Results 1 to 10 of about 32,287 (136)
mBio, 2020 A distinguishing morphological feature of all herpesviruses is the multiprotein tegument layer located between the nucleocapsid and lipid envelope of the virion. Tegument proteins play multiple roles in viral replication, including viral assembly, but we
Claire M. Metrick +2 more
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MobiDB: intrinsically disordered proteins in 2021 [PDF]
Nucleic Acids Research, 2020 AbstractThe MobiDB database (URL: https://mobidb.org/) provides predictions and annotations for intrinsically disordered proteins. Here, we report recent developments implemented in MobiDB version 4, regarding the database format, with novel types of annotations and an improved update process.
Piovesan, Damiano +14 more
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Biophysical Reviews, 2022 Many different intrinsically disordered proteins and proteins with intrinsically disordered regions are associated with neurodegenerative diseases. These types of proteins including amyloid-β, tau, α-synuclein, CHCHD2, CHCHD10, and G-protein coupled receptors are increasingly becoming evaluated as potential drug targets in the pharmaceutical-based ...
Orkid Coskuner-Weber +2 more
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Expose flexible conformations for intrinsically disordered protein
Current Research in Structural BiologyThe folding conformation of native protein has flexibility in different degrees, which may bring difficulty in presenting the structures, and also it causes complexity in understanding the relationship between structure and functions.
Jiaan Yang +8 more
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Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Frontiers in Physics, 2019 Recognition of the natural abundance and functional importance of intrinsically disordered proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions (IDPRs) and ordered regions, is changing protein science.
Vladimir N. Uversky, Vladimir N. Uversky
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Entropy, 2019 We propose a framework to convert the protein intrinsic disorder content to structural entropy (H) using Shannon’s information theory (IT). The structural capacity (C), which is the sum of H and structural information (I), is equal to the amino acid ...
Hao-Bo Guo +5 more
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Evolutionarily conserved network properties of intrinsically disordered proteins. [PDF]
PLoS ONE, 2015 Intrinsically disordered proteins (IDPs) lack a stable tertiary structure in isolation. Remarkably, however, a substantial portion of IDPs undergo disorder-to-order transitions upon binding to their cognate partners.
Nivedita Rangarajan +2 more
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Order, Disorder, and Everything in Between
Molecules, 2016 In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
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Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins
Biomolecules, 2021 Motifs within proteins help us categorize their functions. Intrinsically disordered proteins (IDPs) are rich in short linear motifs, conferring them many different roles.
Estella A. Newcombe +7 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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