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Forms of amino acids
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Sowseii
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#1
Hi guys currently doing an assignment for biochemistry I’ve been asked which forms of amino acid would be present in pH 7 and pH 9, protonated, deprotonated, zwitterion or neutral? I would really appreciate any help
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Thanks!
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adina456
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Sowseii
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#3
(Original post by adina456)
Are there any amino acids in particular that were mentioned?
Are there any amino acids in particular that were mentioned?
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adina456
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#4
(Original post by Sowseii)
Hi, the amino acid is asparagine
Hi, the amino acid is asparagine
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
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Kallisto
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#5
(Original post by Sowseii)
x
x
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.
Last edited by Kallisto; 2 years ago
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Sowseii
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#6
(Original post by adina456)
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
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
(Original post by Kallisto)
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.
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.
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Sowseii
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#7
(Original post by adina456)
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
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
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