ArticleProtein science : a publication of the Protein Society2024
Structural adaptability and surface activity of peptides derived from tardigrade proteins.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Screening of Xeroprotectants for Efficient Mammalian Cell Structural Preservation in Dry Conditions.ACS omega · 2026Article
- Tardigrade-Derived Strategy for Low-Cost Storage of Cell-Free Expression Lysates.ACS synthetic biology · 2026Article
- Diversity in the protective role(s) of the conserved motif 1 from tardigrade cytoplasmic-abundant heat-soluble proteins during drying.Protein science : a publication of the Protein Society · 2025Article
- Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024Article
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14 authors.
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Abstract
Tardigrades are unique micro-organisms with a high tolerance to desiccation. The protection of their cells against desiccation involves tardigrade-specific proteins, which include the so-called cytoplasmic abundant heat soluble (CAHS) proteins. As a first step towards the design of peptides capable of mimicking the cytoprotective properties of CAHS proteins, we have synthesized several model peptides with sequences selected from conserved CAHS motifs and investigated to what extent they exhibit the desiccation-induced structural changes of the full-length proteins. Using circular dichroism spectroscopy, two-dimensional infrared spectroscopy, and molecular dynamics simulations, we have found that the CAHS model peptides are mostly disordered, but adopt a more
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