Skip to main content

Advertisement

Table 2 Comparison of KD values for the wild type and mutant 6 × His-ATD2B proteins.

From: Structural insights into phenylethanolamines high-affinity binding site in NR2B from binding and molecular modeling studies

Protein KD (nM) Fold Shift
WT 60 ± 18 1
F176A 331 ± 122 5.5
D101A 173 ± 52 2.9
F176A/D101A 627 ± 295 10.5
I150A 139 ± 28 2.3
D113A 48 ± 15 0.8
  1. Values are mean ± S.E. of the KD values from five experiments using proteins obtained from at least two independent batches of bacteria induction. The fold shift in KD values for each mutant is the ratio of KD(mutant) to KD(WT).