ArticleBiophysical journal2013
Direct observation of protein unfolded state compaction in the presence of macromolecular crowding.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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Who cites it
30 citing papers in PubMed, 61 citations in OpenAlex.
- 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
- Effects of Molecular Crowding on the Structural, Dynamic, and Functional Properties of Biological Macromolecules: A General Overview.Sub-cellular biochemistry · 2025Review
- Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions.Communications chemistry · 2023Article
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Progress on Crowding Effect in Cell-like Structures.Membranes · 2022Review
- Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein.The journal of physical chemistry letters · 2022Article
- Article
- All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.Nature communications · 2020Article
- Liquid-Liquid Phase Separation in Crowded Environments.International journal of molecular sciences · 2020Review
- Influence of crowding agents on the dynamics of a multidomain protein in its denatured state: a solvation approach.European biophysics journal : EBJ · 2020Article
- Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders.Biomolecules · 2020Article
- Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.Journal of Parkinson's disease · 2020Review
- Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder.Biomolecules · 2019Article
- 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
- Cosolutes, Crowding, and Protein Folding Kinetics.The journal of physical chemistry. B · 2017Article
- Calcineurin in a Crowded World.Biochemistry · 2016Article
- A sensor for quantification of macromolecular crowding in living cells.Nature methods · 2015Article
- Beyond the excluded volume effects: mechanistic complexity of the crowded milieu.Molecules (Basel, Switzerland) · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins fold and function in cellular environments that are crowded with other macromolecules. As a consequence of excluded volume effects, compact folded states of proteins should be indirectly stabilized due to destabilization of extended unfolded conformations. Here, we assess the role of excluded volume in terms of protein stability, structural dimensions and folding dynamics using a sugar-based crowding agent, dextran 20, and the small ribosomal protein S16 as a model system. To specifically address dimensions, we labeled the protein with BODIPY at two positions and measured Trp-BODIPY distances under different conditions. As expected, we found that dextran 20 (200 mg/ml) stabilized the variants against urea-induced unfolding. At conditions where the protein is unfolded, Förster resonance energy transfer measurements reveal that in the presence of dextran, the unfolded ensemble is more compact and there is residual structure left as probed by far-ultraviolet circular dichroism. In the presence of a crowding agent, folding rates are faster in the two-state regime, and at low denaturant concentrations, a kinetic intermediate is favored. Our study provides direct evidence for protein unfolded-state compaction in the presence of macromolecular crowding along with its energetic and kinetic consequences.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.