ArticleProtein science : a publication of the Protein Society2015
Intracellular pH modulates quinary structure.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- Measurement of protein non-covalent interactions in buffer and cells.Magnetic resonance letters · 2025Article
- Effects of Macromolecular Cosolutes on the Kinetics of Huntingtin Aggregation Monitored by NMR Spectroscopy.The journal of physical chemistry letters · 2024Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditionsMagnetic resonance letters · 2023Review
- Revitalizing an important field in biophysics: The new frontiers of molecular crowding.Frontiers in molecular biosciences · 2023Article
- The Protein Unfolded State: One, No One and One Hundred Thousand.Journal of the American Chemical Society · 2022Review
- In-cell destabilization of a homodimeric protein complex detected by DEER spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Diffusive protein interactions in human versus bacterial cells.Current research in structural biology · 2020Article
- Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019Review
- Review
- Quinary interactions with an unfolded state ensemble.Protein science : a publication of the Protein Society · 2017Article
- Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.The journal of physical chemistry. B · 2017Article
- Cosolutes, Crowding, and Protein Folding Kinetics.The journal of physical chemistry. B · 2017Article
- A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.Protein science : a publication of the Protein Society · 2017Review
- In-cell NMR: a topical review.IUCrJ · 2017Review
- Cosolute and Crowding Effects on a Side-By-Side Protein Dimer.Biochemistry · 2017Article
- Protein charge determination and implications for interactions in cell extracts.Protein science : a publication of the Protein Society · 2017Article
- Transient protein-protein interactions perturbeLife · 2016Article
- Simple NMR methods for evaluating higher order structures of monoclonal antibody therapeutics with quinary structure.Journal of pharmaceutical and biomedical analysis · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NMR spectroscopy can provide information about proteins in living cells. pH is an important characteristic of the intracellular environment because it modulates key protein properties such as net charge and stability. Here, we show that pH modulates quinary interactions, the weak, ubiquitous interactions between proteins and other cellular macromolecules. We use the K10H variant of the B domain of protein G (GB1, 6.2 kDa) as a pH reporter in Escherichia coli cells. By controlling the intracellular pH, we show that quinary interactions influence the quality of in-cell (15) N-(1) H HSQC NMR spectra. At low pH, the quality is degraded because the increase in attractive interactions between E. coli proteins and GB1 slows GB1 tumbling and broadens its crosspeaks. The results demonstrate the importance of quinary interactions for furthering our understanding of protein chemistry in living cells.
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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.