A protein's secondary structure contains helixes and sheets that result from hydrogen bonding between carboxyl and amino groups of the polypeptide chain.
The secondary structure of a protein is a level of organization that the molecule acquires, depending on the amino acid sequence that compose it.
Hydrogen bonds are the main stabilizing force in this structure.
Hydrogen bonds are established between the -CO- and -NH- groups of the peptide bond (the first as an H acceptor, and the second as an H donor).
In this way, the polypeptide chain is capable of adopting lower free energy conformations, and therefore more stable.
The rigidity of the peptide bond, the turning capacity of the bonds established with the asymmetric carbon and the interaction of the radicals of the amino acids with the solution in which it is found, leads the molecule to fold on itself.
The resulting conformations can be the α-helix, the beta sheets and the collagen helix.
Therefore, we can conclude that secondary structure refers to the three-dimensional organization of the regions of the polypeptide chain, where nearby amino acids interact by hydrogen bonds between their tails.
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