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Methods for structural characterization of prefibrillar intermediates and amyloid fibrils
Author(s) -
Langkilde Annette Eva,
Vestergaard Bente
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.040
Subject(s) - amyloid fibril , chemistry , biochemistry , amyloid (mycology) , fibril , characterization (materials science) , biophysics , stereochemistry , amyloid β , biology , nanotechnology , medicine , pathology , materials science , inorganic chemistry , disease
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.