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Article

The coupling of structural fluctuations to hydride transfer in dihydrofolate reductase.

Proteins - 15 Nov 2004

Thorpe Ian F, Brooks Charles L

Abstract excerpt

The energy barrier for hydride transfer in wild-type G121V and G121S variants of Escherichia coli dihydrofolate reductase (DHFR) fluctuates in a time-dependent manner. This fluctuation may be attributed to structural changes in the protein that modulate the site of chemistry. Despite being far from the active site, mutations at position 121 of DHFR reduce the hydride transfer rate of the enzyme. This occurrence...

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Source

Identifiers

PMID: 15382243
DOI: 10.1002/prot.20219

Genes

DHFR

Provenance

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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