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Article

Structure, dynamics, and catalytic function of dihydrofolate reductase.

Annual review of biophysics and biomolecular structure - 1 Jan 2004

Schnell Jason R, Dyson H Jane, Wright Peter E

Abstract excerpt

Molecular motions are widely regarded as contributing factors in many aspects of protein function. The enzyme dihydrofolate reductase (DHFR), and particularly that from Escherichia coli, has become an important system for investigating the linkage between protein dynamics and catalytic function, both because of the location and timescales of the motions observed and because of the availability of a large amount...

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Source

Identifiers

PMID: 15139807
DOI: 10.1146/annurev.biophys.33.110502.133613

Genes

DHFR

Provenance

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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Structure, dynamics, and catalytic function of dihydrofolate reductase.PMID 15139807Read ↗

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