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Trifluoroethanol and the behavior of a tardigrade desiccation-tolerance protein.
Wang, Shikun; Eicher, Jonathan; Pielak, Gary J.
Afiliación
  • Wang S; Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
  • Eicher J; Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
  • Pielak GJ; Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
Protein Sci ; 32(8): e4716, 2023 08.
Article en En | MEDLINE | ID: mdl-37401908
ABSTRACT
The cosolvent 2,2,2-trifluoroethanol (TFE) is often used to mimic protein desiccation. We assessed the effects of TFE on cytosolic abundant heat soluble protein D (CAHS D) from tardigrades. CAHS D is a member of a unique protein class that is necessary and sufficient for tardigrades to survive desiccation. We find that the response of CAHS D to TFE depends on the concentration of both species. Dilute CAHS D remains soluble and, like most proteins exposed to TFE, gains α-helix. More concentrated solutions of CAHS D in TFE accumulate ß-sheet, driving both gel formation and aggregation. At even higher TFE and CAHS D concentrations, samples phase separate without aggregation or increases in helix. Our observations show the importance of considering protein concentration when using TFE.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Trifluoroetanol / Tardigrada Límite: Animals Idioma: En Revista: Protein Sci Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Trifluoroetanol / Tardigrada Límite: Animals Idioma: En Revista: Protein Sci Asunto de la revista: BIOQUIMICA Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos