ArticleScientific reports2018
Ion-ion interactions in the denatured state contribute to the stabilization of CutA1 proteins.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Insights into the low-temperature adaptation of an enzyme as studied through ancestral sequence reconstruction.Protein science : a publication of the Protein Society · 2025Article
- Article
- Statistical and molecular dynamics (MD) simulation approach to investigate the role of intrinsically disordered regions of shikimate dehydrogenase in microorganisms surviving at different temperatures.Extremophiles : life under extreme conditions · 2020Article
- Evaluating the strengths of salt bridges in the CutA1 protein using molecular dynamic simulations: a comparison of different force fields.FEBS open bio · 2019Article
- Selection and analyses of variants of a designed protein suggest importance of hydrophobicity of partially buried sidechains for protein stability at high temperatures.Protein science : a publication of the Protein Society · 2019Article
- Confirmation of the formation of salt bridges in the denatured state of CutA1 protein using molecular dynamics simulations.Biophysics and physicobiology · 2019Article
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Authors and funding
4 authors.
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Abstract
In order to elucidate features of the denatured state ensembles that exist in equilibrium with the native state under physiological conditions, we performed 1.4-μs molecular dynamics (MD) simulations at 400 K and 450 K using the monomer subunits of three CutA1 mutants from Escherichia coli: an SH-free mutant (Ec0SH) with denaturation temperature (T
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