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. Author manuscript; available in PMC: 2012 Jun 1.
Published in final edited form as: Exp Biol Med (Maywood). 2011 May 23;236(6):681–691. doi: 10.1258/ebm.2011.011009

Figure 1.

Figure 1

Schematic of the redox biosensor. Minimum energy configurations for dispersed cysteine residues are shown on the left – with (bottom) and without (top) locking the disulfide bonds – and were calculated in MOE (Molecular Operating Environment; Chemical Computing Group, Montreal, Canada). On the right, cartoons of the final redox-sensitive biosensor design (CY-RL7) are shown to illustrate the conformational change that leads to enhanced Förster resonance energy transfer (FRET) in the oxidized ‘clamped coil’ state compared with the reduced α-helical low-FRET state