Understanding Casein's Reaction in Water: pH 4.6 Residue Formation

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When protein, such as casein, is dissolved in water at a pH of approximately 4.6, it can lead to residue formation due to the protein's isoelectric point (pI). At this pH, the positive and negative charges on the amino acids balance, minimizing repulsive forces and allowing the amino acids to attract each other through van der Waals bonds. This interaction causes casein to aggregate and form a residue. If the pH deviates from the pI, repulsive forces prevent the proteins from aggregating effectively. Understanding these interactions is crucial for explaining casein's behavior in solution.
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What happens when you put protein in water?

I know that an amino acid in water vill dissolve into:
^{+}H_3 N-CHR-COO^{-}
As protein is built up by over 50 amino acids, will the very same thing (as the formula above) happen to it?

(My homework is to explain why Casein produces a residue when put into a water solution with pH≈4,6)
 
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Protein is in a way similar to a single amino acid. You should be able to see it if you draw a simple protein, say GlyGlyGly.
 
I think this is the answer to the question why Casein produces a residue when put into a water solution with pH≈4,6 (but I'm very uncertain)

At that pH, this is what happens:

H_2N-CHR-COOH \rightarrow ^{+}H_3N-CHR-COO^{-} (Amino acid put into water solution)

pH ≈ pI \Rightarrow [^{+}H_3N-CHR-COOH] = [H_2N-CHR-COO^{-}]

This leads us to the fact that there are no repulsive forces between the amino acids, thus the R-group of the amino acids of Casein are able to attract each other via van der Waals-bonds.
When pH≠pI the protein can not come together, because of the repulsive forces.

Correct, or incorrect?
 
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