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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 ...
Draw the structure, and save it as a ChemDraw file. If you drew the structure before applying any settings, then you need to select the object, open the "Object" menu and choose "Apply document settings from → ACS Document 1996". Then save it as a PNG file, to be read by an image editor such as GIMP or IrfanView (see below for details).
The other type is the G1 beta bulge, of which there are two common sorts, both mainly occurring in association with antiparallel sheet; one residue has the α L conformation and is usually a glycine. In one sort, the beta bulge loop , one of the hydrogen bonds of the beta-bulge also forms a beta turn or alpha turn, such that the motif is often ...
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