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Changing the binding specificity of a represser by redesigning an -helix Robin P. Wharton & Mark Ptashne
Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts 02138, USA
We replaced amino acids on the 'outside', or solvent-exposed, surface of the DNA recognition -helix of 434 repressor with the corresponding amino acids from the recognition helix of P22 repressor. The binding specificity of the resulting hybrid protein, as measured in vivo and in vitro, was that of P22 repressor.
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