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Structural vs. nonstructural proteins
Structural vs. nonstructural proteins

... Electrophoretic mobility shift assays (EMSA) ‐ Protein–DNA complexes migrate more slowly than free DNA molecules when  subjected to nondenaturing polyacrylamide or agarose gel electrophoresis. The assay is  also referred to as a gel shift or gel retardation assay because the rate of DNA migration  ...
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Intrinsically disordered proteins



An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure. IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins).The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three-dimensional structure. This dogma has been challenged over the last decades by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems. Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins. In some cases, IDPs can adopt a fixed three-dimensional structure after binding to other macromolecules.
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