ArticleJournal of the American Chemical Society2010
Effects of proteins on protein diffusion.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
What it found
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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.
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Who cites it
105 citing papers in PubMed, 276 citations in OpenAlex.
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Engineering macromolecular crowding-driven amyloid-mineral hybrid scaffolds for enhanced bone regeneration.Bioactive materials · 2026Article
- Residue-level mapping of crowding effects on protein phase separation.Protein science : a publication of the Protein Society · 2026Article
- How does cytoplasmic crowding affect reaction rates?Molecular cell · 2026Review
- A new GFP chromophore analogue for detection of viscosity and cysteine with AND logic-gate-based fluorescence readout.Analytical and bioanalytical chemistry · 2025Article
- Ballistic diffusion fronts in biomolecular condensates.Nature nanotechnology · 2025Article
- GRAMMCell: Docking-based Cell Modeling Resource.Journal of molecular biology · 2025Article
- NMR Assessment of the High Order Structure of Biological Therapeutics in Erythrocytes Provides a Tool for Drug Delivery Design.Journal of the American Chemical Society · 2025Article
- Measurement of protein non-covalent interactions in buffer and cells.Magnetic resonance letters · 2025Article
- Structured Random Binding: a minimal model of protein-protein interactions.bioRxiv : the preprint server for biology · 2025Article
- Article
- (Macro)Molecular Crowding Effects Beyond Volume Exclusion.Sub-cellular biochemistry · 2025Review
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Diffusion and Viscosity in Mixed Protein Solutions.The journal of physical chemistry. B · 2024Article
- Article
- Dynamics of Single-Chain Nanoparticles under Crowding: A Neutron Spin Echo Study.Macromolecules · 2024Article
- Entropy Tug-of-War Determines Solvent Effects in the Liquid-Liquid Phase Separation of a Globular Protein.The journal of physical chemistry letters · 2024Article
- What determines sub-diffusive behavior in crowded protein solutions?Biophysical journal · 2024Article
- Time-Resolved X-ray Observation of Intracellular Crystallized Protein in Living Animal.International journal of molecular sciences · 2023Article
45 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Despite increased attention, little is known about how the crowded intracellular environment affects basic phenomena like protein diffusion. Here, we use NMR to quantify the rotational and translational diffusion of a 7.4-kDa test protein, chymotrypsin inhibitor 2 (CI2), in solutions of glycerol, synthetic polymers, proteins, and cell lysates. As expected, translational diffusion and rotational diffusion decrease with increasing viscosity. In glycerol, for example, the decrease follows the Stokes-Einstein and Stokes-Einstein-Debye laws. Synthetic polymers cause negative deviation from the Stokes laws and affect translation more than rotation. Surprisingly, however, protein crowders have the opposite effect, causing positive deviation and reducing rotational diffusion more than translational diffusion. Indeed, bulk proteins severely attenuate the rotational diffusion of CI2 in crowded protein solutions. Similarly, CI2 diffusion in cell lysates is comparable to its diffusion in crowded protein solutions, supporting the biological relevance of the results. The rotational attenuation is independent of the size and total charge of the crowding protein, suggesting that the effect is general. The difference between the behavior of synthetic polymers and protein crowders suggests that synthetic polymers may not be suitable mimics of the intracellular environment. NMR relaxation data reveal that the source of the difference between synthetic polymers and proteins is the presence of weak interactions between the proteins and CI2. In summary, weak but nonspecific, noncovalent chemical interactions between proteins appear to fundamentally impact protein diffusion in cells.
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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.