ArticleBiology2013
Thermodynamic stability of psychrophilic and mesophilic pheromones of the protozoan ciliate euplotes.
Article in Biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Bioactive molecules from ciliates: Structure, activity, and applicative potential.The Journal of eukaryotic microbiology · 2022Review
- Primary Structure and Coding Genes of Two Pheromones from the Antarctic Psychrophilic Ciliate,Microorganisms · 2022Article
- Structural prediction of a novel laminarinase from the psychrophilic Glaciozyma antarctica PI12 and its temperature adaptation analysis.Journal of molecular modeling · 2015Article
- Structural and functional analysis of a novel psychrophilic β-mannanase from Glaciozyma antarctica PI12.Journal of computer-aided molecular design · 2014Article
- Unfolding thermodynamics of cysteine-rich proteins and molecular thermal-adaptation of marine ciliates.Biomolecules · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three psychrophilic protein pheromones (En-1, En-2 and En-6) from the polar ciliate, Euplotes nobilii, and six mesophilic pheromones (Er-1, Er-2, Er-10, Er-11, Er-22 and Er-23) from the temperate-water sister species, Euplotes raikovi, were studied in aqueous solution for their thermal unfolding and refolding based on the temperature dependence of their circular dichroism (CD) spectra. The three psychrophilic proteins showed thermal unfolding with mid points in the temperature range 55-70 °C. In contrast, no unfolding was observed for any of the six mesophilic proteins and their regular secondary structures were maintained up to 95 °C. Possible causes of these differences are discussed based on comparisons of the NMR structures of the nine proteins.
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Registered trials
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