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In proteins in general all four beta turn types occur frequently but I is most common, followed by II, I' and II' in that order. Beta turns are especially common at the loop ends of beta hairpins; they have a different distribution of types from the others; type I' is the most common, followed by types II', I and II. Additional turn types have ...
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A hairpin is a special case of a turn, in which the direction of the protein backbone reverses and the flanking secondary structure elements interact. For example, a beta hairpin connects two hydrogen-bonded , antiparallel β-strands (a rather confusing name, since a β-hairpin may contain many types of turns – α, β, γ, etc.).
The secondary structure is assigned based on hydrogen bonding patterns as those initially proposed by Pauling et al. in 1951 (before any protein structure had ever been experimentally determined). There are eight types of secondary structure that DSSP defines: G = 3-turn helix (3 10 helix). Min length 3 residues. H = 4-turn helix . Minimum ...
This template is intended for use on protein secondary structure pages. To insert, use {{Alpha beta structure}}. On the Alpha helix and Beta sheet pages, it displays alternative versions of the image with the relevant section highlighted. Alternatively, for the non-interactive image, use [[File:Alpha beta structure (full).png]]
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