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Introduction to intrinsically disordered proteins and regions
2019Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are fascinating dynamic conformational ensembles that are observed under physiological conditions. They facilitate a wide variety of biological processes via mechanisms that are distinct from their structured counterparts.
Oldfield, Christopher J. +3 more
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Role of Intrinsically Disordered Regions in Acceleration of Protein–Protein Association
The Journal of Physical Chemistry B, 2019Although intrinsically disordered proteins and intrinsically disordered regions (IDRs) in folded proteins are not able to form stable structures, it is known that they play critically important roles in various biological processes. However, despite multiple studies, the molecular mechanisms of their functions remain not fully understood. In this work,
Mikita M. Misiura, Anatoly B. Kolomeisky
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PREDICTION OF BOUNDARIES BETWEEN INTRINSICALLY ORDERED AND DISORDERED PROTEIN REGIONS
Biocomputing 2003, 2002Using proteins with both disordered and ordered regions collected through literature searches and database scanning, we assembled a set of 24-residue long segments centered on their order/disorder boundaries as well as a larger set of non-boundary segments consisting of either order or disorder.
Predrag Radivojac +3 more
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Predicting Protein–Protein Interfaces that Bind Intrinsically Disordered Protein Regions
Journal of Molecular Biology, 2019A long-standing goal in biology is the complete annotation of function and structure on all protein-protein interactions, a large fraction of which is mediated by intrinsically disordered protein regions (IDRs). However, knowledge derived from experimental structures of such protein complexes is disproportionately small due, in part, to challenges in ...
Eric T C, Wong, Jörg, Gsponer
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The Journal of Membrane Biology, 2019
The intrinsically disordered proteins and protein regions (IDPs/IDPRs) do not have unique structures, but are known to be functionally important and their conformational flexibility and structural plasticity have engendered a paradigmatic shift in the classical sequence-structure-function maxim. Fundamental understanding in this field has significantly
Rajeswari Appadurai +2 more
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The intrinsically disordered proteins and protein regions (IDPs/IDPRs) do not have unique structures, but are known to be functionally important and their conformational flexibility and structural plasticity have engendered a paradigmatic shift in the classical sequence-structure-function maxim. Fundamental understanding in this field has significantly
Rajeswari Appadurai +2 more
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Alternative splicing of intrinsically disordered regions and rewiring of protein interactions
Current Opinion in Structural Biology, 2013Alternatively spliced protein segments tend to be intrinsically disordered and contain linear interaction motifs and/or post-translational modification sites. An emerging concept is that differential inclusion of such disordered segments can mediate new protein interactions, and hence change the context in which the biochemical or molecular functions ...
Buljan M. +6 more
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Journal of Structural Biology, 2020
Intrinsically disordered proteins (IDPs) are crucial players in various cellular activities. Several experimental and computational analyses have been conducted to study structural pliability and functional potential of IDPs. In spite of active research in past few decades, what induces structural disorder in IDPs and how is still elusive. Many studies
Sushmita, Basu, Ranjit Prasad, Bahadur
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Intrinsically disordered proteins (IDPs) are crucial players in various cellular activities. Several experimental and computational analyses have been conducted to study structural pliability and functional potential of IDPs. In spite of active research in past few decades, what induces structural disorder in IDPs and how is still elusive. Many studies
Sushmita, Basu, Ranjit Prasad, Bahadur
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Archives of Biochemistry and Biophysics
In the early 2000s, the concept of "unstructured biology" has emerged to be an important field in protein science by generating various new research directions. Many novel strategies and methods have been developed that are focused on effectively identifying/predicting intrinsically disordered proteins (IDPs) and intrinsically disordered protein ...
Bondeepa Saikia, Anupaul Baruah
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In the early 2000s, the concept of "unstructured biology" has emerged to be an important field in protein science by generating various new research directions. Many novel strategies and methods have been developed that are focused on effectively identifying/predicting intrinsically disordered proteins (IDPs) and intrinsically disordered protein ...
Bondeepa Saikia, Anupaul Baruah
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Role of intrinsically disordered protein regions/domains in transcriptional regulation
Life Sciences, 2009In recent years, it has become quite evident that numerous proteins exist as an ensemble of conformers that collectively appears to be intrinsically disordered (ID). Of particular significance is the growing body of evidence that intrinsic disorder is found in disproportionately higher amounts in cell signaling proteins and transcription factors ...
Anna S, Garza, Nihal, Ahmad, Raj, Kumar
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Functional roles of transiently and intrinsically disordered regions within proteins
The FEBS Journal, 2015Proteins are structurally heterogeneous and comprise folded regions with variable conformational stabilities and intrinsically disordered protein regions that do not have well‐folded structures. Even small, well‐folded single‐domain proteins are structurally heterogeneous and contain multiple foldon units with different conformational stability ...
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