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Article

Quantification of allosteric influence of Escherichia coli phosphofructokinase by frequency domain fluorescence.

Biophysical journal - 1 Jul 2003

Pham Audrey S, Reinhart Gregory D

Abstract excerpt

The allosteric properties of the wild-type Escherichia coli phosphofructokinase were compared to the E187A mutant by using frequency-domain techniques. Tryptophan-shifted mutants comprising of double (W311Y/Y55W and W/311F/F188W) and triple (W311Y/Y55W/E187A and W311F/F188W/E187A) amino acid residue changes, which allowed for better fluorescence probing at targeted sites, were also compared to the wild-type and...

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Identifiers

PMID: 12829519
DOI: 10.1016/S0006-3495(03)74509-3
PMCID: PMC1303120

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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