Results 161 to 170 of about 36,597 (195)
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Isolation and characterization of frameshift mutations in the lac operon

Journal of Molecular Biology, 1970
Abstract A set of lac − mutations has been isolated in cells of Escherichia coli after mutagenesis with ICR-191D, an acridine half-mustard known to cause frameshifts in bacteria. The mutations in the β-galactosidase gene ( z ) were studied and shown to have properties consistent with their assignment to the frameshift class: they are revertible ...
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Characteristics of tight binding repressors of the lac operon

Journal of Molecular Biology, 1981
Abstract A number of tight binding lac repressor mutants (Itb) have been analyzed. The mutant repressors could be shown to have altered DNA binding properties, which can include an increased affinity for operator DNA, an increased affinity for non-specific DNA, or a decreased affinity for non-specific DNA.
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Lac Operon Mutations

A complex educational module designed to evaluate students’ capacity in applying knowledge of mutations within the lactose operon system of bacteria. Through this module, students will gain proficiency in correlating mutations with genotypes to make predictions about phenotypes in diverse environmental conditions.
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The Mechanism of Activation of the Lac Operon

1972
The lac operon consists of a cluster of genes found on the single chromosome of the bacterium Escherichia coli. Starting from one side the cluster contains a promoter, an operator, the structural genes for β-galactosidase, permease and thiogalactoside transacetylase.1 Such a grouping of regulating and structural genes is termed an operon. In 1961 Jacob
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The lac and gal Operons Today

1996
In 1961, Jacob and Monod proposed the operon model of gene expression and its negative control primarily from the experimental results obtained by these authors and their colleagues studying the induced synthesis of proteins involved in the utilization of sugar lactose and development of bacteriophage X from a prophage state in Escherichia coli.
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Understanding the lac operon with GeneAct

International Journal of Computational Biology and Drug Design, 2015
Xiaoli Yang   +3 more
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Allostery in the lac operon: Population selection or induced dissociation?

Biophysical Chemistry, 2011
Allostery, the modulation of function of a protein at one site by the binding of a ligand at a different site, is a property of many proteins. Two kinetically distinct models have been proposed: i) The induced fit model in which the ligand binds to the protein and then induces the conformational change.
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lac Operon

2004
Liskin Swint-Kruse, Kathleen S. Matthews
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Transcription | lac Operon Regulation

2021
Liskin Swint-Kruse   +2 more
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