alpha helix

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alpha helix

[′al·fə ′hē·liks]
(cell and molecular biology)
A spatial configuration of the polypeptide chains of proteins in which the chain assumes a helical form, 0.54 nanometer in pitch, 3.6 amino acids per turn, presenting the appearance of a hollow cylinder with radiating side groups.
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It's the first example of an alpha-helical inhibitor of any protease.
The five domains include 1) a signal peptide, 2) an alpha-helical charged domain (amino acids 1-288), 3) a proline-rich region (amino acids 289-370), 4) a choline-binding domain consisting of 9 to 10 twenty-amino-acid repeats (amino acid 371-571), and 5) a C-terminal 17-amino-acid tail (amino acids 572-589).
Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil.
a molecular biologist at the University of California, Berkeley, and his colleagues have used the alpha-helical strands of proteins to engineer a benzene-sensitive switch.
AILERON's Stapled Peptides are synthetically locked, or 'stapled', into an alpha-helical shape with an optimized cross-linking chemistry to mimic the structure found at the interface of many protein-protein interactions.