Protein structure probed by polarization spectroscopy. II. A time-resolved fluorescence study of human fibrinogen |
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| Authors: | A U Acu?a J González-Rodríguez M P Lillo K R Naqvi |
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| Affiliation: | 1. Instituto de Química Física, C.S.I.C., Serrano 119, E-28006 Madrid, Spain;2. Department of Physics, University of Trondheim, N-7055 Dragvoll, Norway;1. Department of Chemical and Process Engineering, Faculty of Engineering and Built Environment, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia;2. Fuel Cell Institute, Universiti Kebangsaan Malaysia, 43600 UKM Bangi, Selangor, Malaysia;1. Center for Environmental Nanoscience and Risk (CENR) Arnold School of Public Health University of South Carolina, USA;2. PerkinElmer Canada, 501 Rowntree Dairy Rd, Unit 6, Woodbridge, ON, Canada L4L 8H1;1. Department of Chemistry, University College London, 20 Gordon St, London, WC1H 0AJ, United Kingdom;2. College of Science and Engineering, Flinders University, Bedford Park, South Australia, 5042, Australia;3. Australian Institute for Bioengineering and Nanotechnology, University of Queensland, St Lucia, Queensland, 4072, Australia;4. Department of Electronic and Electrical Engineering, University College London, Torrington Place, London, WC1E 7JE, United Kingdom;5. Department of Chemistry, Imperial College London, Imperial College Road, London, SW7 2AZ, United Kingdom;1. Key Laboratory of Applied Surface and Colloid Chemistry (MOE), School of Materials Science and Engineering, Shaanxi Normal University, Xi’an 710062, PR China;2. Science and Technology on Combustion and Explosion Laboratory, Xi’an Modern Chemistry Research Institute, Xi’an 710065, PR China |
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| Abstract: | Human fibrinogen in solution was studied by monitoring the time-resolved depolarization of the fluorescence emitted by two spectroscopic labels of which the fluorescence lifetimes differ by an order of magnitude. Contrary to a long-held view, no evidence of molecular flexibility was found in the 10-1000 ns range. In addition, from the rate of the overall rotation, it is proposed that a prolate and symmetric ellipsoid of 47 X 10.5 nm may represent the time-averaged hydrodynamic size and shape of the protein in solution. This rigid and highly hydrated structure (4 g water/g protein) accommodates the latest nodular models obtained from electron microscopy, explains the singular hydrodynamics of fibrinogen and, apparently, it would perform the two main functions of the protein in haemostasis, blood coagulation and platelet aggregation, more efficiently than the flexible molecule. |
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