Forms of amino acids

Are there any amino acids in particular that were mentioned?

Hi, the amino acid is asparagine

x

okay, the basic anime group (NH3) of amino acids are able to accept a proton from the carboxylic group to form an ion containing both a negative and positive charge - this is called a zwitterion (the charges for both groups are now NH3^+ and COO^-

the isoelectric point is the pH at which the zwitterion is formed (for asparagine it’s pH 10.76)

If the amino acid is placed in a solution with a pH GREATER than its isoelectric point, the amino acid behaves as an acid and the NH3^- group loses a proton (deprotonated). The opposite occurs for a solution with a pH LESS THAN the amino acids isoelectric point, it acts as a base and the COO^- group gains a proton (protonated)

For asparagine:
pH7 - protonated
pH 9 - also protonated

Hope this helped, for more clarity I would research zwitterions

Just as an addition to adina456 explanations, I will give you an understanding what exactly happens to the amino acid placed in a solution with a pH 10.76, the value for asparagine. As you already know, it is a protonation, as pH 9 and pH 7 are lesser than 10.76.

When adding a certain amino acid in this solution, the amino acid becomes a zwitterion which has two different charges now, a positive (NH3+) and a negative (COO-) one. In other words: the functional groups of the amino acid are ionized. In this process, the Carboxyl group (COOH) donated a proton (H+) to the amino group (NH2) which gained it and this zwitterion state is done.

Acting like a base means that the COO- is protonated in solution and gets back to the carboxyl group COOH, while the NH3+ ion remains. It would be vice versa, when the amino acid acts like an acid: NH3+ donates a proton and get back to amino group NH2, while the COO- ion remains. That is the deprotonated process.

okay, the basic anime group (NH3) of amino acids are able to accept a proton from the carboxylic group to form an ion containing both a negative and positive charge - this is called a zwitterion (the charges for both groups are now NH3^+ and COO^-

the isoelectric point is the pH at which the zwitterion is formed (for asparagine it’s pH 10.76)

If the amino acid is placed in a solution with a pH GREATER than its isoelectric point, the amino acid behaves as an acid and the NH3^- group loses a proton (deprotonated). The opposite occurs for a solution with a pH LESS THAN the amino acids isoelectric point, it acts as a base and the COO^- group gains a proton (protonated)

For asparagine:
pH7 - protonated
pH 9 - also protonated

Hope this helped, for more clarity I would research zwitterions