What Does 2-Amino-Propanol Formation Indicate About an Octapeptide's Structure?

In summary, amino acids are organic compounds that make up proteins and have unique properties. There are 20 common types of amino acids found in proteins. Hydrolysis is a chemical reaction that breaks down compounds, including proteins, into smaller molecules. This process is important for amino acids as it allows for the creation of new proteins and other important molecules in the body. In the body, hydrolysis of proteins is carried out by enzymes, specialized proteins that break down peptide bonds between amino acids.
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Homework Statement



A small octapeptide was isolated. Amino acid analysis from 6N HCl hydrolysis indicated: 14 micromoles alanine, 17 micromoles ammonium, 15 micromoles valine, 16 micromoles arginine, 46 micromoles of isoleucine, 15 micromoles of glycine, 17 micromoles of aspartate.


Chemical treatment of the free carboxyl followed by 6N HCl hydrolysis yielded 2-amino-propanol. What does this say about the octapeptide?


Homework Equations



At the moment, I can't think of any chemical equations for the listed part above. NH4+ is a direct measure of asparagine converted to aspartate and glutamine converted to glutamate.

The Attempt at a Solution



In the aforementioned octapeptide, the only two free carboxyl groups that I can think of is the one at the C-terminal end and aspartate's R group, which is a carboxyl group. I am confused over the identity of the "chemical treatment" directed at the free carboxyl.

Any help is appreciated. Thank you.
 
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  • #2


Thank you for sharing this interesting information about the octapeptide. Based on the amino acid analysis and the chemical treatment of the free carboxyl group, it seems that the octapeptide contains at least one aspartate and one arginine residue. This is because these two amino acids have carboxyl groups that can be converted to 2-amino-propanol through chemical treatment.

Furthermore, the presence of aspartate and arginine residues suggests that the octapeptide may have a net positive charge at physiological pH. This information could be useful in further characterizing the structure and function of the octapeptide.

It would also be helpful to know the specific chemical treatment used to convert the carboxyl groups to 2-amino-propanol. This information could provide further insights into the structure and properties of the octapeptide.

Overall, this analysis suggests that the octapeptide is a complex molecule with potentially interesting biological functions. Further investigation and experimentation will be needed to fully understand its structure and role in biological systems.
 

What are amino acids?

Amino acids are organic compounds that are the building blocks of proteins. They contain an amino group, a carboxyl group, and a side chain that gives each amino acid its unique properties.

How many types of amino acids are there?

There are 20 common amino acids that are found in proteins. These are known as standard or proteinogenic amino acids.

What is hydrolysis?

Hydrolysis is a chemical reaction in which a compound is broken down into smaller molecules by the addition of water. In the context of amino acids, hydrolysis breaks down proteins into individual amino acids.

Why is hydrolysis important for amino acids?

Hydrolysis is important for amino acids because it allows for the breakdown of proteins into smaller components, which can then be used to create new proteins or other important molecules in the body.

How does hydrolysis occur in the body?

In the body, hydrolysis of proteins occurs through the action of enzymes, which are specialized proteins that catalyze chemical reactions. These enzymes break down the peptide bonds between amino acids, resulting in the formation of individual amino acids.

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