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- W3213131457 endingPage "406" @default.
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- W3213131457 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." @default.
- W3213131457 created "2021-11-22" @default.
- W3213131457 creator A5032416669 @default.
- W3213131457 creator A5053729838 @default.
- W3213131457 creator A5057354115 @default.
- W3213131457 creator A5076371120 @default.
- W3213131457 creator A5082593650 @default.
- W3213131457 date "2021-11-24" @default.
- W3213131457 modified "2023-10-17" @default.
- W3213131457 title "Protection by desiccation‐tolerance proteins probed at the residue level" @default.
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- W3213131457 doi "https://doi.org/10.1002/pro.4231" @default.
- W3213131457 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34766407" @default.
- W3213131457 hasPublicationYear "2021" @default.
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