Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering.
Intrinsically Disordered Proteins (IDPs) are fundamental actors of biological processes. Their inherent plasticity facilitates very specialized tasks in cell regulation and signalling, and their malfunction is linked to severe pathologies. Understanding the functional role of disorder requires the structural characterization of IDPs and the complexes they form. Small-angle Scattering of X-rays (SAXS) and Neutrons (SANS) have notably contributed to this structural understanding. In this review we summarize the most relevant developments in the field of SAS studies of disordered proteins. Emphasis is given to ensemble methods and how SAS data can be combined with computational approaches or other biophysical information such as NMR. The unique capabilities of SAS enable its application to extremely challenging disordered systems such as low-complexity regions, amyloidogenic proteins and transient biomolecular complexes. This reinforces the fundamental role of SAS in the structural and dynamic characterization of this elusive family of proteins.
['Cordeiro|Tiago N|TN|', 'Herranz-Trillo|Fátima|F|', 'Urbanek|Annika|A|', 'Estaña|Alejandro|A|', 'Cortés|Juan|J|', 'Sibille|Nathalie|N|', 'Bernadó|Pau|P|']
D058227:Amyloidogenic Proteins D003198:Computer Simulation D006801:Humans D064267:Intrinsically Disordered Proteins D008958:Models, Molecular D033363:Neutron Diffraction D019906:Nuclear Magnetic Resonance, Biomolecular D011487:Protein Conformation D053838:Scattering, Small Angle D017356:Synchrotrons D014961:X-Ray Diffraction
Intrinsically disordered proteins Ensemble methods Low-complexity regions Amyloids Nuclear magnetic resonance Protein-protein interactions Random coil models Small-angle neutron scattering Small-angle x-ray scattering