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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Conformational entropy in molecular recognition of intrinsically disordered proteins.
Current Opinion in Structural Biology, 2023 Broad conformational ensembles make intrinsically disordered proteins or regions entropically intriguing. Although methodologically challenging and understudied, emerging studies into their changes in conformational entropy (ΔS°conf) upon complex ...
K. Skriver, F. Theisen, B. Kragelund
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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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Actinidia DRM1--an intrinsically disordered protein whose mRNA expression is inversely correlated with spring budbreak in kiwifruit. [PDF]
PLoS ONE, 2013 Intrinsically disordered proteins (IDPs) are a relatively recently defined class of proteins which, under native conditions, lack a unique tertiary structure whilst maintaining essential biological functions.
Marion Wood +6 more
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Nature Communications, 2023 Intrinsically disordered proteins (IDPs) play crucial roles in cellular processes and hold promise as drug targets. However, the dynamic nature of IDPs remains poorly understood.
Wenzhe Liu +7 more
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, 2013 Molecular recognition by intrinsically disordered proteins (IDPs) commonly involves specific localized contacts and target-induced disorder to order transitions.
Sheung Chun Ng +19 more
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Molecular & Cellular Oncology, 2019 Intrinsically disordered proteins (IDPs) do not have a well-defined structure, but they have key biological tasks in cancer development. By using the disordered cancer-related protein NUPR1 as a proof-of-concept, we have developed a new multidisciplinary
Patricia Santofimia-Castaño +7 more
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Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). [PDF]
PLoS ONE, 2016 Intrinsically disordered proteins (IDPs) play a major role in various cellular functions ranging from transcription to cell migration. Mutations/modifications in such IDPs are shown to be associated with various diseases.
Muniasamy Neerathilingam +2 more
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Data–driven Modelling of Intrinsically Disordered Proteins [PDF]
, 2019 In this thesis we investigated the relationships between amino acid sequence and biophysical properties of intrinsically disordered proteins involved in Parkinson's and Alzheimer's disease (IDPs), gauged from NMR ...
Tamiola, Kamil
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Adenoviral E1A Exploits Flexibility and Disorder to Target Cellular Proteins
Biomolecules, 2020 Direct interaction between intrinsically disordered proteins (IDPs) is often difficult to characterize hampering the elucidation of their binding mechanism.
Maria Grazia Murrali +2 more
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