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Mapping Charge Interactions in Intrinsically Disordered Proteins [PDF]
Advanced ScienceIntrinsically disordered proteins (IDPs) are often rich in charged residues, and electrostatic interactions have a pronounced effect on their conformational distributions, interactions and functions.
Michael Phillips +14 more
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PLoS ONE, 2019 Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Antonio Deiana +3 more
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Intrinsic structural disorder in cytoskeletal proteins. [PDF]
Cytoskeleton, 2013 Cytoskeleton, the internal scaffold of the cell, displays an exceptional combination of stability and dynamics. It is composed of three major filamentous networks, microfilaments (actin filaments), intermediate filaments (neurofilaments), and ...
Szabó, Beáta +3 more
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A membrane insertion code for intrinsically disordered proteins [PDF]
eLifeMembrane association of intrinsically disordered proteins (IDPs) mediates various cellular functions including membrane remodeling and signal transduction.
Fidha Nazreen Kunnath Muhammedkutty +1 more
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Transient tertiary structure in intrinsically disordered proteins revealed by multithermal enhanced sampling [PDF]
Nature CommunicationsIntrinsically disordered proteins populate heterogeneous conformational ensembles that are challenging to characterise. While all-atom molecular dynamics simulations can provide detailed insights into dynamic ensembles, achieving sufficient sampling ...
Julian O. Streit +4 more
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Biomolecules, 2022 Research in previous decades has shown that intrinsically disordered proteins (IDPs) and regions in proteins (IDRs) are as ubiquitous as highly ordered proteins. Despite this, research on IDPs and IDRs still has many gaps left to fill.
Miloš Avramov +7 more
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Roles, Characteristics, and Analysis of Intrinsically Disordered Proteins: A Minireview [PDF]
Life, 2020 In recent years, there has been a growing understanding that a significant fraction of the eukaryotic proteome is intrinsically disordered, and that these conformationally dynamic proteins play a myriad of vital biological roles in both normal and ...
Frederik Lermyte
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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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Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
, 2009 Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
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Intrinsically disordered proteins and their (disordered) proteomes in neurodegenerative disorders [PDF]
Frontiers in Aging Neuroscience, 2015 The recent years have witnessed a rise in the number of intrinsically disordered proteins (IDPs), also known as hybrid proteins, which possess both structured domains and biologically important intrinsically disordered protein regions (IDPRs). These proteins challenge the “one sequence—one structure—one function” concept by demonstrating that the lack ...
Vladimir N. Uversky +3 more
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