What kind of bonding occurs in β-pleated sheets?

β-pleated sheets, a common secondary structure in proteins, are primarily stabilized by hydrogen bonding. This type of bonding occurs between the hydrogen atoms of amino groups (amino hydrogens) and the oxygen atoms of carbonyl groups within the peptide bonds of the polypeptide chain. The arrangement of these hydrogen bonds creates a sheet-like structure that can either be parallel or antiparallel, depending on the orientation of the strands.

The significance of hydrogen bonding in β-pleated sheets is that it allows for a stable structure that contributes to the overall three-dimensional configuration of a protein. This stability is crucial for the protein's function, as it impacts how proteins interact with other molecules and perform their biological roles.

Covalent bonding, ionic bonding, and disulfide bonds, while important in different contexts of protein structure and stability, are not the primary forces that define the structure of β-pleated sheets. Therefore, the focus on hydrogen bonding in this context highlights the specific interactions that are fundamental to this secondary structure.