310 helix
310 Helix[edit | edit source]
The 310 helix is a type of secondary structure found in proteins. It is characterized by a specific pattern of hydrogen bonding and a distinct helical shape. The 310 helix is less common than the more familiar alpha helix, but it plays an important role in the structure and function of certain proteins.
Structure[edit | edit source]
The 310 helix is named for its hydrogen bonding pattern, where each amino acid residue forms a hydrogen bond with the residue three positions ahead in the sequence. This results in a helix with 3 residues per turn and a pitch of approximately 6.0 Å. The 310 helix is more tightly coiled than the alpha helix, which has 3.6 residues per turn.
In a 310 helix, the carbonyl oxygen of the i-th residue forms a hydrogen bond with the amide hydrogen of the (i+3)-th residue. This pattern creates a right-handed helix with a distinct geometry.
Properties[edit | edit source]
The 310 helix is generally less stable than the alpha helix due to its tighter turns and less optimal hydrogen bonding. However, it can be stabilized by specific interactions, such as side chain interactions or the presence of certain amino acids that favor this conformation.
310 helices are often found at the ends of alpha helices or in regions where a tighter turn is required. They can also occur in peptides and small protein domains.
Occurrence[edit | edit source]
While the 310 helix is less common than the alpha helix, it is found in a variety of proteins, including enzymes, receptors, and structural proteins. It can play a role in protein folding and stability, as well as in the formation of protein-protein interactions.
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