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Entropy and Solvation02:05

Entropy and Solvation

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The process of surrounding a solute with solvent is called solvation. It involves evenly distributing the solute within the solvent. The rule of thumb for determining a solvent for a given compound is that like dissolves like. A good solvent has molecular characteristics similar to those of the compound to be dissolved. For example, polar solutions dissolve polar solutes, and apolar solvents dissolve apolar solutes. A polar solvent is a solvent that has a high dielectric constant (ϵ...
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Solvating Effects02:12

Solvating Effects

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An understanding of the solvating effect helps rationalize the relation between solvation and acidity of the compound. In addition, this also explains the relative stability of conjugate bases for compounds with different pKa values. This lesson details, in-depth, the principle of solvating effects. The strength of an acid and the stability of its corresponding conjugate base are determined using pKa values. This observed relationship is a consequence of solvation, which is the interaction...
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Regioselectivity and Stereochemistry of Acid-Catalyzed Hydration02:34

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The rate of acid-catalyzed hydration of alkenes depends on the alkene's structure, as the presence of alkyl substituents at the double bond can significantly influence the rate.
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Chemical and Solubility Equilibria02:21

Chemical and Solubility Equilibria

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The free energy change associated with dissolving a solute in a liter of solvent is called the free energy of a solution, ΔGsolution. The overall ΔGsolution is expressed as the balance of ΔGinteraction against the always-favorable free-energy of mixing, ΔGmixing. Solution formation is favorable if  ΔGsolution is less than zero, whereas it is unfavorable if ΔGsolution is greater than zero. In short, for a solution to form and complete dissolution to take place,...
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Energetics of Solution Formation02:35

Energetics of Solution Formation

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The formation of a solution is an example of a spontaneous process, which is a process that occurs under specified conditions without energy from some external source.
When the strengths of the intermolecular forces of attraction between solute and solvent species in a solution are no different than those present in the separated components, the solution is formed with no accompanying energy change. Formation of the solution requires the solute–solute and solvent–solvent...
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Solubility03:00

Solubility

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Solution, Solubility, and Solubility Equilibrium
A solution is a homogeneous mixture composed of a solvent, the major component, and a solute, the minor component. The physical state of a solution—solid, liquid, or gas—is typically the same as that of the solvent. Solute concentrations are often described with qualitative terms such as dilute (of relatively low concentration) and concentrated (of relatively high concentration).
In a solution, the solute particles (molecules,...
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Updated: Jul 8, 2025

Preparation of Binary and Ternary Deep Eutectic Systems
06:15

Preparation of Binary and Ternary Deep Eutectic Systems

Published on: October 31, 2019

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Protein stability in a natural deep eutectic solvent: Preferential hydration or solvent slaving?

Inês Gomes1, Nuno Galamba1

  • 1BioISI-Biosystems and Integrative Sciences Institute, Faculty of Sciences of the University of Lisbon, C8, Campo Grande, 1749-016 Lisbon, Portugal.

The Journal of Chemical Physics
|December 15, 2023
PubMed
Summary

Deep eutectic solvents (DESs) stabilize proteins by kinetically hindering fluctuations, not through traditional hydration mechanisms. This study explores ubiquitin stability in a betaine-glycerol-water DES, revealing suppressed dynamics and enhanced thermal stability.

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Materials Science

Background:

  • Deep eutectic solvents (DESs) are emerging as promising alternatives for biomolecular applications, including cryopreservation.
  • Understanding protein behavior in DESs is crucial for optimizing their use in stabilizing biological molecules.
  • Traditional models of protein stabilization often rely on hydration layer dynamics, which may differ in DES environments.

Purpose of the Study:

  • To investigate the stability and dynamics of ubiquitin, a small protein, in a betaine-glycerol-water (B:G:W) DES across varying water concentrations.
  • To elucidate the underlying mechanisms of protein stabilization within DESs using molecular dynamics simulations.
  • To develop and validate an AMBER-based model for accurately simulating DES properties like density and viscosity.

Main Methods:

  • Molecular dynamics (MD) simulations were employed to study ubiquitin in water and B:G:W DES mixtures (1:2:ζ; ζ = 0, 1, 2, 5, 10).
  • An AMBER-based force field model was developed and validated against experimental density and shear viscosity data.
  • Analysis focused on protein structural fluctuations, hydration patterns, and backbone dynamics to understand stabilization effects.

Main Results:

  • Water molecules in the B:G:W DES were found to be largely trapped, limiting the formation of complete protein hydration layers.
  • Ubiquitin remained stable in the DES, exhibiting suppressed structural fluctuations that recovered with increased hydration.
  • A significant enhancement in the protein's thermal stability was observed in the DES, attributed to slowed backbone torsional dynamics.

Conclusions:

  • The study supports kinetic stabilization of proteins in DESs, driven by suppressed dynamics rather than preferential hydration.
  • A solvent-slaving mechanism involving beta-fluctuations and non-monotonic amino acid hydration explains protein behavior in aqueous DESs.
  • The findings challenge conventional stabilization mechanisms and highlight the unique role of DESs in biomolecular preservation.