ArticleScientific reports2020
The change of conditions does not affect Ros87 downhill folding mechanism.
Article in Scientific reports, 2020. 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, 5 citations in OpenAlex.
- A Glimpse in the Metal Ion Selectivity Rules: Zn(II), Cd(II) and Co(II) Interplay With Different Protein Coordination Spheres in Determining Variable Thermal Stability and Folding Scenarios.Bioinorganic chemistry and applications · 2026Article
- MucR fromInternational journal of molecular sciences · 2023Article
- The Ros/MucR Zinc-Finger Protein Family in Bacteria: Structure and Functions.International journal of molecular sciences · 2022Review
- Copper (I) or (II) Replacement of the Structural Zinc Ion in the Prokaryotic Zinc Finger Ros Does Not Result in a Functional Domain.International journal of molecular sciences · 2022Article
- Insights into Fluctuations of Structure of Proteins: Significance of Intermediary States in Regulating Biological Functions.Polymers · 2022Review
- Structural characterization of the thermal unfolding pathway of human VEGFR1 D2 domain.The FEBS journal · 2022Article
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Downhill folding has been defined as a unique thermodynamic process involving a conformations ensemble that progressively loses structure with the decrease of protein stability. Downhill folders are estimated to be rather rare in nature as they miss an energetically substantial folding barrier that can protect against aggregation and proteolysis. We have previously demonstrated that the prokaryotic zinc finger protein Ros87 shows a bipartite folding/unfolding process in which a metal binding intermediate converts to the native structure through a delicate barrier-less downhill transition. Significant variation in folding scenarios can be detected within protein families with high sequence identity and very similar folds and for the same sequence by varying conditions. For this reason, we here show, by means of DSC, CD and NMR, that also in different pH and ionic strength conditions Ros87 retains its partly downhill folding scenario demonstrating that, at least in metallo-proteins, the downhill mechanism can be found under a much wider range of conditions and coupled to other different transitions. We also show that mutations of Ros87 zinc coordination sphere produces a different folding scenario demonstrating that the organization of the metal ion core is determinant in the folding process of this family of proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.