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1.
FIGURE 3

FIGURE 3. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

The Dependence of fluorescence maximum emission wavelength on the excitation wavelength. While Nile Red maleimide in a 0.1 molar ratio of methanol in water (triangles) did not change its emission wavelength, both Cys261-NR (circles) and unfolded MDH loaded Cys261-NR (open diamonds) showed red shifts in maximum emission wavelength as excitation wavelength increased.

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.
2.
FIGURE 6

FIGURE 6. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

Sequence dependence of the time-dependent fluorescence intensity changes of Cys261-NR with ADP/AlFx. The fluorescence intensity at maximum was monitored while adding GroES and ADP/AlFx, with unfolded MDH addition at the end. (A). The sequence ES-ADP/AlFx-MDH. (B). The sequence ADP/AlFx-ES-MDH. (C) Same as (A), except long incubation (45 minutes) with ADP/AlFx, (D) Same as (B), except 1:1 molar ratio of GroEL:GroES.

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.
3.
FIGURE 7

FIGURE 7. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

Proposed scheme for the formation of symmetric/asymmetric complex of GroEL/GroES with ADP/AlFx. (A). When GroES is added first, GroES can only bind after adding ADP/AlFx, and the binding affinity of ADP/AlFx to the trans ring may be reduced because of GroES binding to the cis ring. This prevents the formation of the symmetric complex. (B). When ADP/AlFx is added first (before GroES), hindered MDH binding to the GroEL can be explained by the formation of the symmetric football complex.

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.
4.
FIGURE 1

FIGURE 1. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

The GroEL tetradecamer, which consists of two rings, is illustrated on the right (Figure 1B), and one of the monomer subunits shown in orange is expanded on the left to indicate the position of the mutation (Figure 1A). This cysteine mutant (Cys261, shown in yellow) was labeled with Nile Red maleimide. Color of the left figure (Figure 1A) corresponds the three different domains in GroEL; apical is red, intermediate is green and equatorial is blue. This crystal structure is from the x-ray structure of apo-GroEL, PDB filename 1GRL.6

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.
5.
FIGURE 2

FIGURE 2. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

Fluorescence spectra of Nile Red maleimide in methanol/water mixtures. (A) Fluorescence spectra of Nile Red maleimide were measured in water with various molar ratios of methanol. The emission maximum was red-shifted and the emission intensity decreased as solvent hydrophobicity decreased. The molar ratios of methanol in water decreasing from the top are 1 (pure methanol), 0.85, 0.65, 0.5, 0.35, 0.25, 0.2, 0.18, 0.15, 0.13, 0.1, 0.06, 0.03, 0 (pure water). (B) Expanded plot of (A), where the emission intensities of Nile Red maleimide are comparable to Cys261-NR. Inset shows that the emission intensity linearly decreases as a function of Δf in this range. Spectra of Cys261-NR and Cys261-NR with unfolded MDH are shown for comparison.

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.
6.
FIGURE 4

FIGURE 4. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

Fluorescence spectra of the Nile Red-labeled mutant GroEL (Cys261-NR, 0.2 μM) before and after the single addition of substrate, GroES, and different nucleotides (532 nm excitation). (A) Cys261-NR (rectangles) was incubated with the same amount of either unfolded (open triangles) or native MDH (open circles) at 25°C, for 20 minutes. No change in fluorescence was observed upon addition of native MDH, while unfolded MDH produced a significant increase. (B) Cys261-NR was incubated with either nucleotides (ATP (triangles), ADP (open circles), or ADP/AlFx (rectangles)) or GroES (open diamonds, 25°C, incubation times as indicated). All nucleotides and GroES induced a decrease in fluorescence compared to nucleotide-free Cys261-NR.

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.
7.
FIGURE 5

FIGURE 5. From: Probing the Sequence of Conformationally-Induced Polarity Changes in the Molecular Chaperonin GroEL with Fluorescence Spectroscopy.

(A) Kinetic measurements of the relative peak fluorescence intensity of Cys261-NR induced by the addition of denatured MDH, GroES and different nucleotides. The fluorescence intensity at maximum was monitored as a function of time, 10 s per point. MDH was added first, then GroES, and finally various nucleotides (ATP (open rectangles), ADP (open circles), or ADP/AlFx (open triangles)). Five additional analogous experiments with different sequences of adding MDH, GroES and nucleotide were also performed to observe the sequence dependence (see text). (B) Comparison of fluorescence reductions by (GroES + nt) for the two sequences of MDH-ES-nt (black bars), and ES-nt (gray bars) in the same units of part (A).

So Yeon Kim, et al. J Phys Chem B. ;109(51):24517-24525.

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