Beta sheet
Beta sheet
A Beta sheet (pronounced: /ˈbeɪtə ʃiːt/) is a key structural motif in proteins that was first described by Linus Pauling and Robert Corey in the early 1950s.
Etymology
The term "Beta sheet" was coined by Pauling and Corey, who named it after the Alpha helix, another protein structure they discovered. The "Beta" in "Beta sheet" refers to the second letter of the Greek alphabet, indicating that it was the second structure of this type to be discovered.
Definition
A Beta sheet is a level of protein secondary structure characterized by the alignment of peptide chains in a zigzag pattern, which results in a flat, pleated sheet-like structure. The individual peptide chains are held together by hydrogen bonds between the carbonyl oxygen of one peptide bond and the amide hydrogen of another.
Related Terms
- Alpha helix: Another common form of protein secondary structure. Alpha helices are right-handed coils or spirals, where every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier.
- Protein structure: The three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, the monomers of the polymer.
- Peptide bond: A chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O). This is a dehydration synthesis reaction, also known as a condensation reaction.
- Hydrogen bond: A type of attractive intermolecular force that exists between two partial electric charges of opposite polarity. Although stronger than most other intermolecular forces, the hydrogen bond is much weaker than both the ionic bond and the covalent bond.
External links
- Medical encyclopedia article on Beta sheet
- Wikipedia's article - Beta sheet
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