[Analysis of log-normal components of fluorescence spectra of prodan and acrylodan bound to proteins].
Steady-state fluorescence spectra of prodan and acrylodan covalently bound to cystein residue of Lys-Cys-Phe tripeptide in solvents of different polarity were analyzed. It was shown that the shape of spectral bands is well described by a log-normal function. Linear relations between three shape-determining parameters of the log-normal function (namely, the positions of spectral maximum and two half-maximum amplitudes) were revealed and evaluated for both fluorophores. This finding enabled us to present the shape of spectral bands of these fluorophores in any environment as analytical log-normal functions depending on only two parameters, the maximum position and the peak amplitude. The empirical uniparametric log-normal curve was used for the analysis of composite fluorescence spectra of prodan bound to bovine serum albumin and acrylodan covalently attached to actin or subfragment 1 of myosin.
Emel'ianenko
V I
VI
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
Reshetniak
Ia K
IaK
Andreev
O A
OA
Burshteĭn
E A
EA
D015081:2-Naphthylamine / Q000031:analogs & derivatives*; D000199:Actins / Q000737:chemistry*; D005456:Fluorescent Dyes; D015879:Myosin Subfragments / Q000737:chemistry*; D009994:Osmolar Concentration; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012996:Solutions; D013050:Spectrometry, Fluorescence
D000199:Actins; D005456:Fluorescent Dyes; D015879:Myosin Subfragments; D012996:Solutions; D012710:Serum Albumin, Bovine; C038517:prodan; C038518:acrylodan; D015081:2-Naphthylamine