Results 311 to 320 of about 7,902,914 (332)

Role of Intrinsically Disordered Regions in Acceleration of Protein–Protein Association

The Journal of Physical Chemistry B, 2019
Although 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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Remote on–off switching of protein activity by intrinsically disordered region

Nature Structural & Molecular Biology
While the regulation of protein function theoretically encompasses alterations in both structural conformation and dynamic properties, the latter aspect, specifically conformational entropy, remains relatively unexplored. Here we show that an intrinsically disordered region (IDR), a prominent component of the proteome, can remotely switch protein ...
Tuo Ji, Piao Ge, Shan Zhang, Chanjuan Wan, Hai-Long Liu, Xiaozhan Qu, Feng Zhu, Qing-Guo Gong, Weiya Xu, Chao Wang, Yu-Cai Wang, Chengdong Huang   +11 more
semanticscholar   +3 more sources

PREDICTION OF BOUNDARIES BETWEEN INTRINSICALLY ORDERED AND DISORDERED PROTEIN REGIONS

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, Zoran Obradovic, Celeste J. Brown, A. Keith Dunker   +3 more
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Predicting Protein–Protein Interfaces that Bind Intrinsically Disordered Protein Regions

Journal of Molecular Biology, 2019
A 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 Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins

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, Vladimir N. Uversky, Anand Srivastava   +2 more
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Alternative splicing of intrinsically disordered regions and rewiring of protein interactions

Current Opinion in Structural Biology, 2013
Alternatively 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., Chalancon G., Dunker A. K., Bateman A., Balaji S., Fuxreiter M., Babu M. M.   +6 more
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Do sequence neighbours of intrinsically disordered regions promote structural flexibility in intrinsically disordered proteins?

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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Role of intrinsically disordered protein regions/domains in transcriptional regulation

Life Sciences, 2009
In 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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Recent advances in de novo computational design and redesign of intrinsically disordered proteins and intrinsically disordered protein regions

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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Nanoassembly of spider silk protein mediated by intrinsically disordered regions

International Journal of Biological Macromolecules
Spider silk is the self-assembling product of silk proteins each containing multiple repeating units. Each repeating unit is entirely intrinsically disordered or contains a small disordered domain. The role of the disordered domain/unit in conferring silk protein storage and self-assembly is not fully understood yet.
Jiaxin, Li, Gabriel Z, Yang, Xue, Li, Hao Lei, Tan, Zhi Wei, Wong, Shimin, Jiang, Daiwen, Yang   +6 more
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