Final answer:
In the β-pleated sheet secondary structure of proteins, interchain hydrogen bonds form between the oxygen atom of a carbonyl group and the hydrogen of an amine group across amino acid chains.
Step-by-step explanation:
The student is asking about the type of hydrogen bonds found in the β-pleated sheet, which is one of the two most common secondary structures of proteins. In a β-pleated sheet, the chains of amino acids lie alongside each other, forming rows or strands held together by interchain hydrogen bonds. These are formed between the oxygen atom of a carbonyl group in one amino acid and the hydrogen of an amine group in a separate amino acid that may be part of the same or another polypeptide chain. This structure creates a pleated or accordion-like appearance, hence the name β-pleated sheet. Certain amino acids tend to promote the formation of this structure, contributing to the protein's overall shape and function.
The secondary structure of proteins, such as the ß-pleated sheet, is maintained by hydrogen bonding between amino acids in the peptide backbone. In the ß-pleated sheet, hydrogen bonds form between continuous sequences of carbonyl and amino groups that are further separated on the polypeptide chain. These hydrogen bonds create a stable and rigid structure, contributing to the overall folding and shape of proteins.