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Pi helix
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・ Pi Kappa Chi
・ Pi Kappa Delta
・ Pi Kappa Lambda
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Pi helix : ウィキペディア英語版
Pi helix

A pi helix (or π-helix) is a type of secondary structure found in proteins. Although once thought to be rare, short π-helices are found in 15% of known protein structures and are believed to be an evolutionary adaptation derived by the insertion of a single amino acid into an α-helix. Because such insertions are highly destabilizing, the formation of π-helices would tend to be selected against unless it provided some functional advantage to the protein. π-helices therefore are typically found near functional sites of proteins.〔
==Standard structure==

The amino acids in a standard π-helix are arranged in a right-handed helical structure. Each amino acid corresponds to an 87° turn in the helix (i.e., 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).
The majority of π-helices are only 7 residues in length and do not adopt regularly repeating (φ, ψ) dihedral angles throughout the entire structure like that of α-helices or β-sheets. Because of this, textbooks that provide single dihedral values for all residues in the π-helix are misleading. Some generalizations can be made, however. When the first and last residue pairs are excluded, dihedral angles exist such that the ψ dihedral angle of one residue and the φ dihedral angle of the ''next'' residue sum to roughly -125°. The first and last residue pairs sum to -95° and -105°, respectively. For comparison, the sum of the dihedral angles for a 310 helix is roughly -75°, whereas that for the α-helix is roughly -105°. Proline is often seen immediately following the end of π-helices. The general formula for the rotation angle Ω per residue of any polypeptide helix with ''trans'' isomers is given by the equation
:
3 \cos \Omega = 1 - 4 \cos^ \left(\left(\phi + \psi \right)/2 \right )


抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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