ArticleBiochemistry2021
Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.
Article in Biochemistry, 2021. 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 10 papers.
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Who cites it
10 citing papers in PubMed.
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- Trimethylamine N-oxide (TMAO) doubly locks the hydrophobic core and surfaces of protein against desiccation stress.Protein science : a publication of the Protein Society · 2024Article
- Uniform trehalose nanogels for glucagon stabilization.RSC applied polymers · 2024Article
- Protecting Proteins from Desiccation Stress Using Molecular Glasses and Gels.Chemical reviews · 2024Review
- Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditionsMagnetic resonance letters · 2023Review
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- How Sugars Protect Dry Protein Structure.Biochemistry · 2023Article
- Desiccation-tolerance and globular proteins adsorb similar amounts of water.Protein science : a publication of the Protein Society · 2022Article
- Protection by desiccation-tolerance proteins probed at the residue level.Protein science : a publication of the Protein Society · 2022Article
- Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR.Biochemistry · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
Water is key to protein structure and stability, yet the relationship between protein-water interactions and structure is poorly understood, in part because there are few techniques that permit the study of dehydrated protein structure at high resolution. Here, we describe liquid-observed vapor exchange (LOVE) NMR, a solution NMR-based method that provides residue-level information about the structure of dehydrated proteins. Using the model protein GB1, we show that LOVE NMR measurements reflect the fraction of the dried protein population trapped in a conformation where a given residue is protected from exchange with D
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