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Article

Equilibrium folding studies of tetrameric R67 dihydrofolate reductase.

Biochemistry - 12 Apr 1994

Zhuang P, Eisenstein E, Howell E E

Abstract excerpt

R67 dihydrofolate reductase (DHFR) is an R-plasmid encoded enzyme that confers resistance to the antibacterial drug trimethoprim. This enzyme is not homologous in sequence or structure to chromosomal DHFRs. Equilibrium folding of tetrameric R67 DHFR was studied and found to be fully reversible. Formation of an inactive intermediate was assayed by loss of enzyme activity. Denaturation of the intermediate was...

Topics

Anilino Naphthalenesulfonates
Calorimetry, Differential Scanning
Circular Dichroism
Guanidine
Guanidines
Mutation
NADP
Protein Denaturation
Protein Folding
Spectrometry, Fluorescence
Tetrahydrofolate Dehydrogenase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Thermodynamics

Source

Identifiers

PMID: 8155640
DOI: 10.1021/bi00180a018

Genes

DHFR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8155640-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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