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Table 2 Predicted binding energy of each mutant subunit calculated using AMBER89 and CHARMM22 force fields.

From: Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface

 

Binding energy (kcal/mol)

 

AMBER89

CHARMM22

Wild type

-249

-118

Asn340Phe/Tyr418Phe

-291

-134

Asn340Phe/Tyr418Ile

-273

-126

Thr416Val/Thr417Val

-278

-131