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Results: 8

1.
Figure 3

Figure 3. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Sequence plot of Fst and Fst1−27. The strengths of the NOEs are indicated by the thicknesses of the bars.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
2.
Figure 8

Figure 8. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Time evolution of the secondary structure of the two Fst toxin peptides.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
3.
Figure 7

Figure 7. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Residue root-mean-square fluctuation: average RMSF of each residue, averaged over the entire simulation, and both peptides are shown together with the standard deviation.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
4.
Figure 4

Figure 4. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Least-squares superposition of the 20 lowest energy structures of Fst showing all atoms (a) or the backbone only (b). The backbone atoms of residues 5−25 were used for the fitting.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
5.
Figure 5

Figure 5. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Longitudinal (R1) paramagnetic relaxation enhancements (PREs) of Fst obtained by adding Gd(DTPA-BMA). Only values of well-resolved peaks with correlation coefficients of least-squares fits higher than 0.98 were used. A low PRE is indicative of a larger distance from the micelle surface.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
6.
Figure 6

Figure 6. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Representative structures of Fst of a 50 ns MD simulation run. The peptide is shown as a color-coded ribbon (red = negatively charged, blue = positively charged, green = polar, including glycine, and white = unpolar). The phosphate headgroups are indicated by blue spheres.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
7.
Figure 1

Figure 1. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

Overlay of the fingerprint region of 2D TOCSY spectra of Fst (red) and Fst1−27 (black) at 301 K. Correlations between amide protons and α-protons are indicated by the residue numbers. Cross-peaks between NH and other (non-α) protons are indicated by the position in the side chain.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.
8.
Figure 2

Figure 2. From: Solution Structure and Membrane Binding of the Toxin Fst of the par Addiction Module.

CD spectra of Fst (filled circles) and Fst1−27 (empty circles) in 100 mM TPC solution showing the mean residue ellipticity (mre) per residue versus the wavelength. The reduced mean residual ellipticity of Fst is a result of the intrinsically disordered C-terminus.

Christoph Göbl, et al. Biochemistry. 2010 August 10;49(31):6567-6575.

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