ArticleChembiochem : a European journal of chemical biology2020
Insights into Protein Stability in Cell Lysate by
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026Article
- Article
- What remains from living cells in bacterial lysate-based cell-free systems.Computational and structural biotechnology journal · 2023Review
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Monitoring protein unfolding transitions by NMR-spectroscopy.Journal of biomolecular NMR · 2022Article
- Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate.Chembiochem : a European journal of chemical biology · 2021Article
- Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020Article
- Utilizing functional cell-free extracts to dissect ribonucleoprotein complex biology at single-molecule resolution.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In living organisms, protein folding and function take place in an inhomogeneous, highly crowded environment possessing a concentration of diverse macromolecules of up to 400 g/L. It has been shown that the intracellular environment has a pronounced effect on the stability, dynamics and function of the protein under study, and has for this reason to be considered. However, most protein studies neglect the presence of these macromolecules. Consequently, we probe here the overall thermodynamic stability of cold shock protein B from Bacillus subtilis (BsCspB) in cell lysate. We found that an increase in cell lysate concentration causes a monotonic increase in the thermodynamic stability of BsCspB. This result strongly underlines the importance of considering the biological environment when inherent protein parameters are quantitatively determined. Moreover, we demonstrate that targeted application of
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Registered trials
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