β-pleated sheet

Definition

β-pleated sheet is a common secondary structure in proteins, characterized by beta strands linked laterally by at least two or three backbone hydrogen bonds. These sheets can be parallel or antiparallel.

5 Must Know Facts For Your Next Test

1. β-pleated sheets are stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another.
2. They form a zigzag or pleated appearance due to the alternating direction of the peptide backbone.
3. β-pleated sheets can be found in both fibrous and globular proteins.
4. Antiparallel β-sheets have strands that run in opposite directions, which creates more stable hydrogen bonds compared to parallel β-sheets.
5. Silk fibroin is an example of a protein that primarily consists of β-pleated sheets.

Review Questions

• What type of bonding stabilizes β-pleated sheets?
• Describe the structural difference between parallel and antiparallel β-pleated sheets.
• Give an example of a protein that contains a high amount of β-pleated sheets.

Related terms

alpha_helix: A common secondary structure in proteins characterized by a right-handed coil stabilized by hydrogen bonds between every fourth amino acid.

secondary_structure: The level of protein structure that includes α-helices and β-pleated sheets, formed through hydrogen bonding patterns.

hydrogen_bonding: A type of weak chemical bond important for stabilizing structures like α-helices and β-pleated sheets in proteins.