Abstract

The repressor of the lac operon in Escherichia , coli undergoes a distinct conformational change upon addition of a specific inducer isopropyl-β-D-thiogalactoside (IPTG), which is evidenced by changes in ultraviolet absorption spectrum, sedimentation coefficient and in circular dichroism spectrum. The significance of the conformational change reported here is discussed in relation to the allosteric properties of the repressor.

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