ArticleBiophysical journal2012
Contrasting factors on the kinetic path to protein complex formation diminish the effects of crowding agents.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Tackling the Antibiotic Resistance Caused by Class AInternational journal of molecular sciences · 2018Pooled it
- Modeling the Dynamics of Protein-Protein Interfaces, How and Why?Molecules (Basel, Switzerland) · 2022Review
- Preferential Interactions of a Crowder Protein with the Specific Binding Site of a Native Protein Complex.The journal of physical chemistry letters · 2022Article
- Potential Regulatory Role of Competitive Encounter Complexes in Paralogous Phosphotransferase Systems.Journal of molecular biology · 2019Article
- Transfer Free Energies of Test Proteins Into Crowded Protein Solutions Have Simple Dependence on Crowder Concentration.Frontiers in molecular biosciences · 2019Article
- Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Quantifying enzyme activity in living cells.The Journal of biological chemistry · 2017Article
- Protein folding, binding, and droplet formation in cell-like conditions.Current opinion in structural biology · 2017Review
- Low-stringency selection of TEM1 for BLIP shows interface plasticity and selection for faster binders.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Challenges in structural approaches to cell modeling.Journal of molecular biology · 2016Review
- Molecular crowding enhances facilitated diffusion of two human DNA glycosylases.Nucleic acids research · 2015Article
- Article
- Modeling protein association mechanisms and kinetics.Current opinion in structural biology · 2013Review
- Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins.The journal of physical chemistry letters · 2013Article
- Folding free energy surfaces of three small proteins under crowding: validation of the postprocessing method by direct simulation.Physical biology · 2013Article
- Simulation and Modeling of Crowding Effects on the Thermodynamic and Kinetic Properties of Proteins with Atomic Details.Biophysical reviews · 2013Article
- Formation of protein complexes in crowded environments--from in vitro to in vivo.FEBS letters · 2013Review
- Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.PloS one · 2013Article
- A method for computing association rate constants of atomistically represented proteins under macromolecular crowding.Physical biology · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The crowded environment of cells poses a challenge for rapid protein-protein association. Yet, it has been established that the rates of association are similar in crowded and in dilute solutions. Here we probe the pathway leading to fast association between TEM1 β-lactamase and its inhibitor protein BLIP in crowded solutions. We show that the affinity of the encounter complex, the rate of final complex formation, and the structure of the transition state are similar in crowded solutions and in buffer. The experimental results were reproduced by calculations based on the transient-complex theory for protein association. Both experiments and calculations suggest that while crowding agents decrease the diffusion constant of the associating proteins, they also induce an effective excluded-volume attraction between them. The combination of the two opposing effects thus results in nearly identical overall association rates in diluted and crowded solutions.
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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.