Which type of protein structure is characterized by stability through hydrogen bonding?

The type of protein structure characterized by stability through hydrogen bonding is the beta-pleated sheet. In beta-pleated sheets, hydrogen bonds form between the backbone amide hydrogen and carbonyl oxygen of different strands of polypeptides. This creates a sheet-like structure that is vital for the overall stability of proteins. The regular, repeating nature of these hydrogen bonds allows the beta sheets to provide significant tensile strength and structural integrity to proteins, especially in fibrous proteins.

While alpha helices also form through hydrogen bonds, the question specifies stability through the context of the beta-pleated sheet, known for its extensive hydrogen bonding across multiple strands, which allows for great robustness. Tertiary and quaternary structures involve more complex interactions, including hydrophobic interactions and ionic bonds, but they are not defined solely by hydrogen bonding like the beta-pleated sheet is.