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Related Concept Videos

Factors Affecting Solubility04:01

Factors Affecting Solubility

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Compared with pure water, the solubility of an ionic compound is less in aqueous solutions containing a common ion (one also produced by dissolution of the ionic compound). This is an example of a phenomenon known as the common ion effect, which is a consequence of the law of mass action that may be explained using Le Chȃtelier’s principle. Consider the dissolution of silver iodide:
37.2K
Solubility Equilibria03:07

Solubility Equilibria

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Solubility equilibria are established when the dissolution and precipitation of a solute species occur at equal rates. These equilibria underlie many natural and technological processes, ranging from tooth decay to water purification. An understanding of the factors affecting compound solubility is, therefore, essential to the effective management of these processes. This section applies previously introduced equilibrium concepts and tools to systems involving dissolution and precipitation.
The...
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Destabilization of Microtubules01:45

Destabilization of Microtubules

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The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
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Solubility of Ionic Compounds02:55

Solubility of Ionic Compounds

68.3K
Solubility is the measure of the maximum amount of solute that can be dissolved in a given quantity of solvent at a given temperature and pressure. Solubility is usually measured in molarity (M) or moles per liter (mol/L). A compound is termed soluble if it dissolves in water.
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Physical Properties Affecting Solubility02:19

Physical Properties Affecting Solubility

26.6K
Solutions of Gases in Liquids
As for any solution, the solubility of a gas in a liquid is affected by the attractive intermolecular forces between solute and solvent species. Unlike solid and liquid solutes, however, there is no solute-solute intermolecular attraction to overcome when a gaseous solute dissolves in a liquid solvent since the atoms or molecules comprising a gas are far separated and experience negligible interactions. Consequently, solute-solvent interactions are the sole...
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Drugs that Destabilize Microtubules01:10

Drugs that Destabilize Microtubules

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Microtubules are dynamic structures and can be regulated by microtubule targeting agents (MTAs). Microtubule destabilizing drugs are a class of MTAs that destabilize and prevent microtubules' polymerization. Both natural and synthetic chemicals can be found under this class of drugs. Vincristine and vinblastine, two vinca alkaloids, and colchicine were among the first to be discovered. These drugs can affect cells in various ways, either by inducing a change in cell morphology, preventing...
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Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
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Soluble Zwitterionic Poly(sulfobetaine) Destabilizes Proteins.

Lydia Kisley, Kali A Miller, Caitlin M Davis

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    Summary

    Poly(sulfobetaine) (pSB) polymers interact with proteins, reducing thermal stability and altering folding. This challenges the assumption of pSB being universally protein-repellent for biomedical applications.

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    Area of Science:

    • Biomaterials Science
    • Polymer Chemistry
    • Protein Biochemistry

    Background:

    • Neutral, water-soluble polymers like poly(ethylene glycol) (PEG) and poly(zwitterions) (pSB) are widely used in biomedical applications due to their presumed low protein binding.
    • This low protein binding is a key characteristic for their efficacy in preventing non-specific interactions.

    Purpose of the Study:

    • To investigate the direct interaction between poly(sulfobetaine) (pSB) and proteins in solution.
    • To determine the effect of pSB on protein thermal stability and folding cooperativity.
    • To assess whether pSB is universally protein-repellent.

    Main Methods:

    • Utilized tryptophan fluorescence spectroscopy to analyze changes in protein conformation and local polarity.
    • Performed thermal denaturation studies to measure protein melting temperatures and folding cooperativity.
    • Examined the interactions of soluble 100 kDa pSB with three structurally distinct proteins.

    Main Results:

    • Demonstrated direct interaction between soluble pSB and all three tested proteins.
    • Observed that pSB reduces protein thermal stability (up to ~1.9 °C per wt%) and increases folding cooperativity (up to ~130 J mol⁻¹ K⁻¹ per wt%).
    • Found that the extent of these changes is protein-dependent, with some proteins showing increased stability at high pSB concentrations.

    Conclusions:

    • Poly(sulfobetaine) (pSB) is not universally protein-repellent.
    • pSB can directly interact with proteins, influencing their stability and conformation.
    • The effectiveness of pSB in biotechnological applications is dependent on the specific protein interactions involved.