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Intrinsically disordered proteins
Molecular BioSystems, 2011M. Madan Babu introduces this Molecular BioSystems themed issue on intrinsically disordered proteins.
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Intrinsic Fluorescence of Intrinsically Disordered Proteins
2012Resolution of the intrinsic emission properties of a protein by different fluorescence spectroscopy techniques is an invaluable tool to detect and characterize its structural architecture and conformational changes under different experimental conditions.
NEYROZ, PAOLO, CIURLI, STEFANO LUCIANO
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Exploring Protein Intrinsic Disorder with MobiDB
2020Nowadays, it is well established that many proteins or regions under physiological conditions lack a fixed three-dimensional structure and are intrinsically disordered. MobiDB is the main repository of protein disorder and mobility annotations, combining different data sources to provide an exhaustive overview of intrinsic disorder.
Monzon A. M. +4 more
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Translocation of polyampholytes and intrinsically disordered proteins⋆
The European Physical Journal E, 2018Polyampholytes are polymers carrying electrical charges of both signs along their backbone. We consider synthetic polyampholytes with a quenched random charge sequence and intrinsically disordered proteins, which have a well-defined charge sequence and behave like polyampholytes in the denaturated state.
Johner, Albert, Joanny, Jean-François
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Intrinsically disordered proteins: regulation and disease
Current Opinion in Structural Biology, 2011Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions because disordered segments permit interaction with several proteins and hence the re-use of the same protein in multiple pathways. Understanding IDP regulation is important because altered expression of IDPs is associated with many diseases. Recent studies show
Babu, M.M. +3 more
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Druggability of Intrinsically Disordered Proteins
2015Although the proteins in all the current major classes considered to be druggable are folded in their native states, intrinsically disordered proteins (IDPs) are becoming attractive candidates for therapeutic intervention by small drug-like molecules.
Priyanka, Joshi, Michele, Vendruscolo
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Intrinsically disordered proteins
This chapter explores intrinsically disordered proteins (IDPs), detailing their discovery, structural characteristics, and indispensable biological functions. It introduces the hypothesis that unfolded proteins can bind diverse partners, first proposed in 1939, and follows the experimental validation of IDPs using NMR and X-ray methods.openaire +2 more sources
Intrinsic Disorder and Protein Function
Biochemistry, 2002A Keith, Dunker +4 more
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Configurational Entropy of Folded Proteins and Its Importance for Intrinsically Disordered Proteins
International Journal of Molecular Sciences, 2021Robert Vernon +2 more
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