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J Biomol Struct Dyn. 1995 Apr;12(5):1033-40.

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

Author information

1
Center for Biofunctional Molecules, Pohang University of Science and Technology, Korea.

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.

PMID:
7626238
DOI:
10.1080/07391102.1995.10508795
[Indexed for MEDLINE]

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