Table 3.
Comparison of measured chemical shifts in wt and mutant SHaPrP(89–143)
| Label | Expected chemical
shifts
|
Experimental chemical shifts
|
||
|---|---|---|---|---|
| α-Helix | β-Sheet | wt | 3AV, converted | |
| G93 Cα | Unknown | 43.2 | 42.8 | 42.8 |
| G113 C0 | 171.8 | 168.5 | 171.7 | 169.5 |
| V114 Cα | 65.5 | 58.3 | — | 57.6 |
| A119 Cα | 52.5 | 48.7 | 52.0 | 49.2 |
| A132 Cα | 15.1 | 20.1 | 15.6 | 20.6 |
| M128 C0 | 175.1 | 170.6 | 174.7 | 170.8 |
Typical α-helical and β-sheet chemical shifts in solid-state peptides are listed. All chemical shifts are in ppm, externally referenced to tetramethylsilane via the 13C0 resonance in glycine (176.04 ppm).