Intrinsically disordered proteins: structural and functional dynamics

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Intrinsically disordered proteins.

Our understanding of protein function has been predominated by the view that proteins need to adopt a defined three dimensional structure to be able to carry out their function. Indeed, crystal structures of numerous proteins have been instrumental in establishing the structure– function paradigm. For example, the structures of numerous enzymes have highlighted the need for particular chemical ...

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Intrinsically Disordered Proteins

In the same way that neither a messy lab bench nor a clean one is a reliable indicator of a researcher’s productivity, a protein’s function cannot be judged solely on the basis of its neatly folded and stable domains. As evidenced by recent work discussed in this Select, we are learning that intrinsically disordered regions feature in many of the cell’s most productive multitaskers, proteins wh...

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Intrinsically Disordered Proteins: Methods for Structure and Dynamics Studies

Intrinsically disordered proteins (IDPs) partially or completely lack a cooperatively folded structure under native conditions, preventing their equilibrium state from being adequately described by a single structural model. Reaching the goal of quantitatively describing IDP structure–function relationships has required the development of novel experiments aiming to characterize their structure...

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Coevolved Residues and the Functional Association for Intrinsically Disordered Proteins

The evolution of intrinsically disordered proteins has been studied primarily by focusing on evolutionary changes at an individual position such as substitution and conservation, but the evolutionary association between disordered residues has not been comprehensively investigated. Here, we analyze the distribution of residue-residue coevolution for disordered proteins. We reveal that the degre...

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Salt-bridge dynamics in intrinsically disordered proteins: A trade-off between electrostatic interactions and structural flexibility.

Intrinsically Disordered Proteins (IDPs) are enriched in charged and polar residues; and, therefore, electrostatic interactions play a predominant role in their dynamics. In order to remain multi-functional and exhibit their characteristic binding promiscuity, they need to retain considerable dynamic flexibility. At the same time, they also need to accommodate a large number of oppositely charg...

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ژورنال

عنوان ژورنال: Research and Reports in Biology

سال: 2017

ISSN: 1179-7274

DOI: 10.2147/rrb.s57282