Egg White Protein Structure Change

In summary: The strong and weak salt solutions work by breaking down the peptide bonds of the amino acids. This creates a denatured protein that can be studied by looking at the structure.
  • #1
Jordan_
20
0
Hey, I have some homework questions and I'd appreciate some clarification.

As a class we did an experiment where we put egg white into seven different test tubes, and then introduced seven different solutions, one to each test tube. The different solutions were weak & strong salt solutions, weak base (ammonia), strong base (sodium hydroxide), weak acid (acetic acid), strong acid (hydrochloric acid), and acetone.

For the strong and weak salt solutions, nothing really happened at all, except that for the weak salt solution, the protein stayed near the bottom of the mixture and in the strong solution the protein stayed near the top. In the weak base, the protein stayed near the bottom and the top was very clear liquid. In the strong base, the protein denatured into thick white stuff. In the weak acid, the protein did not really denature as far as I saw, just stayed at the bottom of the test tube with clear liquid above it. On the strong acid, the protein again denatured. In the acetone solution, it was clear on top, denatured protein in the middle, and egg white protein on the bottom.

I am thinking the reason it denatured had something to do with peptide bonds holding amino acids together breaking and then reassembling different ways, creating the thick white gel stuff. I just don't really know how to explain this. Can you guys give me any tips on where to start looking because I'm sort of lost.

Thanks in advance.
 
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  • #2
You should look in another direction. Try to look at the effect of the side chain of the amino acid and the charge of the polypeptides on tertiary structure.
 
Last edited:
  • #3
Okay, I've got most of my research done. I just need to know how does the weak and strong salt solutions alter the structure? I've seen it listed in places that it works the same way as acids and bases, but it never really goes on to explain how. I really need to know how to understand this.

Thanks in advance.
 

1. What is egg white protein?

Egg white protein, also known as albumin, is a type of globular protein found in egg whites. It consists of long chains of amino acids and is rich in essential amino acids, making it a complete protein source.

2. How does the structure of egg white protein change?

The structure of egg white protein can change through denaturation, a process in which the protein's shape and structure is altered due to external factors such as heat, pH changes, or mechanical agitation. This leads to unfolding of the protein's three-dimensional structure and exposure of its hydrophobic regions.

3. What causes the change in egg white protein structure?

The change in egg white protein structure is primarily caused by heat. When egg whites are subjected to heat, the proteins undergo a process called coagulation, where the long chains of amino acids become tangled and form a solid mass. Other factors such as pH changes and mechanical agitation can also contribute to the change in structure.

4. How does the change in egg white protein structure affect its properties?

The change in egg white protein structure can affect its properties in several ways. It can alter the protein's solubility, making it less soluble in water. It can also change the protein's ability to form foams and emulsions, which are important properties in food and baking industries. Additionally, it can affect the protein's digestibility and nutritional value.

5. Can the structure of egg white protein be reversed?

In most cases, the change in egg white protein structure is irreversible. However, some methods, such as adding acids or enzymes, can partially reverse the denaturation process. This is because these substances can disrupt the interactions between the protein molecules and allow them to refold into their original structures. However, the protein's functionality and properties may not be fully restored.

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