Final answer:
The beta sheet secondary structure of protein silk is stabilized by hydrogen bonds between the oxygen atom of a carbonyl group and the hydrogen atom of an amino group in the polypeptide chain.
Step-by-step explanation:
The secondary structure of protein silk, which is characterized by beta sheets, is stabilized primarily through hydrogen bonds. These bonds occur between the oxygen atom in the carbonyl group of one amino acid and the hydrogen atom in the amino group of another, often four amino acids away along the chain. The beta sheet structure is formed by the pleating of the polypeptide chain and the alignment of the amino acids in a sheet-like array, with the hydrogen bonds maintaining the stability of this arrangement. This is essential for the protein to maintain its structure and function.