ArticleProtein science : a publication of the Protein Society2013
Amide proton exchange of a dynamic loop in cell extracts.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Residue-Specific Signatures of Structural Water Identified by Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.Angewandte Chemie (International ed. in English) · 2026Article
- Insights into Protein Stability in Cell Lysate byChembiochem : a European journal of chemical biology · 2020Article
- Quinary interactions with an unfolded state ensemble.Protein science : a publication of the Protein Society · 2017Article
- Intracellular pH modulates quinary structure.Protein science : a publication of the Protein Society · 2015Article
- Hydrogen exchange of disordered proteins in Escherichia coli.Protein science : a publication of the Protein Society · 2015Article
- Quinary structure modulates protein stability in cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Measuring hydrogen exchange in proteins by selective water saturation in (1)H- (15)N SOFAST/BEST-type experiments: advantages and limitations.Journal of biomolecular NMR · 2014Article
- An osmolyte mitigates the destabilizing effect of protein crowding.Protein science : a publication of the Protein Society · 2014Article
- Residue level quantification of protein stability in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Impact of reconstituted cytosol on protein stability.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsic rates of exchange are essential parameters for obtaining protein stabilities from amide (1) H exchange data. To understand the influence of the intracellular environment on stability, one must know the effect of the cytoplasm on these rates. We probed exchange rates in buffer and in Escherichia coli lysates for the dynamic loop in the small globular protein chymotrypsin inhibitor 2 using a modified form of the nuclear magnetic resonance experiment, SOLEXSY. No significant changes were observed, even in 100 g dry weight L(-1) lysate. Our results suggest that intrinsic rates from studies conducted in buffers are applicable to studies conducted under cellular conditions.
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