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Looking down a helix
In an α-helix each residue sits about 100° around the axis from the one before it, and 3.6 residues make a full turn. A helical-wheel projection looks down that axis and places residue n at (n − 1) × 100°, counting from the first. Drawing a line from each residue to the next traces the star you see in Sequence Studio.
Fig. 1 · Helical wheel
Computed from the sequence
Residue colors: Hydrophobic Polar Basic (+) Acidic (−)
Color is chemistry
Each residue takes the color of its side-chain class:
- Amber
- Hydrophobic. Here the class also includes glycine and proline.
- Green
- Polar.
- Blue
- Basic. Lysine and arginine are positively charged at neutral pH; histidine (side-chain pKa about 6.5) is mostly neutral.
- Red
- Acidic: negatively charged at neutral pH.
- Gray
- Non-standard residues, such as Aib or 2-naphthylalanine.
The arrow
The arrow is the hydrophobic moment: the vector sum of each residue’s hydropathy pointing out from its position. If hydrophobic residues cluster on one side of the wheel, the arrow points to that face and is long; an even mix gives a short arrow. Amphipathic helices, such as many antimicrobial peptides, show strong moments.
A caveat
The projection assumes an ideal α-helix. Short peptides, proline-rich sequences and many of the peptides we list don’t form stable helices, so for them the wheel is a consistent way to picture the sequence rather than a claim about its structure.