Table 1.
Temperature dependent thermodynamics for the titration of tryptophan into TRAPa
| Temperature | n | ΔG | ΔH | TΔS | KA (/106) |
|---|---|---|---|---|---|
| 298 | 10.97 ± 0.03 | -9.55 ± 0.06 | -13.88 ± 0.09 | -4.33 ± 0.11 | 9.75 ± 0.16 |
| 303 | 11.07 ± 0.09 | -9.43 ± 0.01 | -15.60 ± 0.06 | -6.17 ± 0.07 | 6.28 ± 0.24 |
| 308 | 10.77 ± 0.29 | -9.35 ± 0.01 | -17.37 ± 0.07 | -8.02 ± 0.07 | 4.24 ± 0.05 |
| 313 | 10.40 ± 0.10 | -9.22 ± 0.32 | -19.13 ± 0.25 | -9.91 ± 0.41 | 2.72 ± 0.16 |
| 318 | 10.16 ± 0.23 | -9.13 ± 0.01 | -21.10 ± 0.43 | -11.97 ± 0.43 | 1.83 ± 0.04 |
| 323 | 10.53 ± 0.24 | -8.98 ± 0.02 | -23.03 ± 0.04 | -14.05 ± 0.05 | 1.17 ± 0.05 |
a
Reported errors are the standard deviation of three repeat data sets at each temperature. Values of ΔΗ, ΤΔS, and ΔG are in kcal mol-1, T is in Kelvin, KA is in M-1, and n is the number of tryptophan binding sites per TRAP oligomer.