ArticleThe journal of physical chemistry letters2013
Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins.
Article in The journal of physical chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Lipid Composition Modulates Secondary Structure at the Biocondensate-Membrane Interface.bioRxiv : the preprint server for biology · 2026Article
- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Identifying protein conformational states in the Protein Data Bank: Toward unlocking the potential of integrative dynamics studies.Structural dynamics (Melville, N.Y.) · 2024Article
- Effects of Homogeneous and Heterogeneous Crowding on Translational Diffusion of Rigid Bovine Serum Albumin and Disordered Alfa-Casein.International journal of molecular sciences · 2023Article
- Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail.The journal of physical chemistry. B · 2023Article
- Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein.Science advances · 2022Article
- Disordered-Ordered Protein Binary Classification by Circular Dichroism Spectroscopy.Frontiers in molecular biosciences · 2022Article
- Crowding affects structural dynamics and contributes to membrane association of the NS3/4A complex.Biophysical journal · 2021Article
- Homo-oligomerization of the human adenosine AeLife · 2021Article
- Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.Frontiers in molecular biosciences · 2021Article
- Depletion interactions modulate the binding between disordered proteins in crowded environments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Modeling Crowded Environment in Molecular Simulations.Frontiers in molecular biosciences · 2019Review
- Atomistic Modeling of Intrinsically Disordered Proteins Under Polyethylene Glycol Crowding: Quantitative Comparison with Experimental Data and Implication of Protein-Crowder Attraction.The journal of physical chemistry. B · 2018Article
- Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding.Biophysical journal · 2018Article
- Molecular simulations of cellular processes.Biophysical reviews · 2017Review
- Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.The journal of physical chemistry. B · 2017Article
- Predictions of Backbone Dynamics in Intrinsically Disordered Proteins Using De Novo Fragment-Based Protein Structure Predictions.Scientific reports · 2017Article
- Protein folding, binding, and droplet formation in cell-like conditions.Current opinion in structural biology · 2017Review
- Folding propensity of intrinsically disordered proteins by osmotic stress.Molecular bioSystems · 2016Article
- Protein Composition Determines the Effect of Crowding on the Properties of Disordered Proteins.Biophysical journal · 2016Article
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2 authors.
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Abstract
Due to their conformational malleability, intrinsically disordered proteins (IDPs) are particularly susceptible to influences of crowded cellular environments. Here we report a computational study of the effects of macromolecular crowding on the conformational ensemble of a coarse-grained IDP model, by using two approaches. In one, the IDP is simulated along with the crowders; in the other, crowder-free simulations are postprocessed to predict the conformational ensembles under crowding. We found significant decreases in the radius of gyration of the IDP under crowding, and suggest repulsive interactions with crowders as a common cause for chain compaction in a number of experimental studies. The postprocessing approach accurately reproduced the conformational ensembles of the IDP in the direct simulations here, and holds enormous potential for realistic modeling of IDPs under crowding, by permitting thorough conformation sampling for the proteins even when they and the crowders are both represented at the all-atom level.
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