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Article

Strengthening the dimerisation interface of Lac repressor increases its thermostability by 40 deg. C.

Journal of molecular biology - 9 Jun 2000

Gerk L P, Leven O, Müller-Hill B

Abstract excerpt

We increased drastically the heat stability of Lac repressor (LacR) of Escherichia coli. Wild-type tetrameric LacR denatures irreversibly at 53 degrees C. Improving hydrophobic packing at the dimerisation interface by a single substitution increases LacR heat-resistance by 40 deg. C without abolishing inducer binding at high and low temperatures. Tetrameric LacR mutants carrying substitutions of the positively...

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Share to Allosteric Regulation
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Share to Isopropyl Thiogalactoside

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

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Source

Identifiers

PMID: 10835285
DOI: 10.1006/jmbi.2000.3706

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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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