Table 3.

Comparative docking interaction energies and protein stabilities for ALDH2 and ALDH1B1 subunits.^a

Trimer	Monomer	Interaction energy (kcal/mol)	% change from homotetramer	Protein stability (kcal/mol)	% change from homotetramer
ALDH1A1	ALDH1A1	−352.75	–	−102570.56	–
ALDH1A1	ALDH1A1 homology from ALDH2	−320.00	9.28	−102306.17	0.26
ALDH2	ALDH2	−363.90	–	−109639.68	–
ALDH2	ALDH2 homology from ALDH1A1	−281.96	22.52	−109915.10	−0.25
ALDH2	ALDH2*2	−323.77	11.03	−109298.92	0.31
ALDH1B1	ALDH1B1	−308.87	–	−115686.15	–
ALDH1B1	ALDH2	−445.60	−44.27	−114127.71	1.35
ALDH1B1	ALDH2*2	−367.23	−18.89	−114295.66	1.20

^aEnergies for the binding of an ALDH monomer to an ALDH trimer were calculated in silico. The interaction energy parameter for each indicates the energy of interaction between the monomer and the trimer, whereas the protein stability parameter represents the calculated total stability of the final protein tetramer in solution.