ArticleBiophysical journal2009
Common crowding agents have only a small effect on protein-protein interactions.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 131 citations in OpenAlex.
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- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
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- Chemical Trends in Sample Preparation for Nucleic Acid Amplification Testing (NAAT): A Review.Biosensors · 2023Review
- The variable domain from dynamin-related protein 1 promotes liquid-liquid phase separation that enhances its interaction with cardiolipin-containing membranes.Protein science : a publication of the Protein Society · 2023Article
- Local and Large-Scale Conformational Dynamics in Unfolded Proteins and IDPs. I. Effect of Solvent Viscosity and Macromolecular Crowding.The journal of physical chemistry. B · 2023Article
- Chemical interactions modulate λProtein science : a publication of the Protein Society · 2023Article
- Phase separation and zinc-induced transition modulate synaptic distribution and association of autism-linked CTTNBP2 and SHANK3.Nature communications · 2022Article
- A genetically encoded BRET-based SARS-CoV-2 MCommunications chemistry · 2022Article
- An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement.Scientific reports · 2021Article
- Macromolecular crowding effects on the kinetics of opposing reactions catalyzed by alcohol dehydrogenase.Biochemistry and biophysics reports · 2021Article
- Cosolute modulation of protein oligomerization reactions in the homeostatic timescale.Biophysical journal · 2021Article
- DEPS-1 is required for piRNA-dependent silencing and PIWI condensate organisation in Caenorhabditis elegans.Nature communications · 2020Article
- Influence of crowding agents on the dynamics of a multidomain protein in its denatured state: a solvation approach.European biophysics journal : EBJ · 2020Article
- An in vitro mimic of in-cell solvation for protein folding studies.Protein science : a publication of the Protein Society · 2020Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Studies of protein-protein interactions, carried out in polymer solutions, are designed to mimic the crowded environment inside living cells. It was shown that crowding enhances oligomerization and polymerization of macromolecules. Conversely, we have shown that crowding has only a small effect on the rate of association of protein complexes. Here, we investigated the equilibrium effects of crowding on protein heterodimerization of TEM1-beta-lactamase with beta-lactamase inhibitor protein (BLIP) and barnase with barstar. We also contrasted these with the effect of crowding on the weak binding pair CyPet-YPet. We measured the association and dissociation rates as well as the affinities and thermodynamic parameters of these interactions in polyethylene glycol and dextran solutions. For TEM1-BLIP and for barnase-barstar, only a minor reduction in association rate constants compared to that expected based on solution viscosity was found. Dissociation rate constants showed similar levels of reduction. Overall, this resulted in a binding affinity that is quite similar to that in aqueous solutions. On the other hand, for the CyPet-YPet pair, aggregation, and not enhanced dimerization, was detected in polyethylene glycol solutions. The results suggest that typical crowding agents have only a small effect on specific protein-protein dimerization reactions. Although crowding in the cell results from proteins and other macromolecules, one may still speculate that binding in vivo is not very different from that measured in dilute solutions.
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