Methods for structural characterization of prefibrillar intermediates and amyloid fibrils
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | FEBS Letters |
Volume | 583 |
Issue number | 16 |
Pages (from-to) | 2600-2609 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 2009 |
Bibliographical note
Keywords: Amyloid; Animals; Humans; Models, Chemical; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Scattering, Small Angle; X-Ray Diffraction
- Former Faculty of Pharmaceutical Sciences
Research areas
ID: 18658291