ArticleBiophysical journal2016
Protein Composition Determines the Effect of Crowding on the Properties of Disordered Proteins.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Article
- Anisosmotic Modulation of Mutant Huntingtin Aggregation vis-a-vis HSP70 Induction─Implications for Aging, Hypo-Hydration, and Neurodegeneration.ACS chemical neuroscience · 2026Article
- Multiphasic Organization and Differential Dynamics of Proteins within Protein-DNA Biomolecular Condensates.The journal of physical chemistry. B · 2025Article
- A coarse-grained model for disordered proteins under crowded conditions.Protein science : a publication of the Protein Society · 2025Article
- PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025Article
- Crowder titrations enable the quantification of driving forces for macromolecular phase separation.Biophysical journal · 2024Article
- Sequence-Dependent Conformational Transitions of Disordered Proteins During Condensation.bioRxiv : the preprint server for biology · 2024Article
- 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
- Effect of Charge Distribution on the Dynamics of Polyampholytic Disordered Proteins.Macromolecules · 2022Article
- Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein.The journal of physical chemistry letters · 2022Article
- Crowding affects structural dynamics and contributes to membrane association of the NS3/4A complex.Biophysical journal · 2021Article
- Molecular crowding accelerates aggregation of α-synuclein by altering its folding pathway.European biophysics journal : EBJ · 2021Article
- Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.Frontiers in molecular biosciences · 2021Article
- The Effects of Chain Length on the Structural Properties of Intrinsically Disordered Proteins in Concentrated Solutions.The journal of physical chemistry. B · 2020Article
- 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
- Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding.Protein science : a publication of the Protein Society · 2019Review
- Temperature-Controlled Liquid-Liquid Phase Separation of Disordered Proteins.ACS central science · 2019Article
- 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
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unlike dilute experimental conditions under which biological molecules are typically characterized, the cell interior is crowded by macromolecules, which affects both the thermodynamics and kinetics of in vivo processes. Although the excluded-volume effects of macromolecular crowding are expected to cause compaction of unfolded and disordered proteins, the extent of this effect is uncertain. We use a coarse-grained model to represent proteins with varying sequence content and directly observe changes in chain dimensions in the presence of purely repulsive spherical crowders. We find that the extent of crowding-induced compaction is dependent not only on crowder size and concentration, but also on the properties of the protein itself. In fact, we observe a nonmonotonic trend between the dimensions of the polypeptide chain in bulk and the degree of compaction: the most extended chains experience up to 24% compaction, the most compact chains show virtually no change, and intermediate chains compress by up to 40% in size at a 40% crowder volume fraction. Free-volume theory combined with an impenetrable ellipsoidal representation of the chains predicts the crowding effects only for collapsed protein chains. An additional scaling factor, which can be easily computed from protein-crowder potential of mean force, corrects for the penetrability of extended chains and is sufficient to capture the observed nonmonotonic trend in compaction.
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