Question

What do both a-helix and b-sheet have in common?

1) They are both secondary structures of proteins
2) They are both formed by hydrogen bonding
3) They both have a regular repeating pattern
4) They both contribute to the overall stability of the protein

Answer 1

The α-helix and β-sheet are secondary structures of proteins characterized by hydrogen bonding, regular repeating patterns, and contribute to protein stability.

Step-by-step explanation:

The α-helix and β-sheet are both secondary structures found in proteins. They share several key features:

1. They are both secondary structures of proteins, meaning they are local foldings within the polypeptide chain that contribute to the protein's three-dimensional shape.
2. Both are formed by hydrogen bonding between the oxygen of a carbonyl group and the hydrogen of an amino group in the peptide backbone. In the α-helix, these bonds form between every fourth amino acid.
3. They each have a regular repeating pattern: the α-helix is characterized by a spiral shape, while the β-sheet consists of strands aligned side-by-side either in parallel or antiparallel orientation.
4. Their structure contributes to the overall stability of the protein due to the number of hydrogen bonds that help maintain their shape.

Secondary structures like the α-helix and β-sheet are critical to protein function because they influence the final three-dimensional conformation necessary for the protein's specific biological role.