Beta-sheet
Beta-sheet
Beta-sheet (pronunciation: BAY-tuh sheet) is a common motif of regular secondary structure in proteins. Beta-sheets consist of beta strands (also β-strand) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet.
Etymology
The term "Beta-sheet" was coined by Robert Corey and Linus Pauling in 1951 when they discovered this structure while studying the protein keratin. The prefix "beta" is used to distinguish it from the alpha helix structure, which was discovered around the same time.
Structure
A beta-sheet is made up of two or more beta strands arranged next to each other, forming a sheet-like structure. The strands are held together by hydrogen bonds between the backbone atoms. The pleated, or twisted, shape of the sheet is due to the tetrahedral chemical bonding arrangement common to all proteins.
Types
There are two types of beta-sheets: parallel and antiparallel. In a parallel beta-sheet, all the strands run in the same direction, while in an antiparallel sheet, adjacent strands run in opposite directions.
Function
Beta-sheets are crucial for the stability of many proteins. They provide a large amount of surface area for potential binding interactions with other molecules, making them important in processes such as enzyme catalysis and antibody-antigen interactions.
Related Terms
- Alpha helix: Another common secondary structure in proteins.
- Beta turn: A type of protein secondary structure consisting of four amino acids that form a 180-degree turn.
- Protein folding: The process by which a protein structure assumes its functional shape or conformation.
- Protein structure: The three-dimensional arrangement of atoms in an amino acid-chain molecule.
External links
- Medical encyclopedia article on Beta-sheet
- Wikipedia's article - Beta-sheet
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