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