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Peptide Bond Formation
Amino acids are the building blocks of proteins and they are held together by special covalent bonds known as peptide bonds (also known as amide bonds). These peptide bonds are formed via the dehydrolysis reaction (also known as condensation). In the dehydrolysis reaction, a covalent bond is formed between the carbon of the carbonyl group of one amino acid and the nitrogen of the amino group of the other amino acid. In the process, a water molecule is released. In this dehydrolysis reaction, the reactants (amino acids) are thermodynamically more stable than the products (the dipeptide), which means that energy must be inputed to drive the reaction forward. So if the products are less stable than the reactants, why doesn't the peptide bond spontaneously dissociate? It turns out that the peptide bond is kinetically stable, which simply means that a very high activation energy exists in the reverse hydrolysis reaction. Therefore, under normal physiological conditions, not enough energy exists to break the peptide bond via this hydrolysis reaction. In order to break a peptide bond, our body uses special enzymes to lower the activation energy and speed up the reverse reaction.
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