Investigating the permanent electric dipole moment of b-lactoglobulin fibrils, using transient electric birefringence (2006).

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Author	Rogers, S. S. Venema, P. Linden, E. Van Der Sagis, L. M. C. Donald, A. M.
Abstract	Abstract: Amyloid fibrils, which are polymeric assemblies of protein molecules, have been inten-sively studied on a structural level, yet due to complications such as the disorder within the mole-cules, several aspects of their structure remain mysterious. Similarly, the kinetics of assembly are not well understood. Here we investigate the electric dipole moment of b-lactoglobulin fibrils, a model amyloid fibril system, by applying the technique of transient electric birefringence. This moment appears to be large, and comparable to the total moment of the constituent protein mono-mers if they were joined in a chain, head-to-tail, without changing conformation, suggesting an ordered joining of monomers in the fibril. Such an ordered assembly may have implications for the assembly mechanism of b-lactoglobulin fibrils in particular, and amyloid fibrils in general. # 2006 Wiley Periodicals, Inc. Biopolymers 82: 241–252, 2006 This article was originally published online as an accepted preprint. The ‘‘Published Online’ ’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopoly-mers editorial office at
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Publisher Date	2006-01-01
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Subject Keyword	B-lactoglobulin Fibril Permanent Electric Dipole Moment Using Transient Electric Birefringence Amyloid Fibril Preprint Version Assembly Mechanism Wiley Periodical Biopoly-mers Editorial Office Structural Level Model Amyloid Fibril System Total Moment Transient Electric Birefringence Ordered Joining Accepted Preprint Electric Dipole Moment Constituent Protein Mono-mers Protein Molecule Polymeric Assembly Published Online Date Corresponds Several Aspect
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