Table 1.
Thermodynamic parameters obtained from hydrogen exchange data
| Residuea | ΔG°opapo (kcal/mol) | ΔG°opF (kcal/mol) | ΔG°opB (kcal/mol) | 2° Structure |
| Phe 10b | 4.1 ± 0.014d | — | β1 | |
| Val 11 | 4.3 ± 0.008 | 4.1 ± 0.08 | 6.4 ± 0.18 | β1 |
| Ala 12 | 5.1 ± 0.006 | 4.8 ± 0.05 | β1 | |
| Leu 13b | 4.0 ± 0.013 | — | β1 | |
| Tyr 14 | 4.8 ± 0.008 | 4.5 ± 0.03 | β1 | |
| Asp 15c | — | 3.3 ± 0.26 | 4.7 ± 0.09 | β1 |
| Tyr 16 | 4.7 ± 0.010 | 4.8 ± 0.15 | β1 | |
| Asp 23c | — | 2.1 ± 0.20 | 4.4 ± 0.18 | β2 |
| Leu 24 | 3.4 ± 0.013 | 3.1 ± 0.04 | β2 | |
| Ser 25 | 4.6 ± 0.008 | 5.7 ± 0.75 | 5.5 ± 0.07 | β2 |
| Phe 26 | 4.7 ± 0.011 | 4.5 ± 0.05 | β2 | |
| Lys 27 | 4.7 ± 0.011 | 4.6 ± 0.09 | 6.9 ± 0.17 | β2 |
| Lys 28 | 4.7 ± 0.012 | 4.4 ± 0.05 | β2 | |
| Gly 29 | 4.4 ± 0.016 | 4.6 ± 0.51 | 5.6 ± 0.08 | β2 |
| Glu 30 | 4.2 ± 0.007 | 4.0 ± 0.05 | β3 | |
| Leu 32 | 4.6 ± 0.009 | 4.4 ± 0.05 | β3 | |
| Gln 33 | 4.7 ± 0.010 | 4.5 ± 0.06 | 7.6 ± 0.65 | β3 |
| Trp 43 | 4.9 ± 0.019 | 4.2 ± 0.05 | β4 | |
| Ala 45 | 5.1 ± 0.010 | 4.8 ± 0.05 | β4 | |
| His 46 | 4.9 ± 0.047 | 4.8 ± 0.06 | β4 | |
| Ser 47 | 4.6 ± 0.104 | 5.2 ± 0.05 | 8.7 ± 0.23 | β4 |
| Gln 52c | — | 4.3 ± 0.48 | 4.4 ± 0.04 | β5 |
| Gly 54 | 4.9 ± 0.013 | 4.7 ± 0.05 | β5 | |
| Tyr 55 | 4.7 ± 0.012 | 4.5 ± 0.05 | β5 | |
| Ile 56 | 5.1 ± 0.021 | 4.8 ± 0.30 | 8.1 ± 1.16 | β5 |
| Ser 58 | 4.6 ± 0.054 | 5.0 ± 0.12 | 310 | |
| Asn 59c | — | 3.8 ± 0.85 | 6.7 ± 0.43 | 310 |
| Tyr 60 | 4.3 ± 0.014 | 3.8 ± 0.06 | 310 | |
| Val 61 | 4.5 ± 0.009 | 4.1 ± 0.03 | β6 | |
| Ala 62 | 4.9 ± 0.008 | 4.5 ± 0.06 | 7.5 ± 0.51 | β6 |
a Residues are numbered as in Feng et al. 1994.
b Exchange not measured in ligand complex due to spectral overlap.
c Exchange in apo SH3 is too rapid to measure accurately.
d Errors given are calculated from the standard error of the fit, and are intended only to indicate the quality of the data. Uncertainty in krc introduces an error of approximately 0.4 kcal/mol in all values of ΔG°.