Alpha helices

The alpha helix is a type of secondary structure, that is, a local protein structure stabilized by hydrogen bonds. The alpha helix was first postulated as a fundamental structure in proteins in 1951 by Linus Pauling and Robert Corey.

Click here for a tour of the spacefilling model of an alpha helix.

Click here to see the alpha helix as a ball-and stick model.

The formation of hydrogen bonds that link one peptide group to another stabilize this structure. (The hydrogen bonds are shown as the dotted violet lines). All of these H-bonds are parallel to the axis of the helix.

Click here to see the nitrogen-alpha carbon-carbonyl carbon backbone of the alpha helix.

Click here to see the alpha helix as a ribbon structure.

One turn of the helix is made up of 10 atoms (3.6 residues).

Ignoring the side chains, this helix is approximately 6 Angstroms in diameter.

Any given hydrogen bond in an alpha helix encloses a loop that contains 13 atoms, from the C=O group at the start of the loop to the N-H group at the end. (The hydrogen atom of the H-bond is not shown here, so only 12 atoms are shown in this loop.)

The alpha helix is found in many proteins includine myoglobin. This protein has has seven other alpha helices.

For more information on alpha helices consult:
Garrett, R., and Grisham, C.(1999) Biochemistry, 2nd edition, Saunders College Publishing, Philadelphia, pp: 162-168.

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