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Image segmentation of nuclei in <t>Imaris</t> (A) Import images into Imaris and click convert into Imaris <t>File</t> <t>Format</t> (red box). (B) Click on the surface icon (red box) in the surpass window to start creation of a nuclear surface.
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Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
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Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
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Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
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Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
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Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM <t>Tris</t> (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.
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Image Search Results


Image segmentation of nuclei in Imaris (A) Import images into Imaris and click convert into Imaris File Format (red box). (B) Click on the surface icon (red box) in the surpass window to start creation of a nuclear surface.

Journal: STAR Protocols

Article Title: Protocol to differentially quantify spatially resolved viral protein-cellular protein interactions via proximity ligation assays

doi: 10.1016/j.xpro.2026.104361

Figure Lengend Snippet: Image segmentation of nuclei in Imaris (A) Import images into Imaris and click convert into Imaris File Format (red box). (B) Click on the surface icon (red box) in the surpass window to start creation of a nuclear surface.

Article Snippet: Import image into the Imaris Arena ( A, red box), select all images and right-click to “Convert to Native Imaris File Format” ( A, red box).

Techniques:

Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM Tris (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.

Journal: The Journal of Biological Chemistry

Article Title: PhuS conformational dynamics are essential for DNA binding and heme-responsive control of the prrF operon in Pseudomonas aeruginosa

doi: 10.1016/j.jbc.2026.111314

Figure Lengend Snippet: Characterization of the heme binding properties of the PhuS R25 A variant . A , CD spectra of 10 μM apo-proteins ( left panel ) and holo-proteins ( right panel ) dialyzed in 1 mM potassium phosphate (pH 7.4). PhuS WT and PhuS R25 A spectra shown in blue and red, respectively. B , UV-Visible spectra of holo-WT and holo-R25 A protein in 20 mM Tris (pH 8.0) containing 150 mM NaCl. C , Tryptophan fluorescence quenching of WT PhuS and R25A PhuS. 1 μM of apo-WT PhuS or apo-R25 A PhuS was titrated with increasing concentrations (0 μM–12.8 μM) of heme. Samples were excited at 295 nm and emission was monitored at 337 nm. Relative binding was calculated by dividing the difference in fluorescence by the initial unbound fluorescence emission. The binding constant (K d ) was fit to a one-site binding model in Graphpad Prism by plotting relative binding as a function of heme concentration.

Article Snippet: 30 PM of oligonucleotides were added and incubated further at 37 ̊C for another 20 min. After the incubation, the protein-DNA binding reactions were run on a 10% Tris glycine polyacrylamide native gel (Bio-Rad).

Techniques: Binding Assay, Variant Assay, Circular Dichroism, Fluorescence, Concentration Assay