Table 1 Thermodynamic parameters for binding interactions of ligand-hits with TphC.

From: Structural basis of terephthalate recognition by solute binding protein TphC

Ligand

N sitesa

KD (µM)b

ΔG (cal/mol)

ΔH (cal/mol)

TΔS (cal/mol)

Terephthalate (1)

1.04

0.364

−8672.28

−9602 ± 38.92

−885.45

2-Hydroxyterephthalate (4)

1.13

1.246

−7976.70

−9054 ± 31.21

−1077.30

2,5-Dihydroxyterephthalate (10)

1.08

1.931

−7715.59

−9699 ± 27.09

−1983.41

2-Aminoterephthalate (7)

1.14

119.9

−5294.95

−5493 ± 43.00

−198.05

2,5-Pyridinedicarboxylate (2)

1.01

90.9

−5458.29

−5963 ± 40.74

−504.71

2,6-Naphthalenedicarboxylate (22)

1.14

869.6

−4133.46

−3614 ± 134.3

519.46

  1. aN represents the stoichiometric ratio of protein:ligand interaction.
  2. bA higher affinity for terephthalate disodium and its 2-hydroxy- and 2,5-dihydroxy derivatives was observed.
Back to article page