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Table 1 Characteristics of destabilizing mutations engineered into E. coli β-galactosidase

From: The rate of the molecular clock and the cost of gratuitous protein synthesis

  V567D F758S I141N G353D A880E
Predicted ΔΔG (kcal/mol) -2.6 -2.9 -2.4 -1.6 -0.6
Relative protein activity (%) 31 4 17 2 61
Codon substitution (WT/mutant) GTC/GAC TTT/TCT ATT/AAT GGC/GAC GCG/GAG
Codon preference % (WT/mutant) 13.5/53.9 29.0/32.4 33.5/17.3 42.8/53.9 32.3/24.7
Found in inclusion bodies (see Figure 1a) No Yes Yes Yes No
  1. In the table, ΔΔG values represent destabilizing effects predicted by the I-Mutant2.0 server [32]. The experimentally determined enzymatic activities of the mutants (in percentages) are shown in the table relative to WT.