| | Methods for structural characterization of prefibrillar intermediates and amyloid fibrilsEdited by Peter Brzezinski Received 6 April 2009; received in revised form 20 May 2009; accepted 22 May 2009. published online 28 May 2009. Abstract Protein fibrillation is first and foremost a structural phenomenon. Adequate structural investigation of the central conformational individuals of the fibrillation process is however exceedingly difficult. This is due to the nature of the process, which may be described as a dynamically evolving equilibrium between a large number of structural species. These are furthermore of highly diverging sizes and present in very uneven amounts and timeframes. Different structural methods have different strengths and limitations. These, and in particular recent advances within solution analysis of the undisturbed equilibrium using small angle X-ray scattering, are reviewed here. Abbreviations: 3-D, three dimensional, Aβ, amyloid β, AFM, atomic force microscopy, CD, circular dichroism, EM, electron microscopy, EOM, ensemble optimization method, FTIR, fourier-transform infrared spectroscopy, NMR, nuclear magnetic resonance (spectroscopy), SANS, small-angle neutron scattering, SAS, small-angle scattering, SAXS, small-angle X-ray scattering, ss-NMR, solid-state NMR, STEM, scaning tunneling electron microscopy, ThT, thioflavin T, TTR, transthyretin, WAXS, wide-angle X-ray scattering a Department of Medicinal Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark b Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark  Corresponding author. Fax: +45 35 336 040.
PII: S0014-5793(09)00415-3 doi:10.1016/j.febslet.2009.05.040 © 2009 Federation of European Biochemical Societies | |
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ABSTRACT
