- Yes, the letters are amino acids
- It's a schematic with a whole residue as a circle —possibly from Voet and Voet.
- Residue
i
is the one in focus, the reference. i-1
is the preceding residue. Have a gander at en.wikipedia.org/wiki/Turn_(biochemistry) where this type of relative notation is important.
The diagram shows how secondary structure (helices, sheets etc.) affect the distance between the residues. In a helix a residue 3 positions down will be close, but not in a sheet.
However, for assignment of secondary structure it may be easier to look at the φ and ψ angles:
- α helix: phi=-57.8, psi=-47.0
- π helix: phi=-57.1, psi=-69.7
- 3.10 helix: phi=-74.0, psi=-4.0
- β sheet: phi=-139, psi=+135
Although these have a range and you can get π bulges within α helices —important for conformation switching for pore opening (capsaicin binding to TRPV1 is a classic example).
i
is the one in focus, the reference. i-1 is the preceding residue. Have a gander at en.m.wikipedia.org/wiki/Turn_(biochemistry) where this type of relative notation is important. $\endgroup$