Table 2.
Comparison of measured chemical shifts in wt and mutant MoPrP(89–143) peptides
| Label | Expected chemical
shifts
|
Experimental chemical shifts
|
||
|---|---|---|---|---|
| α-Helix | β-Sheet | wt* | P101L, converted | |
| G93 Cα | Unknown | 43.2 | 42.8 | 42.3 |
| A114 Cα | 52.5 | 48.7 | 52.6; 48.3 | 48.4 |
| V120 Cα | 65.5 | 58.3 | 64.1; 57.8 | 58.1 |
| A132 Cβ | 15.1 | 20.1 | 15.05; 20.88 | 20.6 |
| M128 C0 | 175.1 | 170.6 | 174.9; 170.6† | 170.4 |
| G141 C0 | 171.8 | 168.5 | 170.6†; 169.3 | 168.9 |
Typical α-helical and β-sheet chemical shifts of peptides in solids are listed. All chemical shifts are in ppm, externally referenced to tetramethylsilane via the 13C0 resonance in glycine (176.04 ppm).
*
Two conformations were present in the wt peptide. Shifts for both conformations are listed, with the α-helical chemical shifts listed first.
†
The M128 C0 sheet chemical shift overlaps with the G141 C0 helix chemical shift, and so the two cannot be distinguished in the spectra.