ArticleMethods in molecular biology (Clifton, N.J.)2020
Determining the Protective Activity of IDPs Under Partial Dehydration and Freeze-Thaw Conditions.
Article in Methods in molecular biology (Clifton, N.J.), 2020. 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, 6 citations in OpenAlex.
- A Group 6 LEA Protein Plays Key Roles in Tolerance to Water Deficit, and in Maintaining the Glassy State and Longevity of Seeds.Plant, cell & environment · 2025Article
- Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity.Scientific reports · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12.Biomolecules · 2022Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unlike for structured proteins, the study of intrinsically disordered proteins (IDPs) requires selection of ad hoc assays and strategies to characterize their dynamic structure and function. Late embryogenesis abundant (LEA) proteins are important plant IDPs closely related to water-deficit stress response. Diverse hypothetical functions have been proposed for LEA proteins, such as membrane stabilizers during cold stress, oxidative regulators acting as ion metal binding molecules, and protein protectants during dehydration and cold/freezing conditions. Here we present two detailed protocols to characterize IDPs with potential protein/enzyme protection activity under partial dehydration and freeze-thaw treatments.
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