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. 2015 Oct 26;7(2):1200–1204. doi: 10.1039/c5sc03705k

Fig. 4. The activity of the hemin-Gs in bivalent TSDzyme constructs is dependent on their spacing. (a) Schematic of the bi-hemin-Gs we inserted into TSDzymes. (b) The CD spectra of these confirm that they retain the parallel G-quadruplex conformation of the free G-quadruplex. (c) The catalytic activity of the bi-hemin-Gs increases with increasing spacer length, as shown by the generated Kcat values of various bi-hemin-Gs.

Fig. 4