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The Zn finger provides a model for studies of protein structure and stability. Its core contains a conserved phenylalanine residue adjoining three architectural elements: a β-hairpin, an α-helix and a tetrahedral Zn 2+ -binding site. Here, we demonstrate that the consensus Phe is not required for high-affinity Zn 2+ binding but contributes to the specification of a precise DNA-binding...
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