The Intrinsically Disordered Region of ExbD Is Required for Signal Transduction [PDF]
Journal of Bacteriology, 2019 The TonB system is a virulence factor for Gram-negative pathogens. The mechanism by which cytoplasmic membrane proteins of the TonB system transduce an electrochemical gradient into mechanical energy is a long-standing mystery. TonB, ExbB, and ExbD primary amino acid sequences are characterized by regions of predicted intrinsic ...
Kopp, Dale R., Postle, Kathleen
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Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology. [PDF]
PLoS ONE, 2013 The abundance and potential functional roles of intrinsically disordered regions in aquaporin-4, Kir4.1, a dystrophin isoforms Dp71, α-1 syntrophin, and α-dystrobrevin; i.e., proteins constituting the functional core of the astrocytic dystrophin ...
Insung Na +5 more
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Membranes, 2022 The functional processes of many proteins involve the association of their intrinsically disordered regions (IDRs) with acidic membranes. We have identified the membrane-association characteristics of IDRs using extensive molecular dynamics (MD ...
Sanbo Qin +4 more
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Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis. [PDF]
PLoS Computational Biology, 2009 We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein complexes.
Jessica H Fong +5 more
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Influence of sequence changes and environment on intrinsically disordered proteins. [PDF]
PLoS Computational Biology, 2009 Many large-scale studies on intrinsically disordered proteins are implicitly based on the structural models deposited in the Protein Data Bank. Yet, the static nature of deposited models supplies little insight into variation of protein structure and ...
Amrita Mohan +2 more
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Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered
Biomolecules, 2022 There is increasing evidence that many intrinsically disordered regions (IDRs) in proteins play key functional roles through interactions with other proteins or nucleic acids. These interactions often exhibit a context-dependent structural behavior.
Mariane Gonçalves-Kulik +6 more
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Insights into the regulation of intrinsically disordered proteins in the human proteome by analyzing sequence and gene expression data [PDF]
, 2009 Background: Disordered proteins need to be expressed to carry out specified functions; however, their accumulation in the cell can potentially cause major problems through protein misfolding and aggregation.
Edwards, Y.J.K. +11 more
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Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions
Biomolecules, 2022 Intrinsically disordered regions (IDRs) carry out many cellular functions and vary in length and placement in protein sequences. This diversity leads to variations in the underlying compositional biases, which were demonstrated for the short vs. long IDRs. We analyze compositional biases across four classes of disorder: fully disordered proteins; short
Bi Zhao, Lukasz Kurgan
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Inferring function using patterns of native disorder in proteins [PDF]
, 2007 Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30% and 60% of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they ...
Swindells, MB +14 more
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Allosteric modulation of nucleoporin assemblies by intrinsically disordered regions [PDF]
Science Advances, 2019 Kap121 interacts with an intrinsically disordered region of Nup53 to allosterically modulate Nup53 binding to partner nucleoporins.
Bartlomiej Jan Blus +5 more
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