Protein Secondary Structure - Alpha Helix
The alpha helix is a type of protein secondary structure first postulated as a fundamental structure of proteins in 1951 by Linus Pauling and Robert Corey.
(see http://www.pnas.org/site/misc/classics1.shtml).
Rotate the molecule and observe the helical structure formed by the amino acid chain. All alpha helices are right handed.
The spacefilling model depicts the van der Waals radii of each atom, but the ball and stick model is more useful for examining the arrangement of the atoms.
The alpha helix is stabilised by a series of hydrogen bonds that form between the backbone C=O and H-N groups. There are 3.6 amino acids per turn of the helix, which places the C=O group of amino acid (i) exactly in line with the H-N group of amino acid (i+4).
The alpha helix is sometimes depicted as a helical ribbon with an arrow showing the N- to C-terminal direction of the amino acid chain.
Page skeleton and JavaScript generated by the Export to Web module of Jmol 14.29.29 on 23/01/2019.
