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Volumn 67, Issue 5, 1998, Pages 475-486

The Correct Use of "Average" Fluorescence Parameters

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EID: 0000821397     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1998.tb09082.x     Document Type: Article
Times cited : (389)

References (16)
  • 2
    • 0024016642 scopus 로고
    • Photophysical properties of pyrene covalently bound to polyelectrolytes
    • Stramel, R. D., C. Nguyen, S. E. Webber and M. A. J. Rodgers (1988) Photophysical properties of pyrene covalently bound to polyelectrolytes. J. Phys. Chem. 92, 2934-2938.
    • (1988) J. Phys. Chem. , vol.92 , pp. 2934-2938
    • Stramel, R.D.1    Nguyen, C.2    Webber, S.E.3    Rodgers, M.A.J.4
  • 3
    • 0031049050 scopus 로고    scopus 로고
    • The role of time-dependent measurements in elucidating static versus dynamic quenching processes
    • Webber, S. E. (1997) The role of time-dependent measurements in elucidating static versus dynamic quenching processes. Photochem. Photobiol. 65, 33-38.
    • (1997) Photochem. Photobiol. , vol.65 , pp. 33-38
    • Webber, S.E.1
  • 4
    • 0028961326 scopus 로고
    • Fluorescence study of the three tryptophan residues of the pore-forming domain of colicin A using multifrequency phase fluorometry
    • Vos, R., J. Izard, D. Baty and Y. Engelborghs (1995) Fluorescence study of the three tryptophan residues of the pore-forming domain of colicin A using multifrequency phase fluorometry. Biochemistry 34, 1734-1743.
    • (1995) Biochemistry , vol.34 , pp. 1734-1743
    • Vos, R.1    Izard, J.2    Baty, D.3    Engelborghs, Y.4
  • 5
    • 0000146432 scopus 로고    scopus 로고
    • Distance-dependent fluorescence quenching of p-bis[2-(5-phenyloxazolyl)]benzene by various quenchers
    • Zelent, B., J. Kusba, I. Gryczynski, M. L. Johnson and J. R. Lakowicz (1996) Distance-dependent fluorescence quenching of p-bis[2-(5-phenyloxazolyl)]benzene by various quenchers. J. Phys. Chem. 100, 18592-18602.
    • (1996) J. Phys. Chem. , vol.100 , pp. 18592-18602
    • Zelent, B.1    Kusba, J.2    Gryczynski, I.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 6
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophan fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer, S. S. (1971) Solute perturbation of protein fluorescence. The quenching of the tryptophan fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10, 3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 7
    • 0030767246 scopus 로고    scopus 로고
    • Fluorescence study of neurohypophyseal hormones and their analogues. Distance distribution in a series of arginine-vasopressin analogues
    • Wiczk, W., L. Lankiewicz, F. Kasprzykowski, S. Oldziej, H. Szmacinski, J. R. Lakowicz and Z. Grzonka (1997) Fluorescence study of neurohypophyseal hormones and their analogues. Distance distribution in a series of arginine-vasopressin analogues. Eur. Biophys. J. 26, 183-193.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 183-193
    • Wiczk, W.1    Lankiewicz, L.2    Kasprzykowski, F.3    Oldziej, S.4    Szmacinski, H.5    Lakowicz, J.R.6    Grzonka, Z.7
  • 8
    • 0027303079 scopus 로고
    • Time-resolved fluorescence of the single tryptophan of Bacillus stearothermophilus phosphofructokinase
    • Kim, S. J., F. N. Chowdhury, W. Stryjewski, E. S. Younathan, P. S. Russo and M. D. Barkley (1993) Time-resolved fluorescence of the single tryptophan of Bacillus stearothermophilus phosphofructokinase. Biophys. J. 65, 215-226.
    • (1993) Biophys. J. , vol.65 , pp. 215-226
    • Kim, S.J.1    Chowdhury, F.N.2    Stryjewski, W.3    Younathan, E.S.4    Russo, P.S.5    Barkley, M.D.6
  • 9
    • 0026473498 scopus 로고
    • Dilemma of correlating fluorescence quantum yield and intensity decay times in single tryptophan mutant proteins
    • Szabo, A. G. and C. Faerman (1992) Dilemma of correlating fluorescence quantum yield and intensity decay times in single tryptophan mutant proteins. SPIE 1640, 70-80.
    • (1992) SPIE , vol.1640 , pp. 70-80
    • Szabo, A.G.1    Faerman, C.2
  • 10
    • 84981779372 scopus 로고
    • Zwischenmolekular energiewanderung und fluoreszenze
    • Leipzig
    • Förster, T. (1948) Zwischenmolekular energiewanderung und fluoreszenze. Ann. Phys. (Leipzig) 2, 55-75.
    • (1948) Ann. Phys. , vol.2 , pp. 55-75
    • Förster, T.1
  • 11
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • Wu, P. and L. Brand (1994) Resonance energy transfer: methods and applications. Anal. Biochem. 218, 1-13.
    • (1994) Anal. Biochem. , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 12
  • 13
    • 0001374140 scopus 로고
    • Förster-type energy transfer simultaneous 'forward' and 'reverse' transfer between unlike fluorophores
    • Woolley, P., K. G. Steinhäuser and B. Epe (1987) Förster-type energy transfer simultaneous 'forward' and 'reverse' transfer between unlike fluorophores. Biophys. Chem. 26, 367-374.
    • (1987) Biophys. Chem. , vol.26 , pp. 367-374
    • Woolley, P.1    Steinhäuser, K.G.2    Epe, B.3
  • 14
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. (1994) The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66, 482-501.
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 15
    • 33847682952 scopus 로고
    • Correction of fluorescence spectra and the measurement of fluorescence quantum efficiency
    • Parker, C. A. and W. T. Rees (1960) Correction of fluorescence spectra and the measurement of fluorescence quantum efficiency. Analyst 85, 587-600.
    • (1960) Analyst , vol.85 , pp. 587-600
    • Parker, C.A.1    Rees, W.T.2
  • 16
    • 0030982174 scopus 로고    scopus 로고
    • Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli
    • Hennecke, J., A. Sillen, M. Huber-wunderlich, Y. Engelborghs and R. Glockshuber (1997) Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli. Biochemistry 36, 6391-6400.
    • (1997) Biochemistry , vol.36 , pp. 6391-6400
    • Hennecke, J.1    Sillen, A.2    Huber-wunderlich, M.3    Engelborghs, Y.4    Glockshuber, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.