What Causes an Egg to Harden when Boiled?

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SUMMARY

The hardening of an egg when boiled is primarily due to the denaturation of proteins in the egg white, which are composed of long chains of amino acids. When exposed to heat, weak bonds within these proteins are disrupted, causing them to unfold and solidify. Amino acids alone lack specific functions; however, when linked in a polypeptide chain, they form proteins with distinct three-dimensional structures essential for their biological roles. Additionally, dissolving hard-boiled egg whites requires both a detergent and a reducing agent to break down the protein avidin and its disulfide bonds.

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  • Understanding of protein structure and function
  • Knowledge of amino acids and polypeptide chains
  • Familiarity with denaturation processes in biochemistry
  • Basic concepts of detergents and reducing agents in chemical reactions
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  • Research the process of protein denaturation and its implications in cooking
  • Study the role of amino acids in protein synthesis and function
  • Explore the chemistry behind detergents and their applications in biochemistry
  • Learn about the structure and function of avidin and its interactions with biotin
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what is the difference between amino acids on their own and amino acids that have been incorporated into a polypeptide chain?

My answer is that amino acids on their on do nothing. However when they interact they create a protein which eventually takes on a particular function.

why does boiling an egg cause it to harden?
why does it require both a detergent and a reducing agent to dissolve the hard boiled white.

Thanks
 
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Hey there! It's been a while since I've had Biology but I'm pretty sure you're thinking in the right direction. I haven't read anywhere that amino acids do anything else except bond to each other and produce proteins which have either structural or functional purposes. On their own, they're drifters just kind of floating around in the cell until they are ready to be used. This is about all I can explain right now...not sure what you mean by your last couple of questions. Do they have to do with amino acids in particular or the proteins formed by them? :rolleyes:
 
for your question!

The hardening of an egg when boiled is due to the denaturation of proteins in the egg white. Proteins are made up of long chains of amino acids, which are held together by weak bonds. When heat is applied, these weak bonds are disrupted and the protein molecules unfold, causing the protein to change shape and become more firm. This is why the egg white changes from a clear, runny liquid to a solid, opaque substance when boiled.

As for the difference between amino acids on their own and those incorporated into a polypeptide chain, amino acids on their own do not have a specific function. However, when they are linked together in a specific sequence to form a polypeptide chain, they create a unique 3-dimensional structure that allows the protein to carry out its specific function. This structure is essential for the protein's proper functioning and can be affected by external factors such as heat, pH, and chemicals.

In regards to dissolving a hard-boiled egg white, both a detergent and a reducing agent are needed. The egg white contains a protein called avidin, which binds to biotin (a B vitamin) and makes it unavailable for absorption. Detergents are able to break down the lipid membrane surrounding the egg white, allowing the reducing agent to access the avidin and break it down. The reducing agent then breaks the disulfide bonds in the protein, causing it to unfold and lose its structure, making it easier to dissolve in water. Without both the detergent and reducing agent, it would be difficult to break down the protein and dissolve the hard boiled egg white.
 

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