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Article
Nature 316, 601 - 605 (15 August 1985); doi:10.1038/316601a0

Changing the binding specificity of a represser by redesigning an alpha-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 alpha-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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