, 2020 Several intrinsically disordered proteins (IDPs) exhibit high affinity for lipid membranes. Among the different biophysical methods to probe protein-lipid interaction, neutron reflectometry (NR) can provide direct and structural detailed information on ...
Luchini A +5 more
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An Evolutionary Algorithm for the Design of Different Degrees of Secondary Structure in Intrinsically Disordered Proteins (IDPs) [PDF]
Biophysical Journal, 2015 In recent experimental studies of coupled folding and binding of IDPs investigators have adapted methods from the protein folding literature whereby point mutations are used to identify the degree to which different regions are pre-folded prior to the rate limiting step in binding and folding. These approaches assume a one-to-one correspondence between
Harmon, Tyler S., Pappu, Rohit V.
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, 2021 The protein folding problem was apparently solved recently by the advent of a deep learning method for protein structure prediction called AlphaFold. However, this program is not able to make predictions about the protein folding pathways.
Strodel, Birgit
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Binding of two intrinsically disordered peptides to a multi-specific protein: a combined Monte Carlo and molecular dynamics study. [PDF]
PLoS Computational Biology, 2012 The unique ability of intrinsically disordered proteins (IDPs) to fold upon binding to partner molecules makes them functionally well-suited for cellular communication networks.
Iskra Staneva +3 more
doaj +1 more source
Regulated Disorder: Posttranslational Modifications Control the RIN4 Plant Immune Signaling Hub
Molecular Plant-Microbe Interactions, 2019 RIN4 is an intensively studied immune regulator in Arabidopsis and is involved in perception of microbial features outside and bacterial effectors inside plant cells.
Tania Y. Toruño +3 more
doaj +1 more source
Intrinsic Disorder of the C-Terminal Domain of Drosophila Methoprene-Tolerant Protein. [PDF]
PLoS ONE, 2016 Methoprene tolerant protein (Met) has recently been confirmed as the long-sought juvenile hormone (JH) receptor. This protein plays a significant role in the cross-talk of the 20-hydroxyecdysone (20E) and JH signalling pathways, which are important for ...
Marta Kolonko +6 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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Connecting the αα-hubs: same fold, disordered ligands, new functions
Cell Communication and Signaling, 2021 Background Signal fidelity depends on protein–protein interaction–‘hubs’ integrating cues from large interactomes. Recently, and based on a common secondary structure motif, the αα-hubs were defined, which are small α-helical domains of large, modular ...
Lasse Staby +5 more
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Modulation of the disordered conformational ensembles of the p53 transactivation domain by cancer-associated mutations. [PDF]
PLoS Computational Biology, 2015 Intrinsically disordered proteins (IDPs) are frequently associated with human diseases such as cancers, and about one-fourth of disease-associated missense mutations have been mapped into predicted disordered regions.
Debabani Ganguly, Jianhan Chen
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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
doaj +1 more source