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Perround et al. 10.1073/pnas.0508975102. |
Fig. 7. Experimental PCH fit with different models for TMR-cytochrome c labeled at a 1:50 ratio: one-species model, fixed F (black); two- or three-species model (red). The difference between the two- and three-species model is negligible on this plot. The histogram was built with a bin time of 20 ms. The fitting results are listed in Table 4.
Fig. 8. Absorbance spectra of TMR-cytochrome c as a function of labeling molar ratio. (A) Absorbance spectra for TMR-cytochrome c labeled at 1:50 (black), 1:10 (red), 1:5 (green), and 2:1 (blue) labeling molar ratios and normalized to the Soret band at 412 nm. (B and C) Absorbance spectra of conjugated TMR after subtraction of the unlabeled cytochrome c spectrum (B) and after normalization to the fluorescent TMR absorbance peak at 550 nm (C).
Fig. 9. Absorbance and fluorescence spectra of TMR-cytochrome c as a function of pH. (A and B) Effect of pH on the shape of the absorbance spectra of TMR-cytochrome c labeled at 2:1 labeling molar ratio (A) and 1:5 labeling molar ratio (pH 7.0, 7.8, 8.6, 9.4, 10.0, 10.8, and 12.0: black, red, green, blue, cyan, magenta, and gray) (B). (C) Fluorescence emission spectra of TMR-cytochrome c for any labeling molar ratio (pH 7.0, 9.5, and 11.8: black, red, and blue).
Fig. 10. CD spectra of unlabeled (·) and TMR labeled cytochrome c (○).
Fig. 11. The fluorescence of TMR-cysteine is not sensitive to pH changes. The small fluorescence decrease arises from dilution.
Fig. 12. Dependence of the PCH parameters on the concentration of cytochrome c and on laser power. (A and C) The average number of molecules of each species 
correlates with concentration (A) but not with laser power (C). (B and D) The molecular brightness of each species ei correlates with laser power (D) but not with concentration (B). ● = species 1, left axes; ○= species 2, right axes.
Fig. 13. Evolution of 
with time after labeling.
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