ArticleProtein science : a publication of the Protein Society2019
Sequence composition versus sequence order in the cryoprotective function of an intrinsically disordered stress-response protein.
Article in Protein science : a publication of the Protein Society, 2019. 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, 11 citations in OpenAlex.
- The Emerging Role of the Salt Tolerance-Related Protein in the Abiotic Stress Response ofPlants (Basel, Switzerland) · 2025Review
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- The Effect of Positive Charge Distribution on the Cryoprotective Activity of Dehydrins.Biomolecules · 2022Article
- The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective.Biomolecules · 2022Review
- IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions-Insights from transcription factors.Protein science : a publication of the Protein Society · 2020Article
- Protecting Enzymes from Stress-Induced Inactivation.Biochemistry · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Intrinsically disordered stress proteins have been shown to act as chaperones, protecting proteins from damage caused by stresses such as freezing and thawing. Dehydration proteins (dehydrins) are intrinsically disordered stress proteins that are found in almost all land plants. They consist of a variable number of the short, semi-conserved, Y-, S-, and K-segments, with longer stretches of poorly conserved sequences in between. Previous studies have provided conflicting views on the details of the dehydrin cryoprotective mechanism of enzymes. Experiments with polyethylene glycol (PEG) have shown that PEG cryoprotective efficiency is the same as dehydrins of the same hydrodynamic radius, suggesting that the protein's disordered and polar nature is important, rather than the specific order of the residues. To further elucidate the mechanism, we created scrambled variants of the wild grape dehydrins K
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