Portability of a Small-Molecule Binding Site between Disordered Proteins
Biomolecules, 2022 Intrinsically disordered proteins (IDPs) are important in both normal and disease states. Small molecules can be targeted to disordered regions, but we currently have only a limited understanding of the nature of small-molecule binding sites in IDPs ...
Rajesh Jaiprashad +4 more
doaj +1 more source
Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins
Biomolecules, 2019 The common conception of intrinsically disordered proteins (IDPs) is that they stochastically sample all possible configurations driven by thermal fluctuations.
Ucheor B. Choi +4 more
doaj +1 more source
SPEADI: Accelerated Analysis of IDP-Ion Interactions from MD-Trajectories
Biology, 2023 The disordered nature of Intrinsically Disordered Proteins (IDPs) makes their structural ensembles particularly susceptible to changes in chemical environmental conditions, often leading to an alteration of their normal functions.
Emile de Bruyn +3 more
doaj +1 more source
Creating and Exploiting the Intrinsically Disordered Protein Knowledge Graph (IDP-KG).
, 2022 There are many data sources containing overlapping information about Intrinsically Disordered Proteins (IDP). IDPcentral aims to be a registry to aid the discovery of data about proteins known to be intrinsically disordered by aggregating the content from these sources. Traditional ETL approaches for populating IDPcentral require the API and data model
Gray, Alasdair +4 more
openaire +2 more sources
Diverging Liquid–Liquid Phase Separation Behavior of Different Recombinant Major Ampullate Spidroins
Advanced Science, EarlyView.Fibers spun from the MaSp1‐derivative as well as MaSp1‐MaSp2‐mixtures provide a deeper insight into the assembly process of the spidroins and how hierarchical architectures of spider silk fibers could be achieved. ABSTRACT Spider silk fibers show exceptional mechanical properties, based on their underlying spider silk proteins (spidroins) as well as a ...
Tim Schiller +2 more
wiley +1 more source
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
α‐Synuclein Forms Distinct Micelle‐Like Assemblies at Low Ionic Strengths
Advanced Science, EarlyView.At high ionic strength, α‐synuclein forms diverse assemblies, including oligomers, fibrils, and condensates. Here, we show that at low ionic strength, α‐synuclein adopts a distinct, low‐abundance assembly state. These assemblies maintain a constant size above a critical concentration and do not coalesce, suggesting a micelle‐like organization ...
Sophie Hertel +10 more
wiley +1 more source
IDP-Bert: Predicting Properties of Intrinsically Disordered Proteins Using Large Language Models
The Journal of Physical Chemistry B22 pages, 5 ...
Parisa Mollaei +3 more
openaire +3 more sources
Environment-Specific Force Field for Intrinsically Disordered and Ordered Proteins [PDF]
, 2020 The need for accurate and efficient force fields for modeling 3D structures of macrobiomolecules and in particular intrinsically disordered proteins (IDPs) has increased with recent findings to associate IDPs and human diseases.
Dong Song (2474047) +7 more
core +2 more sources
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
core +1 more source