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Article

Probing the physical basis for trp repressor-operator recognition.

Journal of molecular biology - 2 Apr 1999

Grillo A O, Brown M P, Royer C A

Abstract excerpt

The bacterial repressor protein, trp repressor, is one of the best studied transcriptional regulatory proteins in terms of function, structure, dynamics and stability. Despite these significant advances, the structural and energetic basis for the specific recognition of its operator sites by trp repressor remains poorly understood. In fact, recognition in this system is controled by the binding of the...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 10092458
DOI: 10.1006/jmbi.1999.2625

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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Probing the physical basis for trp repressor-operator recognition.PMID 10092458Read ↗

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The basis for the super-repressor phenotypes of the AV77 and EK18 mutants of trp repressor.Semantic proximity Read ↗

An alkaline phosphatase protection assay to investigate trp repressor/operator interactions.Semantic proximity Read ↗

Conformational changes induced in the Tet repressor protein TetR(B) upon operator or anhydrotetracycline binding as revealed by time-resolved fluorescence spectroscopy on single tryptophan mutants.Semantic proximity Read ↗

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