Hydration in Deep Eutectic Solvents Induces Non-monotonic Changes in the Conformation and Stability of Proteins
Adrian Sanchez-Fernandez, Medina Basic, Jenny Xiang, Sylvain Prévost, Andrew Jackson, Cedric Dicko
Abstract
O is required to recover the native folding fully. The half-denaturation temperature of the protein increases with decreasing hydration, but even the dilute DESs significantly enhance the thermal stability of bovine serum albumin. Also, protein unfolding can be reversed by rehydrating the sample to the high hydration regime, also recovering protein function. This correlation provides a new perspective to understanding protein behavior in hydrated DESs, where quantifying the DES hydration becomes imperative to identifying the folding and stability of proteins.
Topics & Concepts
ChemistryEutectic systemMonotonic functionStability (learning theory)Chemical engineeringComputational chemistryCrystallographyEngineeringMathematical analysisComputer scienceMathematicsMicrostructureMachine learningAnalytical Chemistry and ChromatographyIonic liquids properties and applicationsCrystallization and Solubility Studies