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Article

Energetic analysis of binding of progesterone and 5 beta-androstane-3,17-dione to anti-progesterone antibody DB3 using molecular dynamics and free energy calculations.

Protein engineering - 1 Oct 2001

Peräkylä M, Nordman N

Abstract excerpt

Molecular dynamics simulations and molecular mechanics-Poisson-Boltzmann surface area (MM-PBSA) free energy calculations were used to study the energetics of the binding of progesterone (PRG) and 5 beta-androstane-3,17-dione (5AD) to anti-PRG antibody DB3. Although the two steroids bind to DB3 in different orientations, their binding affinities are of the same magnitude, 1 nM for PRG and 8 nM for 5AD. The...

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Identifiers

PMID: 11739893
DOI: 10.1093/protein/14.10.753

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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