Table 1 Comparison of observed 13C shifts and known values for amino acids in a given secondary structure.
From: Protein secondary structure in spider silk nanofibrils
Amino acid | Peak | Recluse silk [ppm] | Literature assignmenta | Range [ppm]a |
|---|---|---|---|---|
Ala | Cα main peak | 48.9 | β-sheet | 48.2–49.3 |
Ala | Cα shoulder | 53.3 | α-helix | 52.3–52.8 |
Ala | Cβ main peak | 20.4 | β-sheet | 19.9–20.7 |
Ala | Cβ shoulder | 16.7 | Random-coil | 15.7–17.1 |
Ala | COb | 172.5 | β-sheet | 171.6–172.4 |
Gly | Cα | 42.7 | 31-helix | 41.4–42.5 |
Gly | COb | 172.5 | 31-helix | 171.2–173.1 |
Gly | CO shoulder | 169.5 | β-sheet | 168.4–169.7 |
