Final answer:
Secondary structure in proteins includes organized regions like α-helix and β-pleated sheets, stabilized by hydrogen bonds.
Step-by-step explanation:
The secondary structure of proteins refers to the organized regions of a polypeptide backbone that are stabilized by hydrogen bonds between atoms. Two common examples are the α-helix and the β-pleated sheet. The α-helix is a right-handed coil where every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier.
The β-pleated sheet consists of beta strands connected laterally by at least two or three backbone hydrogen bonds forming a sheet-like structure. Recognizing these structures is key in understanding protein folding and function.