ArticleProceedings of the National Academy of Sciences of the United States of America2016
In-cell thermodynamics and a new role for protein surfaces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
68 citing papers in PubMed.
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
- Marginal Stability of the YB1 Cold-Shock Domain in Cells Enables Binding of Multiple Nucleic Acids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Computational and Experimental Approaches and Applications of Biological NMR.Advances in experimental medicine and biology · 2026Review
- Water Under Molecular Crowding: From Femtosecond H-Bond Networks Dynamics to Biological Function.Sub-cellular biochemistry · 2026Review
- Glycopolymers stabilize protein folding and protein-protein interactions via enthalpic interactions.Protein science : a publication of the Protein Society · 2026Article
- Rational design ofNature communications · 2025Article
- Weak, specific chemical interactions dictate barnase stability in diverse cellular environments.Protein science : a publication of the Protein Society · 2025Article
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Progress, Challenges and Opportunities of NMR and XL-MS for Cellular Structural Biology.JACS Au · 2024Review
- Macromolecular Crowding and DNA: Bridging the Gap between In Vitro and In Vivo.International journal of molecular sciences · 2023Review
- 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
- In silico protein dynamics in the human cytoplasm: Partial folding, misfolding, fold switching, and non-native interactions.Protein science : a publication of the Protein Society · 2023Article
- Systematic conformation-to-phenotype mapping via limited deep sequencing of proteins.Molecular cell · 2023Article
- Article
- Direct Expression of Fluorinated Proteins in Human Cells forJournal of the American Chemical Society · 2023Article
- Shedding light on the base-pair opening dynamics of nucleic acids in living human cells.Nature communications · 2022Article
- Measuring Structural Changes in CytochromePolymers · 2022Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
8 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
5 authors.
Funding
Abstract
There is abundant, physiologically relevant knowledge about protein cores; they are hydrophobic, exquisitely well packed, and nearly all hydrogen bonds are satisfied. An equivalent understanding of protein surfaces has remained elusive because proteins are almost exclusively studied in vitro in simple aqueous solutions. Here, we establish the essential physiological roles played by protein surfaces by measuring the equilibrium thermodynamics and kinetics of protein folding in the complex environment of living Escherichia coli cells, and under physiologically relevant in vitro conditions. Fluorine NMR data on the 7-kDa globular N-terminal SH3 domain of Drosophila signal transduction protein drk (SH3) show that charge-charge interactions are fundamental to protein stability and folding kinetics in cells. Our results contradict predictions from accepted theories of macromolecular crowding and show that cosolutes commonly used to mimic the cellular interior do not yield physiologically relevant information. As such, we provide the foundation for a complete picture of protein chemistry in cells.
Indexed as
Identifiers
What OpenQuestion holds
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.