Electric birefringence study of an amyloid fibril system: The short end of the length distribution |
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Authors: | S S Rogers P Venema J P M van der Ploeg L M C Sagis A M Donald E van der Linden |
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Institution: | (1) Department of Physics, Cambridge University, CB3 0HE Cambridge, UK;(2) Laboratory of Food Physics, Wageningen University, P.O. Box 8129, 6700 EV Wageningen, The Netherlands;(3) Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands |
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Abstract: | In this article, a system of amyloid fibrils, based on the protein β-lactoglobulin, is studied by transient electric birefringence.
Single pulses of an electric field were applied to the solution, and the initial rise and subsequent decay of birefringence
analysed. The decay takes place on a range of relaxation times, and therefore contains information about the length distribution
of fibrils in the system. The information can be extracted using theories of the electric polarisability of polyelectrolyte
rods, since the fibrils are an example of these. Despite the long-standing complications of such theories, useful quantitative
information about the system can still be obtained. Using the Fixman model of polyelectrolyte polarisability, we obtain a
measurement of the short end of the length distribution which shows the fibril concentration as a function of length rising
linearly from 0.02-2 μm. The short end of the length distribution was unobtainable in our previous study using rheo-optics
(S.S. Rogers et al., Macromolecules 38, 2948 (2005)), but reasonable agreement between the two techniques shows they are complementary. |
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Keywords: | 82 35 Pq Biopolymers biopolymerization 82 35 Rs Polyelectrolytes 83 85 Ns Data analysis (interconversion of data computation of relaxation and retardation spectra time-temperature superposition etc ) 87 14 Ee Proteins |
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