ArticleProceedings of the National Academy of Sciences of the United States of America2015
Quinary structure modulates protein stability in cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.
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Who cites it
94 citing papers in PubMed.
- Predicting Protein-Protein Interactions from Machine-Learned Representations.Advances in experimental medicine and biology · 2026Review
- Weak, specific chemical interactions dictate barnase stability in diverse cellular environments.Protein science : a publication of the Protein Society · 2025Article
- Measurement of protein non-covalent interactions in buffer and cells.Magnetic resonance letters · 2025Article
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- Enzymes in a human cytoplasm model organize into submetabolon complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- RNA Structure: Past, Future, and Gene Therapy Applications.International journal of molecular sciences · 2024Review
- Diffusion and Viscosity in Mixed Protein Solutions.The journal of physical chemistry. B · 2024Article
- Probing Electrostatic and Hydrophobic Associative Interactions in Cells.The journal of physical chemistry. B · 2024Article
- Transient Structural Properties of the Rho GDP-Dissociation Inhibitor.Angewandte Chemie (International ed. in English) · 2024Article
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- Progress, Challenges and Opportunities of NMR and XL-MS for Cellular Structural Biology.JACS Au · 2024Review
- Ligand-Based Competition Binding by Real-TimeJournal of medicinal chemistry · 2024Article
- In vivo-like nearest neighbor parameters improve prediction of fractional RNA base-pairing in cells.Nucleic acids research · 2023Article
- Protein translational diffusion as a way to detect intermolecular interactions.Biophysical reviews · 2023Review
- In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution.Nature chemical biology · 2023Article
- Intracellular environment can change protein conformational dynamics in cells through weak interactions.Science advances · 2023Article
- Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail.The journal of physical chemistry. B · 2023Article
- Crowded environments tune the fold-switching in metamorphic proteins.Communications chemistry · 2023Article
- Rock, scissors, paper: How RNA structure informs function.The Plant cell · 2023Article
- Shedding light on the base-pair opening dynamics of nucleic acids in living human cells.Nature communications · 2022Article
34 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
Protein quinary interactions organize the cellular interior and its metabolism. Although the interactions stabilizing secondary, tertiary, and quaternary protein structure are well defined, details about the protein-matrix contacts that comprise quinary structure remain elusive. This gap exists because proteins function in the crowded cellular environment, but are traditionally studied in simple buffered solutions. We use NMR-detected H/D exchange to quantify quinary interactions between the B1 domain of protein G and the cytosol of Escherichia coli. We demonstrate that a surface mutation in this protein is 10-fold more destabilizing in cells than in buffer, a surprising result that firmly establishes the significance of quinary interactions. Remarkably, the energy involved in these interactions can be as large as the energies that stabilize specific protein complexes. These results will drive the critical task of implementing quinary structure into models for understanding the proteome.
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