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Article

Free energy simulations of active-site mutants of dihydrofolate reductase.

The journal of physical chemistry. B - 22 Jan 2015

Doron Dvir, Stojković Vanja, Gakhar Lokesh, Vardi-Kilshtain Alexandra, Kohen Amnon, Major Dan Thomas

Abstract excerpt

This study employs hybrid quantum mechanics-molecular mechanics (QM/MM) simulations to investigate the effect of mutations of the active-site residue I14 of E. coli dihydrofolate reductase (DHFR) on the hydride transfer. Recent kinetic measurements of the I14X mutants (X = V, A, and G) indicated slower hydride transfer rates and increasingly temperature-dependent kinetic isotope effects (KIEs) with systematic...

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Source

Identifiers

PMID: 25382260
DOI: 10.1021/jp5059963

Genes

DHFR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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