β-pleated sheet
Definition
A β-pleated sheet is a common secondary structure in proteins characterized by two or more polypeptide chains lying side by side, linked together by hydrogen bonds. This structure forms a sheet-like arrangement that 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 can be found in both parallel and antiparallel orientations depending on the direction of the polypeptide chains.
- β-pleated sheets contribute to the overall stability and rigidity of protein structures.
- They play a crucial role in the structural framework of many proteins, including silk fibroin and amyloid fibrils.
- Misfolded β-pleated sheets are associated with several diseases, such as Alzheimer's disease and prion diseases.
Review Questions
- What type of bonding stabilizes β-pleated sheets?
- How do parallel and antiparallel β-pleated sheets differ?
- Name one disease associated with misfolded β-pleated sheets.
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Related terms
Alpha helix: A common secondary structure in proteins characterized by a coiled shape held together by hydrogen bonds.
Hydrogen bond: A weak bond between two molecules resulting from an electrostatic attraction between a proton in one molecule and an electronegative atom in the other.
Protein folding: The process by which a protein assumes its functional three-dimensional shape.
