title: Structural characterization of prefibrillar intermediates and amyloid fibrils by small-angle X-ray scattering.
abstract: Structural investigation of the species present during protein fibrillation is of tremendous importance, yet complicated by the equilibrium between species of very different sizes and life-times. Small-angle X-ray scattering may be applied to solve this problem, providing both information about the process (number of species present and volume fractions of individual species) and low-resolution three-dimensional shape reconstructions of individual species. Here, we describe in detail the challenges associated with the approach, exemplified using data from fibrillating insulin or α-synuclein samples.
authors.affiliation: Faculty of Pharmaceutical Sciences, University of Copenhagen, Copenhagen, Denmark.
authors.forename: Annette Eva
authors.initials: AE
authors.lastname: Langkilde
authors.forename: Bente
authors.initials: B
authors.lastname: Vestergaard
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D007328:Insulin / Q000737:chemistry*; D008958:Models, Molecular; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction / Q000379:methods*; D051844:alpha-Synuclein / Q000737:chemistry*
chemical_list: D000682:Amyloid; D007328:Insulin; D051844:alpha-Synuclein