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. Author manuscript; available in PMC: 2010 Oct 5.
Published in final edited form as: J Phys Chem C Nanomater Interfaces. 2009 Oct 5;113(43):18552–18561. doi: 10.1021/jp9060329

Figure 6. Correlations between b-PE structure and FRET data.

Figure 6

(A) Schematic representation of possible conformations. θQD:b-PE is the angle between the QD-b-PE center-to-center axis and the axis perpendicular to the b-PE structure. RQD:b-PE is the QD-b-PE center to center separation distance. (B) QD-b-PE center-to-center distances estimated from FRET efficiencies and plotted versus RQD:b-PE (correspond to 0° ≤ θQD:b-PE ≤ 90°) for 540 nm (circles) and 520 nm (triangles) QDs. (C) Schematic mapping of the FRET efficiency for the QD-b-PE conjugate showing the effects of distance and distribution of the chromophores in the protein. Two representative b-PE conformations (dotted) along with the region explored by all possible conformations sampled by the protein on the nanocrystal (dashed). The color intensities indicate the FRET efficiencies between the QD and individual dyes in the b-PE (see bar on the right).