The integration of complementary molecular methods (including X-ray crystallography, NMR spectroscopy, small angle X-ray/neutron scattering, and computational techniques) is frequently required to obtain a comprehensive understanding of dynamic macromolecular complexes. In particular, these techniques are critical for studying intrinsically disordered protein regions (IDRs) or intrinsically disordered proteins (IDPs) that are part of large protein:protein complexes. Here, we explain how to prepare IDP samples suitable for study using NMR spectroscopy, and describe a novel SAXS modeling method (ensemble refinement of SAXS; EROS) that integrates the results from complementary methods, including crystal structures and NMR chemical shift perturbations, among others, to accurately model SAXS data and describe ensemble structures of dynamic macromolecular complexes.
CITATION STYLE
Peti, W., Page, R., Boura, E., & Różycki, B. (2018). Structures of dynamic protein complexes: Hybrid techniques to study MAP kinase complexes and the ESCRT system. In Methods in Molecular Biology (Vol. 1688, pp. 375–389). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7386-6_17
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