The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Proline inhibits aggregation during protein refolding
Open accessAbstract
The in vitro refolding of hen egg‐white lysozyme is studied in the presence of various osmolytes. Proline is found to prevent aggregation during protein refolding. However, other osmolytes used in this study fail to exhibit a similar property. Experimental evidence suggests that proline inhibits protein aggregation by binding to folding intermediate(s) and trapping the folding intermediate(s) into enzymatically inactive, “aggregation‐insensitive” state(s). However, elimination of proline from the refolded protein mixture results in significant recovery of the bacteriolytic activity. At higher concentrations (>1.5 M), proline is shown to form loose, higher‐order molecular aggregate(s). The supramolecular assembly of proline is found to possess an amphipathic character. Formation of higher‐order aggregates is believed to be crucial for proline to function as a protein folding aid. In addition to its role in osmoregulation under water stress conditions, the results of this study hint at the possibility of proline behaving as a protein folding chaperone.
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
Lin, T.-Y., & Timasheff, S. N. (1994) · Biochemistry · doi:10.1021/bi00208a021 · Cited by 371 · cited 1×
“Under conditions of osmotic equilibrium, reduced water activity is believed to be a crucial factor for stability of enzymes and other cellular components~Lin & Timasheff, 1994!.”
Background
Cited by
Understanding plant responses to drought—from genes to the whole plant.
Chaves, M. M., Maroco, J. P., & Pereira, J. S. (2003) · Functional Plant Biology · doi:10.1071/fp02076 · Cited by 3,845
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
Singh, A., Upadhyay, V., Upadhyay, A. K., Singh, S. M., & Panda, A. K. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0222-8 · Cited by 444
Refolding Techniques for Recovering Biologically Active Recombinant Proteins from Inclusion Bodies
Yamaguchi, H., & Miyazaki, M. (2014) · Biomolecules · doi:10.3390/biom4010235 · Cited by 251
Metadata
- Authors
- Samuel, D., Ganesh, G., Yang, P., Chang, M., Wang, S., Hwang, K., Yu, C., Jayaraman, G., Kumar, T. K. S., Trivedi, V. D., & Chang, D.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2000-01
- Volume
- 9
- Issue
- 2
- Pages
- 344-352
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2106275356
- Cited by
- 302
- References
- 1
- FWCI
- 1.58
- Type
- journal article
- Language
- en
- Open access
- bronze
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Proline inhibits aggregation during protein refolding. https://app.cochat.ai/papers/10.1110/ps.9.2.344
- The paper
- Samuel, D., Ganesh, G., Yang, P., Chang, M., Wang, S., Hwang, K., Yu, C., Jayaraman, G., Kumar, T. K. S., Trivedi, V. D., & Chang, D. (2000). Proline inhibits aggregation during protein refolding. Protein Science. https://doi.org/10.1110/ps.9.2.344
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.
