Pi helix Totally Explained

Everything about Pi Helix totally explained

A pi helix (or π-helix) is a type of secondary structure found in proteins. These structure are particularly common in membrane proteins

Standard structure

The amino acids in a standard π-helix are arranged in a right-handed helical structure. Each amino acid corresponds to a 87° turn in the helix (for example, the helix has 4.1 residues per turn), and a translation of 1.15 Å (=0.115 nm) along the helical axis. Most importantly, the N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid five residues earlier; this repeated i+5→i hydrogen bonding defines a π-helix. Similar structures include the 3₁₀ helix (i+3→i hydrogen bonding) and the α-helix (i+4→i hydrogen bonding).
Residues in π-helices typically adopt (φ, ψ) dihedral angles near (-55°, -70°). More generally, they adopt dihedral angles such that the ψ dihedral angle of one residue and the φ dihedral angle of the next residue sum to roughly -125°. For comparison, the sum of the diheral angles for a 3₁₀ helix is roughly -75°, whereas that for the α-helix is roughly -105°. The general formula for the rotation angle Ω per residue of any polypeptide helix with trans isomers is given by the equation ť

3 cos Omega = 1 - 4 cos^ left[ left(phi + psi 
ight)/2 
ight]

Left-handed structure

In principle, a left-handed version of the π-helix is possible by reversing the sign of the (φ, ψ) dihedral angles to (55°, 70°). This pseudo-"mirror-image" helix has roughly the same number of residues per turn (4.1) and helical pitch (1.5 angstroms or 150 picometers). It isn't a true mirror image, because the amino-acid residues still have a left-handed chirality. A long left-handed π-helix is unlikely to be observed in proteins because, among the naturally occurring amino acids, only glycine is likely to adopt positive φ dihedral angles such as 55°.

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