Sugiura, Y.

Acc. Chem. Res. 2006, 39, 45-52, 10.1021/ar050158u

The design of artificial functional DNA-binding proteins has long been a goal for several research laboratories. The zinc finger proteins, which typically contain many fingers linked in tandem fashion, are some of the most studied DNA-binding proteins. The zinc finger protein's tandem arrangement and its the ability to recognize a wide variety of DNA sequences make it an attractive framework to design novel DNA-binding peptides/proteins. Our laboratory has utilized several design strategies to create novel zinc finger peptides by re-engineering the C2H2-type zinc finger motif of transcription factor Sp1. Some of the engineered zinc fingers have shown nuclease and catalytic functional properties. Based on these results, we present the design strategies for the creation of novel zinc fingers.

Birnbaum, E.R.; Darnall, D.W.

J. Biol. Chem. 1970, n/a

The rate of activation of the conversion of trypsinogen to trypsin has been found to be greatly accelerated by the neodymium(III) ion. The similarity of this process to the calcium(II) ion activation suggests that both metal ions bind at identical sites in trypsinogen. The rate of activation in the presence of the neodymium ion is much greater than that of the calcium ion, probably reflecting the increased stability constant of the neodymium-protein complex. In contrast to the calcium ion, however, neodymium(III) can be scrutinized by a variety of spectral and magnetic techniques which should reveal information concerning the calcium ion binding sites in proteins. Since the chemistry and the range of sires of the rare earth metal ions are so similar to that of the calcium ion, it is suggested that generally these ions should make good replacement ions for probing the calcium ion binding sites of proteins and enzymes.