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Related Concept Videos

Intermolecular Forces in Solutions02:28

Intermolecular Forces in Solutions

The formation of a solution is an example of a spontaneous process, 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. Such a solution is called an ideal solution. A mixture of ideal gases (or gases such as helium and argon,...
Energetics of Solution Formation02:35

Energetics of Solution Formation

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 electrostatic forces to...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Intermolecular Forces03:13

Intermolecular Forces

Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen bonds, and dispersion...
Chemical and Solubility Equilibria02:21

Chemical and Solubility Equilibria

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, the Gibbs energy change must be...
Aqueous Solutions and Heats of Hydration02:42

Aqueous Solutions and Heats of Hydration

Water and other polar molecules are attracted to ions. The electrostatic attraction between an ion and a molecule with a dipole is called an ion-dipole attraction. These attractions play an important role in the dissolution of ionic compounds in water.
When ionic compounds dissolve in water, the ions in the solid separate and disperse uniformly throughout the solution because water molecules surround and solvate the ions, reducing the strong electrostatic forces between them. This process...

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Related Experiment Video

Updated: May 24, 2026

Computation of Atmospheric Concentrations of Molecular Clusters from ab initio Thermochemistry
12:11

Computation of Atmospheric Concentrations of Molecular Clusters from ab initio Thermochemistry

Published on: April 8, 2020

Proximity energies: a framework for understanding concentrated solutions.

Tom Laue1

  • 1Molecular, Cellular and Biomedical Sciences, University of New Hampshire, Durham, NH, USA. tom.laue@unh.edu

Journal of Molecular Recognition : JMR
|March 13, 2012
PubMed
Summary

High concentration protein solutions (>100 mg/ml) are crucial for biopharmaceuticals. This study offers an energetic framework to understand and manipulate protein solubility, stability, and viscosity in these concentrated solutions.

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Spatial Separation of Molecular Conformers and Clusters
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Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

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Last Updated: May 24, 2026

Computation of Atmospheric Concentrations of Molecular Clusters from ab initio Thermochemistry
12:11

Computation of Atmospheric Concentrations of Molecular Clusters from ab initio Thermochemistry

Published on: April 8, 2020

Spatial Separation of Molecular Conformers and Clusters
10:37

Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

Area of Science:

  • Biophysics
  • Chemical Engineering
  • Materials Science

Background:

  • High-concentration fluids are defined by molecular distances comparable to molecular size.
  • Many biological fluids and high-concentration protein solutions (>100 mg/ml) are of commercial interest, particularly in the biopharmaceutical industry.

Purpose of the Study:

  • To establish an energetic framework for understanding the functional properties of high-concentration protein solutions.
  • To provide insights into how protein or solvent modifications impact solution behavior.

Main Methods:

  • Development of a theoretical energetic framework.
  • Analysis of protein behavior in concentrated solutions.

Main Results:

  • The framework offers a clear view of protein behavior at high concentrations.
  • It elucidates how protein and solvent modifications influence solubility, stability, and viscosity.

Conclusions:

  • The energetic framework serves as a foundation for rational manipulation of protein solubility, viscosity, and stability.
  • This approach aids in the development of advanced protein formulations for biopharmaceutical applications.