Table 1. 3J(HN,Hα) coupling constants (Hertz) in water and coil library data.
| Residue | Dipeptide* pH 2.9 | Dipeptide* pH 4.9 | Coil† | GGXGG‡ GdmCl | fβ-coil§ | fβ-uls¶ |
|---|---|---|---|---|---|---|
| Gly | 5.90 | 5.85 | 5.720 | N.D. | 0.031 | 0.291 |
| Ala | 6.02 | 6.06 | 6.075 | 6.1 | 0.144 | 0.271 |
| Val | 7.32 | 7.30 | 7.547 | 7.2 | 0.392 | 0.534 |
| Ile | 7.37 | 7.33 | 7.495 | 7.1 | 0.359 | 0.500 |
| Leu | 6.84 | 6.88 | 6.991 | 6.8 | 0.201 | 0.345 |
| Phe | 7.17 | 7.18 | 7.351 | 7.3 | 0.304 | 0.506 |
| Met | 7.09 | 7.02 | 6.974 | 7.1 | 0.230 | 0.401 |
| Trp | 6.92 | 6.91 | 7.007 | 7.0 | 0.257 | 0.453 |
| Cys | 7.30 | 7.31 | 7.103 | 7.3 | 0.259 | 0.437 |
| Ser | 7.05 | 7.02 | 6.615 | 7.0 | 0.221 | 0.421 |
| Thr | 7.32 | 7.35 | 7.642 | 7.9 | 0.296 | 0.538 |
| Asn | 7.50 | 7.45 | 7.294 | 7.7 | 0.153 | 0.424 |
| Gln | 7.06 | 7.14 | 7.050 | 7.1 | 0.223 | 0.430 |
| Tyr | 7.12 | 7.13 | 7.318 | 7.8 | 0.286 | 0.484 |
| His | 7.76 | 7.89 | 7.177 | 7.2 | 0.248 | 0.505 |
| Asp | 7.51 | 6.93 | 6.931 | 7.8 | 0.132 | 0.322 |
| Glu | 7.02 | 6.63 | 6.495 | 6.7 | 0.174 | 0.351 |
| Lys | 6.85 | 6.83 | 6.920 | 7.0 | 0.229 | 0.447 |
| Arg | 6.91 | 6.85 | 6.920 | 6.9 | 0.229 | 0.440 |
The dipeptide coupling constants are independent of peptide concentration, both at pH 2.9 and 4.9, except for the value of His at pH 4.9. The temperature is 30°C. The pH 4.9 values of the dipeptide coupling constants (J-dipep) are discussed in the text.
Average coupling constants (J-coil) computed from residue φ-values in the coil library (see Materials and Methods).
These coupling constants (29) (J-GGXGG) were measured for residue X in blocked GGXGG peptides in 6 M GdmCl (pH 5.0) at 20°C.
The fraction of residues in the coil library β basin (-180° < φ < -100°; 90° < ψ < 180°) divided by all residues in the φ, ψ map of this amino acid type.
The fraction of residues in the coil library β basin when divided by the number of residues in the upper left strip (-180° < φ < 0°; 90° < ψ < 180°) of the φ, ψ map.