Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Solubility03:00

Solubility

21.3K
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,...
21.3K
Intermolecular Forces03:13

Intermolecular Forces

73.1K
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...
73.1K
Entropy and Solvation02:05

Entropy and Solvation

8.6K
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...
8.6K
Intermolecular Forces in Solutions02:28

Intermolecular Forces in Solutions

40.1K
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,...
40.1K
Chemical and Solubility Equilibria02:21

Chemical and Solubility Equilibria

5.1K
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,...
5.1K
Energetics of Solution Formation02:35

Energetics of Solution Formation

7.6K
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...
7.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Editorial for Special Issue "Recombinant Proteins for Molecular Biology Research: Technologies and Applications".

Current issues in molecular biology·2026
Same author

Parameter optimization for circular dichroism spectroscopy of proteins: A practical approach for rapid acquisition of high-quality spectra.

Analytical biochemistry·2026
Same author

A robust and sensitive method for detecting subtle structural differences in bovine serum albumin.

BioTechniques·2026
Same author

Effects of Arginine on Hierarchical Protein Aggregation.

The protein journal·2026
Same author

Differences and Similarities in Protein and Nucleic Acid Structures and Their Biological Interactions.

Current issues in molecular biology·2026
Same author

Non-ionic Detergent-Assisted Refolding of Protein from Protein-SDS Complex.

The protein journal·2025

Related Experiment Video

Updated: Feb 17, 2026

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
05:08

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid

Published on: September 20, 2017

17.7K

Protein-solvent interaction.

Tsutomu Arakawa1

  • 1Alliance Protein Laboratories, a Division of KBI Biopharma, 6042 Cornerstone Court West, San Diego, CA, 92121, USA. tarakawa@kbibiopharma.com.

Biophysical Reviews
|December 4, 2017
PubMed
Summary
This summary is machine-generated.

High concentrations of co-solvents can control protein folding and assembly in vitro. These co-solvents are excluded from protein surfaces, enhancing protein stability and assembly.

Keywords:
Co-solventsDialysis equilibriumIn vitro systemsPreferentially excluded co-solventsProtein folding and assembly

More Related Videos

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.4K
Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
08:38

Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro

Published on: August 14, 2011

22.6K

Related Experiment Videos

Last Updated: Feb 17, 2026

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
05:08

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid

Published on: September 20, 2017

17.7K
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

9.4K
Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
08:38

Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro

Published on: August 14, 2011

22.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Science

Background:

  • Protein folding and assembly are crucial biological processes.
  • In vitro manipulation of these processes is important for research and applications.
  • Co-solvents are known to influence protein behavior.

Purpose of the Study:

  • To investigate the role of co-solvents in protein folding and assembly.
  • To understand the mechanism by which co-solvents affect protein stability and assembly.

Main Methods:

  • Utilizing in vitro systems with high concentrations of co-solvents.
  • Employing dialysis experiments to study co-solvent exclusion from protein surfaces.

Main Results:

  • Co-solvents at high concentrations can manipulate protein folding and assembly.
  • Co-solvent exclusion from the protein surface was demonstrated.
  • Co-solvent exclusion was correlated with enhanced protein stability and assembly.

Conclusions:

  • Co-solvent exclusion is a key mechanism for enhancing protein stability and assembly in vitro.
  • This finding has implications for controlling protein behavior in biochemical and biotechnological applications.