Table 2 In silico mutagenesis and affinity/stability analysis and calculations.

From: Strategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form

T16F

Δaffinity (kcal/mol)

Δstability (kcal/mol)

Homodimer

−14.23

−19.88

Monomer

—

−4.82

  1. Δaffinity values report the change in binding affinity within protomers between the wild type and VbTA T16F mutant; Δstability values report the changes in protein (monomer or homodimer) stability occurring after the mutation; stability is defined as the difference in energy between the folded and unfolded states. Δaffinity and Δstability data are calculated using an implicit solvent MM-GBSA method.
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