Engagement of intrinsic disordered proteins in protein–protein interaction
Frontiers in Molecular Biosciences, 2023 Proteins from the intrinsically disordered group (IDP) focus the attention of many researchers engaged in protein structure analysis. The main criteria used in their identification are lack of secondary structure and significant structural variability ...
Irena Roterman +2 more
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D2P2: database of disordered protein predictions [PDF]
, 2013 We present the Database of Disordered Protein Prediction (D2P2), available at http://d2p2.pro (including website source code). A battery of disorder predictors and their variants, VL-XT, VSL2b, PrDOS, PV2, Espritz and IUPred, were run on all protein ...
Oates, Matt E. +3 more
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Biomolecules, 2021 Intrinsic disorder plays an important functional role in proteins. Disordered regions are linked to posttranslational modifications, conformational switching, extra/intracellular trafficking, and allosteric control, among other phenomena.
David Ortega-Alarcon +6 more
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Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle [PDF]
, 2007 The potent immunomodulatory, anti-inflammatory and procoagulant properties of the protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been previously found to be modulated by a supramolecular monomer-trimer ...
Silvia Vilasi +4 more
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Intrinsically Disordered Proteins (IDPs): Experimental and Computational Approaches in Drug Discovery [PDF]
Drug Designing & Intellectual Properties International Journal, 2018 Intrinsically disordered proteins (IDPs) are proteins that usually do not adopt well-defined native structures when isolated in solution under physiological conditions. Numerous IDPs have close relationships with human diseases such as Parkinson disease, Alzheimer disease, diabetes, and so on.
openaire +1 more source
Interactions of yeast dynein with dynein light chain and dynactin: General implications for intrinsically disordered duplex scaffolds in multi-protein assemblies [PDF]
Intrinsically disordered protein (IDP) duplexes composed of two IDP chains cross-linked by bivalent partner proteins form scaffolds for assembly of multiprotein complexes.
Barbar, Elisar, Jie, Jing, Löhr, Frank
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Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments
Frontiers in Molecular Biosciences, 2019 Intrinsically disordered proteins (IDPs) represent a structural class of proteins that do not have a well-defined, 3D fold in solution, and often have little secondary structure.
Steffen P. Graether
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AlphaFold2 models indicate that protein sequence determines both structure and dynamics
Scientific Reports, 2022 AlphaFold 2 (AF2) has placed Molecular Biology in a new era where we can visualize, analyze and interpret the structures and functions of all proteins solely from their primary sequences. We performed AF2 structure predictions for various protein systems,
Hao-Bo Guo +12 more
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, 2023 Intrinsically disordered proteins (IDPs) play a vital role in various biological processes and have attracted increasing attention in the past few decades. Predicting IDPs from the primary structures of proteins offers a rapid and facile means of protein
Akira Onoda +3 more
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Toward a consensus in protein structure nomenclature
, 2019 In a recent article, published in Intrinsically Disordered Proteins, a valuable consensus view regarding the nomenclature for disordered proteins was presented.1 In this work the authors present a thoughtful and systemic review of terms that have been ...
DaSilva, Linder C +2 more
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