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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

 

Mutant

 

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.