Protein structure probed by polarization spectroscopy. I. Evidence for fibrinogen rigidity from stationary fluorescence |
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| Authors: | A U Acu?a J González-Rodríguez M P Lillo K R Naqvi |
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| Affiliation: | 1. Flanders Marine Institute (VLIZ), InnovOcean Site, Wandelaarkaai 7, 8400 Ostend, Belgium;2. Flanders Research Institute for Agriculture, Fisheries and Food (ILVO), Animal Sciences Unit - Aquatic Environment and Quality, Ankerstraat 1, 8400 Ostend, Belgium;3. Department of Animal Sciences and Aquatic Ecology, Laboratory of Aquaculture & Artemia Reference Center, Ghent University, Coupure Links 653, 9000 Gent, Belgium;4. Department of Animal Sciences and Aquatic Ecology, GhEnToxLab, Ghent University, Coupure Links 653, 9000 Gent, Belgium;1. Department of Medical Chemistry, Key Laboratory of Medical Molecular Probes, School of Basic Medicine, Xinxiang Medical University, 601 Jin-sui Road, Hong Qi District, Xinxiang, Henan 453003, PR China;2. Grade 2020, Clinical Medicine, School of Basic Medicine, Xinxiang Medical University, Xinxiang, Henan 453003, PR China;1. Institute for the Application of Nuclear Energy, Department for Metabolism, University of Belgrade, Banatska 31b, 11080 Belgrade, Serbia;2. Faculty of Chemistry, Department of Biochemistry, Centre of Excellence for Molecular Food Sciences, University of Belgrade, Studentski trg 12-16, 11000 Belgrade, Serbia;3. Ghent University Global Campus, Yeonsu-gu, Incheon, South Korea;4. Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium;5. Serbian Academy of Sciences and Arts, Knez Mihailova 35, 11000 Belgrade, Serbia |
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| Abstract: | Two fluorescent derivatives of human fibrinogen have been synthesized, by the covalent bonding of 1-dimethylaminoaphthalene-5-sulphonyl and methylpyrene chromophores, to investigate the internal molecular dynamics of the protein in solution. The stationary fluorescence depolarization of these derivatives under isothermal conditions is described here while in an accompanying paper (part II) a time-resolved study is reported. From the static fluorescence data it is concluded that reorientational processes in the subnanosecond and microsecond time ranges account for all the observed depolarization. The faster motion was assigned to the restricted, localized oscillations of the label while the slow motion was ascribed to the overall rotation of the protein molecule. Consequently, the protein in solution appears considerably rigid in the 10-1000 ns range, in contrast with a previous conception of a flexible fibrinogen based on non-isothermal depolarization experiments. These previous experiments are, in fact, concordant with the rigid fibrinogen proposed here if they are reinterpreted using Weber's early ideas on thermally activated depolarization (G. Weber, J. Biochem. 51 (1952) 145). |
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