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[Conformations of multi-domain and partially disordered proteins - simulations and experiments].

Structural biology unravels three-dimensional structures of macromolecules such as proteins, DNA, RNA, and their complexes in the attempt to explain the basic mechanisms of their functions. Among the proteins that are most difficult to characterize structurally are those which have several large domains connected by long, unstructured polypeptide segments. Such proteins perform diverse functions in living organisms and, at the same time, they are very difficult to characterize using conventional methods of structural biology. This gap in the market has recently led to the development of hybrid methods that use state-of-the-art computational tools to combine complementary data from various experiments. This review article is focused on the implementation and usage of such hybrid methods. It includes a detailed description of how representative structures of multi-domain proteins are obtained using the so-called EROS (Ensemble Refinement of SAXS) hybrid method.

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