Eggs are rich in proteins. The three main components are the egg shell, the egg white, and the egg yolk. All proteins are made of building blocks called amino acids arranged in chains. The specific folding a chain of amino acids undergoes gives a protein its properties.
This structure can now be modified by various applications of heat or chemicals, and the process of changing the original structure of a protein is called denaturing. In simple words, denaturation alters the bonds between the amino acid chains in the original or native structure of the protein. Altering the bonds alters the properties of the protein.
In the case of an egg, the egg white, which is in a semi-fluid state in its native form, on application of heat through boiling clumps together and hardens, forming the white exterior of boiled eggs. The egg yolk, which is also in a semi-fluid state, hardens, forming the hard yellow yolk we find in a boiled egg.
However, food scientists have found that boiling eggs for different durations of time leads to different extents of denaturation, enabling them to experiment with dishes that have a slightly runny yolk or a slightly soft texture.
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