SAS-Based Studies of Protein Fibrillation
Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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SAS-Based Studies of Protein Fibrillation. / Marasini, Carlotta; Vestergaard, Bente.
Biological Small Angle Scattering: Techniques, Strategies and Tips. Vol. 1009 Springer Science+Business Media, 2017. p. 149-165 (Advances in Experimental Medicine and Biology).Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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TY - CHAP
T1 - SAS-Based Studies of Protein Fibrillation
AU - Marasini, Carlotta
AU - Vestergaard, Bente
PY - 2017
Y1 - 2017
N2 - Protein fibrillation is associated with a number of fatal amyloid diseases (e.g. Alzheimer's and Parkinson's diseases). From a structural point of view, the aggregation process starts from an ensemble of native states that convert into transiently formed oligomers, higher order assemblies and protofibrils and, finally, fibrils. The different species exist in equilibrium in solution leading to a high degree of sample heterogeneity. It is impossible to physically isolate any single species for structural analysis: separation will alter the equilibrium and potentially cause structural changes.Small angle scattering is an optimal method for structural studies of the fibrillation process in order to further the knowledge of the associated diseases. The recorded scattering data include the scattering contribution of all the species in solution and must be decomposed to enable structural modeling of the individual components involved during the fibrillation, notably without physical separation of the species. In this chapter we explain how to optimize a small angle scattering analysis of the fibrillation process and the basic principles behind analysis of the data. We include several practical tips and highlight existing reports, exemplifying the wealth of information that can be derived from the method.
AB - Protein fibrillation is associated with a number of fatal amyloid diseases (e.g. Alzheimer's and Parkinson's diseases). From a structural point of view, the aggregation process starts from an ensemble of native states that convert into transiently formed oligomers, higher order assemblies and protofibrils and, finally, fibrils. The different species exist in equilibrium in solution leading to a high degree of sample heterogeneity. It is impossible to physically isolate any single species for structural analysis: separation will alter the equilibrium and potentially cause structural changes.Small angle scattering is an optimal method for structural studies of the fibrillation process in order to further the knowledge of the associated diseases. The recorded scattering data include the scattering contribution of all the species in solution and must be decomposed to enable structural modeling of the individual components involved during the fibrillation, notably without physical separation of the species. In this chapter we explain how to optimize a small angle scattering analysis of the fibrillation process and the basic principles behind analysis of the data. We include several practical tips and highlight existing reports, exemplifying the wealth of information that can be derived from the method.
KW - Journal Article
U2 - 10.1007/978-981-10-6038-0_9
DO - 10.1007/978-981-10-6038-0_9
M3 - Book chapter
C2 - 29218558
VL - 1009
T3 - Advances in Experimental Medicine and Biology
SP - 149
EP - 165
BT - Biological Small Angle Scattering: Techniques, Strategies and Tips
PB - Springer Science+Business Media
ER -
ID: 186866696