis
    • I. Sirangelo, S. Tavassi and G. Irace, "Tryptophanyl contributions to apomyoglobin fluorescence resolved by site-directed mutagenesis", Biochim. Biophys. Acta 1476, pp. 173-180, 2000.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 173-180
    • Sirangelo, I.1    Tavassi, S.2    Irace, G.3
  • 31
    • 0034727681 scopus 로고    scopus 로고
    • Methanol-induced conformations of myoglobin at pH 4.0
    • K.R. Babu, and D.J. Douglas, "Methanol-induced conformations of myoglobin at pH 4.0", Biochemistry 39, pp. 14702-14710, 2000.
    • (2000) Biochemistry , vol.39 , pp. 14702-14710
    • Babu, K.R.1    Douglas, D.J.2
  • 32
    • 0000578033 scopus 로고
    • Chemical modification of myoglobin by isothiocyanate reagents - Effect of N-terminal amino group modification on protein conformation
    • G.B. Postnikova, "Chemical modification of myoglobin by isothiocyanate reagents - Effect of N-terminal amino group modification on protein conformation", Biochemistry (Moscow) 59, pp. 1069-1077, 1994.
    • (1994) Biochemistry (Moscow) , vol.59 , pp. 1069-1077
    • Postnikova, G.B.1
  • 33
    • 0029339452 scopus 로고
    • Comparison of three common amine reactive fluorescent probes used for conjugation to biomolecules by capillary zone electrophoresis
    • P.R. Banks, and D.M. Paquette, "Comparison of three common amine reactive fluorescent probes used for conjugation to biomolecules by capillary zone electrophoresis", Bioconjugate Chem. 6, pp. 447-458, 1995.
    • (1995) Bioconjugate Chem. , vol.6 , pp. 447-458
    • Banks, P.R.1    Paquette, D.M.2
  • 34
    • 0001626445 scopus 로고    scopus 로고
    • Chemical modification of proteins: Addition of fluorescein isothiocyanate
    • Edited by J.E. Coligan et al., Wiley, New York
    • K.F. Geoghegan, "Chemical modification of proteins: Addition of fluorescein isothiocyanate" in Current protocols in protein science Vol. 2, (Edited by J.E. Coligan et al.), pp. 15.2.7-15.2.8. Wiley, New York, 1997.
    • (1997) Current protocols in protein science , vol.2 , pp. 1527-1528
    • Geoghegan, K.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.