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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 been defined by clustering turn conformations within very high-resolution protein structures.
Over the years, many beta turn prediction methods have been developed. Recently, Dr. Raghava's Group developed BetaTPred3 method which predicts a complete beta turn rather than individual residues falling into a beta turn. The method also achieves good accuracy and is the first method which predicts all 9 types of beta turns.
Residues in beta hairpins with loops of 2, 3, or 4 residues have distinct conformations. However, a wide range of conformations can be seen in longer loops, which are sometimes referred to as 'random coils'. A beta-meander consists of consecutive antiparallel-beta strands linked by hairpins. [3] Two residue loops are called beta turns or ...
The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure .
Beta bend ribbons may be formed from any of these types but type I is the commonest in proteins, as it is for single beta turns. Beta bend ribbons made from type I or I’ turns are somewhat twisted, while beta bend ribbons made from type II or II’ beta turns are flat. Beta bend ribbons with mixtures of different beta turn types also occur ...
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Four-residue turns also have their own characteristic amino acids; proline and glycine are both common in turns. A turn is predicted only if the turn probability is greater than the helix or sheet probabilities and a probability value based on the positions of particular amino acids in the turn exceeds a predetermined threshold. The turn ...
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