Sandbox Reserved 786
From Proteopedia
This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807. |
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The shows that it is a homo-tetramer. However the is a dimer. In the image, the alpha-helices are green, Beta-sheets are red, and random coils (turns) are grey.
Secondary Structure
The is formed by hydrogen bonding interactions of the amino acids backbone. There are two beta-sheet regions in each monomer of the natural dimer. Five beta-sheets in each monomer are anti-parallel, and form a pseudo beta-barrel motif. Six beta-sheets in each monomer show parallel configuration. The angle of the hydrogen bonds relative to one another between beta-sheets gives insight as to which beta-sheets are parallel and which are anti-parallel. Parallel beta-sheets have "crooked" h-bonding. This makes them more unstable than the anti-parallel beta-sheets which have straight h-bonds between them.