Condensation joins two amino acids and releases a water molecule. The reverse — hydrolysis — splits the bond by adding water back, and it is the most fundamental degradation route available to any peptide.
That symmetry is the whole argument for freeze-drying. Remove the water and the reverse reaction has nothing to work with, which is why lyophilised material is stable in a way a solution is not.
The nitrogen lone pair delocalises into the adjacent carbonyl, giving the bond partial double-bond character. A double bond cannot rotate freely, so each peptide linkage is planar and the backbone is constrained.
That constraint is what makes defined secondary structure possible at all. A fully flexible chain would have no preferred conformation; a chain rigid at every linkage and rotatable between them does.
The peptide bond absorbs in the far ultraviolet, around 210–220 nm. A detector set there responds to every linkage in the chain, which is why it is the common wavelength for peptide HPLC.
Aromatic residues absorb near 280 nm, which some methods use instead — but only a peptide containing them will respond, so the backbone wavelength is the general-purpose one.
Condensation joins two amino acids and releases a water molecule. The reverse — hydrolysis — splits the bond by adding water back, and it is the most fundamental degradation route available to any peptide.
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