Conformational energies of substrates and inhibitors for carboxypeptidase A: stereoelectronic effect.

J K Park, S J Cho, S Lee, K S Kim, D H Kim

Index: J. Biomol. Struct. Dyn. 12(5) , 1033-40, (1995)

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Abstract

Because of the complexity involved in binding of a ligand to an enzyme the conformational preference of the bound ligand has not been well understood yet. We have examined the conformational energies of ligands for carboxypeptidase A using ab initio calculations. Considering the large stereoelectronic effect of 4-5 kcal/mol, the energetic preference of the unbound ligand conformers which arises from the stereoelectronic effect appears to play a significant role in determining the bound ligand conformations.