ArticleBiophysical journal2013
Quantification of excluded volume effects on the folding landscape of Pseudomonas aeruginosa apoazurin in vitro.
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 27 papers.
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27 citing papers in PubMed, 60 citations in OpenAlex.
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- Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics.The journal of physical chemistry letters · 2023Article
- Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditionsMagnetic resonance letters · 2023Review
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate.Chembiochem : a European journal of chemical biology · 2021Article
- Macromolecular crowding modulates α-synuclein amyloid fiber growth.Biophysical journal · 2021Article
- Response to crowded conditions reveals compact nucleus for amyloid formation of folded protein.QRB discovery · 2021Article
- CYP2J2 Molecular Recognition: A New Axis for Therapeutic Design.Pharmacology & therapeutics · 2020Review
- Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders.Biomolecules · 2020Article
- Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder.Biomolecules · 2019Article
- Crowding-Induced Elongated Conformation of Urea-Unfolded Apoazurin: Investigating the Role of Crowder Shape in Silico.The journal of physical chemistry. B · 2019Article
- Lipid composition and macromolecular crowding effects on CYP2J2-mediated drug metabolism in nanodiscs.Protein science : a publication of the Protein Society · 2019Article
- Macromolecular Crowding Tunes Protein Stability by Manipulating Solvent Accessibility.Chembiochem : a European journal of chemical biology · 2019Article
- Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.Cellular and molecular life sciences : CMLS · 2018Review
- Protein shape modulates crowding effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Large cosolutes, small cosolutes, and dihydrofolate reductase activity.Protein science : a publication of the Protein Society · 2017Article
- Cosolutes, Crowding, and Protein Folding Kinetics.The journal of physical chemistry. B · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins fold and function inside cells that are crowded with macromolecules. Here, we address the role of the resulting excluded volume effects by in vitro spectroscopic studies of Pseudomonas aeruginosa apoazurin stability (thermal and chemical perturbations) and folding kinetics (chemical perturbation) as a function of increasing levels of crowding agents dextran (sizes 20, 40, and 70 kDa) and Ficoll 70. We find that excluded volume theory derived by Minton quantitatively captures the experimental effects when crowding agents are modeled as arrays of rods. This finding demonstrates that synthetic crowding agents are useful for studies of excluded volume effects. Moreover, thermal and chemical perturbations result in free energy effects by the presence of crowding agents that are identical, which shows that the unfolded state is energetically the same regardless of method of unfolding. This also underscores the two-state approximation for apoazurin's unfolding reaction and suggests that thermal and chemical unfolding experiments can be used in an interchangeable way. Finally, we observe increased folding speed and invariant unfolding speed for apoazurin in the presence of macromolecular crowding agents, a result that points to unfolded-state perturbations. Although the absolute magnitude of excluded volume effects on apoazurin is only on the order of 1-3 kJ/mol, differences of this scale may be biologically significant.
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