Table 1.
Free energy for protection against exchange for amide hydrogens in αTS.a
| Residue | Structureb | ΔGoHXc(kcal mol-1) | mHXc(kcal mol-1M1) |
|---|---|---|---|
| F8 | α0 | 8.6(±0.1) | 0.84(±0.1) |
| G17d | loop | 8.2 | ND |
| A18 | β1 | 9.5(±0.1) | 1.0(±0.1) |
| F19 | β1 | 9.6(±(0.2) | 1.2(±0.1) |
| V20 | β1 | 8.8(±0.1) | 1.1(±0.1) |
| L25 | β1 | 8.7(±0.1) | 0.6(±0.1) |
| I36 | α1 | 9.9(±0.2) | 0.7(±0.2) |
| I37 | α1 | 11.7(±0.6) | 2.2(±0.5) |
| L40 | α1 | 10.6(±0.4) | 1.2(±0.3) |
| E42d | α1 | 7.2 | ND |
| A47 | β2 | 11.7(±0.4) | 2.0(±0.3) |
| L48 | β2 | 11.0(±0.4) | 2.0(±0.3) |
| E49 | β2 | 10.6(±0.3) | 1.8(±0.3) |
| L50 | β2 | 10.6(±0.4) | 1.9(±0.3) |
| G51 | β2 | 11.3(±0.2) | 1.6(±0.2) |
| I97 | β3 | 10.3(±0.8) | 1.7(±0.5) |
| G98 | β3 | 11.7(±0.4) | 1.8(±0.3) |
| L99 | β3 | 11.0(±0.5) | 1.7(±0.3) |
| L100e | β3 | ≥10.3 | ND |
| M101 | β3 | 10.4(±0.3) | 1.3(±0.2) |
| V121d | α3 | 6.9 | ND |
| S125 | β4 | 10.2(±0.2) | 1.3(±0.1) |
| L127 | β4 | 9.2(±0.2) | 1.3(±0.2) |
| A149 | β5 | 9.7(±0.1) | 1.3(±0.1) |
| I151 | β5 | 9.3(±0.2) | 1.6(±0.2) |
| Y175 | β6 | 9.1(±0.1) | 0.9(±0.1) |
| L176 | β6 | 8.7(±0.1) | 1.0(±0.1) |
| L209 | β7 | 8.0(±0.1) | 0.8(±0.1) |
| D225d | α7 | 6.8 | ND |
| G230 | β8 | 9.1(±0.1) | 0.7(±0.1) |
| A231 | β8 | 9.1(±0.1) | 0.7(±0.1) |
| I232 | β8 | 8.0(±0.1) | 0.7(±0.1) |
| I240d | α8′ | 6.8 | ND |
| M262 | α8 | 8.2(±0.1) | 0.6(±0.1) |
a
In the absence of urea at pH 7.8 and 25 °C; the buffer contained 50 mM potassium phosphate, 0.2 mM EDTA, 1 mM DTE.
b
The location of the residues in the secondary structure.
c
mHX values and errors for ΔGoHX were obtained from fitting the protection data to ΔGHX= ΔGoHX - mHX[urea].
d
Estimates of ΔGHX were based upon the measurement of exchange in the absence of urea; the mHX values were not determined.
e
ΔGoHX for L100 represents a minimum estimate. The scatter in the data prevented accurate determination.