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. Author manuscript; available in PMC: 2022 Mar 5.
Published in final edited form as: J Mol Biol. 2021 Jan 1;433(5):166793. doi: 10.1016/j.jmb.2020.166793

Table 4. Comparison of Calculated Interchromophore Distances for CLY Constructs.

Data for each CLY protein is organized into rows as indicated in the first column. The interchromophore distances (in nm) were calculated from the FRET efficiency using several approaches: the κ2= 2/3 approximation for isotropic rotation (<Disotropic>); the κ2= 0.475 approximation for a static ensemble (<Dstatic>); a published lookup table relating FP-FRET to distance based on Monte Carlo calculations of a static FP ensemble [61] (<DMC>); using the average κ2 from the ensemble of conformations observed in DMD (<DDMD>). These are compared to the RMS population-mean interchromophore distance observed in DMD simulations (<DDMD Mean>). ND, not determined as the DMD simulations were not successful for CLY9.

Protein FRET Efficiency <Disotropic> <Dstatic> <DMC> <DSAW> <DDMD> <DDMD Mean>
CLY1 0.61 ± 0.01 4.46 ± 0.03 4.21 ± 0.03 3.81 ± 0.05 4.57 ± 0.02 4.5 ± 0.03 5.2 ± 1.5
CLY5 0.44 ± 0.02 5.01 ± 0.1 4.74 ± 0.1 4.56 ± 0.1 5.60 ± 0.04 5.0 ± 0.1 6.2 ± 1.8
CLY9 0.37 ± 0.04 5.24 ± 0.1 4.95 ± 0.1 4.85 ± 0.14 6.15 ± 0.15 ND ND