ArticleProceedings of the National Academy of Sciences of the United States of America2018
Protein shape modulates crowding effects.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Programmable Electrostatics in Charge-Patterned Polypeptoid Micelles Probed by Small-Angle Neutron Scattering.Macromolecules · 2026Article
- Protein oxidation in crowded environments.The Biochemical journal · 2026Review
- Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.Protein science : a publication of the Protein Society · 2026Article
- Article
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- Crowding beyond excluded volume: A tale of two dimers.Protein science : a publication of the Protein Society · 2025Article
- Rational design of monomeric IL37 variants guided by stability and dynamical analyses of IL37 dimers.Computational and structural biotechnology journal · 2024Article
- Effects of Macromolecular Cosolutes on the Kinetics of Huntingtin Aggregation Monitored by NMR Spectroscopy.The journal of physical chemistry letters · 2024Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Probing macromolecular crowding at the lipid membrane interface with genetically-encoded sensors.Protein science : a publication of the Protein Society · 2023Article
- Not Always Sticky: Specificity of Protein Stabilization by Sugars Is Conferred by Protein-Water Hydrogen Bonds.Journal of the American Chemical Society · 2023Article
- Simulations of a protein fold switch reveal crowding-induced population shifts driven by disordered regions.Communications chemistry · 2023Article
- Crowded environments tune the fold-switching in metamorphic proteins.Communications chemistry · 2023Article
- Effects of Molecular Crowding and Betaine on HSPB5 Interactions, with Target Proteins Differing in the Quaternary Structure and Aggregation Mechanism.International journal of molecular sciences · 2022Article
- Preferential Regulation of Transient Protein-Protein Interaction by the Macromolecular Crowders.The journal of physical chemistry. B · 2022Article
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- Cleavage-Resistant Protein Labeling With Hydrophilic Trityl Enables Distance MeasurementsThe journal of physical chemistry. B · 2021Article
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Authors and funding
5 authors.
Funding
Abstract
Protein-protein interactions are usually studied in dilute buffered solutions with macromolecule concentrations of <10 g/L. In cells, however, the macromolecule concentration can exceed 300 g/L, resulting in nonspecific interactions between macromolecules. These interactions can be divided into hard-core steric repulsions and "soft" chemical interactions. Here, we test a hypothesis from scaled particle theory; the influence of hard-core repulsions on a protein dimer depends on its shape. We tested the idea using a side-by-side dumbbell-shaped dimer and a domain-swapped ellipsoidal dimer. Both dimers are variants of the B1 domain of protein G and differ by only three residues. The results from the relatively inert synthetic polymer crowding molecules, Ficoll and PEG, support the hypothesis, indicating that the domain-swapped dimer is stabilized by hard-core repulsions while the side-by-side dimer shows little to no stabilization. We also show that protein cosolutes, which interact primarily through nonspecific chemical interactions, have the same small effect on both dimers. Our results suggest that the shape of the protein dimer determines the influence of hard-core repulsions, providing cells with a mechanism for regulating protein-protein interactions.
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