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Proteins are comprised of amino acids, which have distinct properties and sequences that determine a protein's structure and function. The secondary structure of a protein refers to the local arrangement of amino acids into stable patterns, typically driven by hydrogen bonding between the amino acids' backbone groups. The α-helix and β-sheet are the most common secondary structures found in proteins.

The α-helix is a right-handed coil, with amino acids forming a spiral structure. This structure is stabilized by hydrogen bonds forming between the carbonyl oxygen atom (-C=O) of a given amino acid and the amide hydrogen atom (-N-H) of a nearby amino acid located approximately four residues ahead in the sequence. The side chains of the amino acids (R-groups) face outward from the helix core, allowing for interactions with other amino acids or molecules.

The β-sheet is characterized by extended "zig-zag" amino acid chains that are arranged side by side in a sheet-like pattern. This structure is stabilized by hydrogen bonds that form between carbonyl oxygen atoms (-C=O) and amide hydrogen atoms (-N-H) present on adjacent chains. The β-sheet is further subdivided into two types: parallel β-sheets, in which the adjacent amino acid chains have their N-termini and C-termini aligned, and antiparallel β-sheets, where the N-terminus of one chain is aligned with the C-terminus of an adjacent chain.

The following differences distinguish the α-helix from the β-sheet: 1. Structure: The α-helix has a coiled, spiral structure, while the β-sheet consists of extended, side-by-side chains with a "zig-zag" pattern. 2. Hydrogen Bonding: In the α-helix, hydrogen bonds form between nearby amino acids within the same chain, while in the β-sheet, hydrogen bonds form between adjacent chains. 3. Amino Acid Side Chains: The side chains of amino acids in the α-helix point outward from the helix core, whereas in the β-sheet, side chains alternate between pointing above and below the sheet plane. 4. Types: While the α-helix only exists in one form, β-sheets are further subdivided into parallel and antiparallel types, depending on the orientation of adjacent chains. By understanding the differences between the α-helix and β-sheet secondary structures, one can appreciate their various roles in determining protein structure and function.