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Related Concept Videos

Intermolecular Forces in Solutions02:28

Intermolecular Forces in Solutions

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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,...
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Intermolecular Forces03:13

Intermolecular Forces

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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...
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Intermolecular vs Intramolecular Forces03:00

Intermolecular vs Intramolecular Forces

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Intermolecular forces (IMF) are electrostatic attractions arising from charge-charge interactions between molecules. The strength of the intermolecular force is influenced by the distance of separation between molecules. The forces significantly affect the interactions in solids and liquids, where the molecules are close together. In gases, IMFs become important only under high-pressure conditions (due to the proximity of gas molecules). Intermolecular forces dictate the physical properties of...
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Ideal Solutions02:24

Ideal Solutions

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According to Raoult’s law, the partial vapor pressure of a solvent in a solution is equal or identical to the vapor pressure of the pure solvent multiplied by its mole fraction in the solution. However, Raoult's Law is only valid for ideal solutions. For a solution to be ideal, the solvent-solute interaction must be just as strong as a solvent-solvent or solute-solute interaction. This suggests that both the solute and the solvent would use the same amount of energy to escape to the...
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Comparing Intermolecular Forces: Melting Point, Boiling Point, and Miscibility02:34

Comparing Intermolecular Forces: Melting Point, Boiling Point, and Miscibility

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Intermolecular forces are attractive forces that exist between molecules. They dictate several bulk properties, such as melting points, boiling points, and solubilities (miscibilities) of substances. Molar mass, molecular shape, and polarity affect the strength of different intermolecular forces, which influence the magnitude of physical properties across a family of molecules.
Temporary attractive forces like dispersion are present in all molecules, whether they are polar or nonpolar. They...
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Solution Formation02:16

Solution Formation

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There is no one solvent that can dissolve every type of solute. Some substances that readily dissolve in a certain solvent might be insoluble in a different solvent. A simple way to predict which substances dissolve in which solvent is the phrase "like dissolves like". This means that polar substances, such as salt and sugar, dissolve in a polar substance like water. In contrast, non-polar substances are more soluble in non-polar solvents such as carbon tetrachloride.
This selective...
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Related Experiment Video

Updated: Feb 5, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII

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INTERMOLECULAR INTERACTIONS IN THE SOLUTIONS OF SERUM ALBUMIN.

A M Polyanichko, N V Mikhailov, N M Romanov

    Tsitologiia
    |September 11, 2018
    PubMed
    Summary

    Investigating bovine serum albumin (BSA) aggregation revealed a dynamic equilibrium between monomers and aggregates. Changes in pH and urea concentration significantly influence protein complex formation and aggregate size.

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    Last Updated: Feb 5, 2026

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    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Physical Chemistry

    Background:

    • Intermolecular protein complex formation is crucial in biological systems.
    • Understanding protein aggregation mechanisms is vital for disease research and biotechnology.
    • Bovine serum albumin (BSA) serves as a model protein for studying protein behavior.

    Purpose of the Study:

    • To elucidate the mechanisms of intermolecular protein complex formation in bovine serum albumin (BSA).
    • To investigate the influence of protein concentration, pH, and urea concentration on BSA aggregation.
    • To characterize the dynamic equilibrium between BSA monomers and aggregates.

    Main Methods:

    • Dynamic Light Scattering (DLS) for aggregate size analysis.
    • Analytical Ultracentrifugation (AUC) for studying molecular எடை and interactions.
    • Polyacrylamide Gel Electrophoresis (PAG electrophoresis) for protein separation and analysis.

    Main Results:

    • A dynamic equilibrium exists between BSA monomers and aggregates in solution.
    • Decreasing pH (4.0–1.0) leads to an increase in aggregate sizes.
    • Low urea concentrations (below 2 M) reduce aggregate sizes, while higher concentrations promote larger aggregates due to protein unfolding.

    Conclusions:

    • Protein concentration, pH, and urea concentration are critical factors modulating BSA aggregation.
    • BSA aggregation is a reversible process influenced by solution conditions.
    • The study provides insights into protein complex formation and conformational changes.