Re: Re: Salting-Out Effect

Hi Nedrick,

Salting out is the process of separating proteins form solution by increasing salt concentration.

As proteins are less soluble in salt solution.

There are hydrophobic amino acids and hydrophilic amino acid in protein  molecules. After protein folding in aqueous solution, hydrophobic amino acids usually form protected hydrophobic areas while hydrophilic amino 
acids interact with the molecules of aolvation and allow proteins to form hydrogen bonds with the surrounding water 
molecules. If enough of the protein surface is hydrophilic, the protein 
can be dissolved in water.
When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water 
molecules available to interact with the charged part of the protein. As a result of the increased demand for solvent molecules, the 
protein-protein interactions are stronger than the solvent-solute 
interactions; the protein molecules coagulate by forming hydrophobic interaction with each other. This process is known as salting out.

Regards
Aftab Hussain
Lecturer (Visiting)
Department of Chemistry
The Islamia University Of Bahawalpur



________________________________
From: Krzysztof Mitko <[email protected]>
To: [email protected]
Sent: Sunday, July 3, 2011 1:40 PM
Subject: [The Chemistry Cluster] Re: Salting-Out Effect


  
On 03/07/11 06:57, Nedrick wrote:
> Please explain what is salting-out effect all about?
> How will I illustrate the salting-out effect.
> These are the reagents:
> 1. 1-butanol
> 2. water
> 3. then it was treated with Sodium Chloride.
> 
> *What is it all about? All I was seeing in the internet was all about proteins. And, it's not about Organic Chemistry. 

After you add sodium chloride, the solubility of butanol decreases and
a new, alcohol-rich phase will emerge.

-- 
Best regards,
Krzysztof Mitko


 

[Non-text portions of this message have been removed]



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