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Intrinsically disordered proteins/regions and insight into their biomolecular interactions
Biophysical Chemistry, 2022Proteins may vary from being rigid to having flexible regions to being completely disordered, either as an intrinsically disordered protein (IDP) or having specific intrinsically disordered regions (IDRs). IDPs/IDRs can form complexes otherwise impossible, such as wrapping around the binding partner, hence providing the plasticity needed for achieving ...
Pinak, Chakrabarti, Devlina, Chakravarty
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Journal of Genetics and Genomics, 2023 The phytohormone auxin plays crucial roles in nearly every aspect of plant growth and development. Auxin signaling is activated through the phytohormone-induced proteasomal degradation of the Auxin/INDOLE-3-ACETIC ACID (Aux/IAA) family of transcriptional
Hongwei Jing +2 more
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Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Annual Review of Biochemistry, 2014Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet they exhibit biological activities. Their mobile flexibility and structural instability are encoded by their amino acid sequences. They recognize proteins, nucleic acids, and other types of partners; they accelerate interactions and chemical reactions between
Christopher J, Oldfield, A Keith, Dunker
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PREDICTION OF BOUNDARIES BETWEEN INTRINSICALLY ORDERED AND DISORDERED PROTEIN REGIONS [PDF]
Biocomputing 2003, 2002 Using 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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Protein & Peptide Letters, 2020
Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
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Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
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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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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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