ArticleChembiochem : a European journal of chemical biology2019
Macromolecular Crowding Tunes Protein Stability by Manipulating Solvent Accessibility.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
- Quantifying Ligand-to-Protein Distances in Complex Environments Using IntermolecularChembiochem : a European journal of chemical biology · 2026Article
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Pitfalls of Using ANS Dye Under Molecular Crowding Conditions.International journal of molecular sciences · 2024Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Crowded environments tune the fold-switching in metamorphic proteins.Communications chemistry · 2023Article
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Mutations in the regulatory regions result in increased streptomycin resistance and keratinase synthesis in Bacillus thuringiensis.Archives of microbiology · 2021Article
- Fluorine NMR Spectroscopy Enables to Quantify the Affinity Between DNA and Proteins in Cell Lysate.Chembiochem : a European journal of chemical biology · 2021Article
- Impact of crowded environments on binding between protein and single-stranded DNA.Scientific reports · 2021Article
- Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020Article
- All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.Nature communications · 2020Article
- Desiccation-induced cell damage in bacteria and the relevance for inoculant production.Applied microbiology and biotechnology · 2020Review
- Crowder-Induced Conformational Ensemble Shift in Escherichia coli Prolyl-tRNA Synthetase.Biophysical journal · 2019Article
- Macromolecular Crowding Tunes Protein Stability by Manipulating Solvent Accessibility.Chembiochem : a European journal of chemical biology · 2019Article
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2 authors.
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Abstract
In all intracellular processes, protein structure and dynamics are subject to the influence of macromolecular crowding (MC). Here, the impact of MC agents of different types and sizes on the model protein Bacillus subtilis Cold shock protein B (BsCspB) during both thermal and chemical denaturation have been comprehensively investigated. We consistently reveal a distinct stabilization of BsCspB in a manner dependent on the MC concentration but not on viscosity, polarity, or size of the MC agent used. This general stabilization has been decoded by use of NMR spectroscopy, through monitoring of chemical shift (CS) perturbations and the intramolecular hydrogen-bonding networks, as well as local protection of amide protons against exchange with solvent protons. Whereas CSs and hydrogen-bonding networks are not systematically affected in the presence of MC, we detected a pronounced reduction in exchange in loop regions of BsCspB. We conclude that this reduced accessibility of solvent protons is a key parameter for the increases in protein stability seen under MC.
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