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Open questions: Reflections on intrinsically disordered proteins [PDF]
Network Biology, 2021 Intrinsically Disordered Proteins or Regions (IDPs) are proteins that lack a predetermined 3D structure playing key cellular functions including regulation, signaling, and protein-protein/DNA interaction.
Mouna Choura, Ahmed Rebai
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IDP–CRF: Intrinsically Disordered Protein/Region Identification Based on Conditional Random Fields [PDF]
International Journal of Molecular Sciences, 2018 Accurate prediction of intrinsically disordered proteins/regions is one of the most important tasks in bioinformatics, and some computational predictors have been proposed to solve this problem. How to efficiently incorporate the sequence-order effect is critical for constructing an accurate predictor because disordered region distributions show global
Liu, Yumeng, Wang, Xiaolong, Liu, Bin
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RFPR-IDP: reduce the false positive rates for intrinsically disordered protein and region prediction by incorporating both fully ordered proteins and disordered proteins [PDF]
Briefings in Bioinformatics, 2020 AbstractAs an important type of proteins, intrinsically disordered proteins/regions (IDPs/IDRs) are related to many crucial biological functions. Accurate prediction of IDPs/IDRs is beneficial to the prediction of protein structures and functions. Most of the existing methods ignore the fully ordered proteins without IDRs during training and test ...
Yumeng Liu, Xiaolong Wang, Bin Liu
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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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The IDP-Specific Force Field ff14IDPSFF Improves the Conformer Sampling of Intrinsically Disordered Proteins [PDF]
Journal of Chemical Information and Modeling, 2017 Intrinsically disordered proteins (IDPs) or intrinsically disordered regions do not have a fixed tertiary structure but play key roles in signal regulation, molecule recognition, and drug targeting. However, it is difficult to study the structure and function of IDPs by traditional experimental methods because of their diverse conformations ...
Dong Song, Ray Luo 0001, Hai-Feng Chen
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Frontiers in Genetics, 2018 Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are functional proteins and domains that devoid stable secondary and/or tertiary structure.
April L. Darling +2 more
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Journal of Chemical Theory and Computation, 2023 Intrinsically disordered proteins (IDPs) populate a range of conformations that are best described by a heterogeneous ensemble. Grouping an IDP ensemble into “structurally similar” clusters for visualization, interpretation, and analysis purposes is a ...
Rajeswari Appadurai +4 more
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New insights into disordered proteins and regions according to the FOD-M model.
PLoS ONE, 2022 A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit ...
Irena Roterman +3 more
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PLoS ONE, 2023 Intrinsically disordered proteins (IDPs) are proteins that lack a stable 3D structure but maintain a biological function. It has been frequently suggested that IDPs are difficult to align because they tend to have fewer conserved residues compared to ...
Andrew C Riley +2 more
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Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions
Biomolecules, 2021 Intrinsically disordered proteins (IDPs) are highly prevalent and play important roles in biology and human diseases. It is now also recognized that many IDPs remain dynamic even in specific complexes and functional assemblies.
Xiping Gong, Yumeng Zhang, Jianhan Chen
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