ArticleProtein science : a publication of the Protein Society2022
Protection by desiccation-tolerance proteins probed at the residue level.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Fibril Structure of Desiccation-Protective Tardigrade Protein CAHS-8.Angewandte Chemie (International ed. in English) · 2026Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- LEA_4 motifs function alone and in conjunction with synergistic cosolutes to protect a labile enzyme during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Protective roles of highly conserved motif 1 in tardigrade cytosolic-abundant heat soluble protein in extreme environments.Protein science : a publication of the Protein Society · 2024Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
- Trifluoroethanol and the behavior of a tardigrade desiccation-tolerance protein.Protein science : a publication of the Protein Society · 2023Article
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- Properties of a tardigrade desiccation-tolerance protein aerogel.Biophysical journal · 2023Article
- How Sugars Protect Dry Protein Structure.Biochemistry · 2023Article
- Secondary structure and stability of a gel-forming tardigrade desiccation-tolerance protein.Protein science : a publication of the Protein Society · 2022Article
- Desiccation-tolerance and globular proteins adsorb similar amounts of water.Protein science : a publication of the Protein Society · 2022Article
- Natural and Designed Proteins Inspired by Extremotolerant Organisms Can Form Condensates and Attenuate Apoptosis in Human Cells.ACS synthetic biology · 2022Article
- Protection by desiccation-tolerance proteins probed at the residue level.Protein science : a publication of the Protein Society · 2022Article
- Expression of tardigrade disordered proteins impacts the tolerance to biofuels in a model cyanobacteriumFrontiers in microbiology · 2022Article
Corrections and comments
- Erratum issuedErratum.2022
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Extremotolerant organisms from all domains of life produce protective intrinsically disordered proteins (IDPs) in response to desiccation stress. In vitro, many of these IDPs protect enzymes from dehydration stress better than U.S. Food and Drug Administration-approved excipients. However, as with most excipients, their protective mechanism is poorly understood. Here, we apply thermogravimetric analysis, differential scanning calorimetry, and liquid-observed vapor exchange (LOVE) NMR to study the protection of two model globular proteins (the B1 domain of staphylococcal protein G [GB1] and chymotrypsin inhibitor 2 [CI2]) by two desiccation-tolerance proteins (CAHS D from tardigrades and PvLEA4 from an anhydrobiotic midge), as well as by disordered and globular protein controls. We find that all protein samples retain similar amounts of water and possess similar glass transition temperatures, suggesting that neither enhanced water retention nor vitrification is responsible for protection. LOVE NMR reveals that IDPs protect against dehydration-induced unfolding better than the globular protein control, generally protect the same regions of GB1 and CI2, and protect GB1 better than CI2. These observations suggest that electrostatic interactions, charge patterning, and expanded conformations are key to protection. Further application of LOVE NMR to additional client proteins and protectants will deepen our understanding of dehydration protection, enabling the streamlined production of dehydrated proteins for expanded use in the medical, biotechnology, and chemical industries.
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Registered trials
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.