. Author manuscript; available in PMC: 2010 May 31.

Published in final edited form as: J Am Chem Soc. 2008 Mar 15;130(15):5140–5149. doi: 10.1021/ja077972s

Table 5.

Mutation-caused shifts of free energy barrier (ΔG_av in kcal/mol) calculated for cocaine hydrolysis catalyzed by the antibody mutants in comparison with available experimental data.

antibody	Calc.		Expt.
antibody	ΔΔG_av^a	Relative ΔG_av^b	Relative activity^c	Relative ΔG_av^b
Wild-type	−6.33	0	100%	0
AsnH33Ala	−2.83	3.50	0% (i.e. < 0.5%)	> 3.14
TyrH35Phe	−5.08	0.55	24%	0.85

The free energy barrier shift from the cocaine hydrolysis in water to the antibody-catalyzed cocaine hydrolysis corresponding to the wild-type antibody and its mutants.

Mutation-caused shift of the free energy barrier, i.e. ΔΔG_av – ΔΔG_av (wild-type). The experimental shifts are derived from the experimental relative activity data (i.e. < 0.5% and 24%).

Experimental activity of the mutant relative to the wild-type antibody (data from ref. 6).