The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein Crowding Tunes Protein Stability
Abstract
Thirty percent of a cell's volume is filled with macromolecules, and protein chemistry in a crowded environment is predicted to differ from that in dilute solution. We quantified the effect of crowding by globular proteins on the equilibrium thermodynamic stability of a small globular protein. Theory has long predicted that crowding should stabilize proteins, and experiments using synthetic polymers as crowders show such stabilizing effects. We find that protein crowders can be mildly destabilizing. The destabilization arises from a competition between stabilizing excluded-volume effects and destabilizing nonspecific interactions, including electrostatic interactions. This competition results in tunable stability, which could impact our understanding of the spatial and temporal roles of proteins in living systems.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Excluded volume as a determinant of macromolecular structure and reactivity
Minton, A. P. (1981) · Biopolymers · doi:10.1002/bip.1981.360201006 · Cited by 589
Cited by
Macromolecular Crowding In Vitro , In Vivo , and In Between
Rivas, G., & Minton, A. P. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.013 · Cited by 470
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Macromolecular Crowding and Protein Stability
Wang, Y., Sarkar, M., Smith, A. E., Krois, A. S., & Pielak, G. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305300m · Cited by 346
Self-citationRational design of 19F NMR labelling sites to probe protein structure and interactions
Streit, J. O., Chan, S. H. S., Daya, S., & Christodoulou, J. (2025) · Nature Communications · doi:10.1038/s41467-025-59105-6 · Cited by 17
Metadata
- Authors
- Miklos, A. C., Sarkar, M., Wang, Y., & Pielak, G. J.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-04-20
- Volume
- 133
- Issue
- 18
- Pages
- 7116-7120
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2325407743
- Cited by
- 296
- References
- 1
- FWCI
- 9.05
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
