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Abstract
Ultraviolet difference spectra of the lactose repressor have been studied under various conditions. Changes in the aromatic residues of the protein upon addition of inducers, but not anti-inducers, are found. The extent of exposure of aromatic residues to solvent perturbation is also found to differ in the presence of inducers and anti-inducers. These differences are interpreted in terms of a change in the protein structure at points distinct from the ligand binding site.
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