Protonated and deprotonated forms of amino acids and electrophoresis

Started by Pranjal Singh, January 20, 2022, 10:52:06 PM

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Pranjal Singh

Here it is
[attachment id=0 msg=3214]

chenbeier

At pH 1 the molecule has positiv charge at nitrogen. The COOH groups are not dissociated. Movement to negative electrode. Positiv is wrong. At pH 2.45 we have inner salt of amino acid and one COOH is not  dissociated. So no movement. At pH 7 inner salt but second COOH is dissociated movement to positiv.
At pH 9 all COOH dissociated and  free NH2. Movement to positiv electrode. Negative is wrong.
So answer 2 is correct.

uma

Quote from: Pranjal Singh on January 20, 2022, 10:52:06 PM
Here it is
[attachment id=0 msg=3214]
Aspartic acid has two acidic protons and one basic lone pairs.
In strong acidic conditions means below pka=2 Aspartic acid is fully protonated with net positive and hence during electrophoresis migrate towards negative terminal..
In very strong basic conditions ,Aspartic acid is fully deprotonated with net negative charge and hence during electrophoresis migrate towards positive terminal.
Understand more from this image about protonated and deprotonated forms of amino acids at different pH values and migrations of ions during electrophoresis.
[attachment id=0 msg=3216]

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