Journal: Protein Science : A Publication of the Protein Society

Article Title: Lipopolysaccharide binding to the periplasmic protein L pt A

doi: 10.1002/pro.3177

Figure Lengend Snippet: Overlays of X‐band CW EPR spectra of spin‐labeled apo LptA at the positions indicated at 2 µM (black) and 100 µM (green) protein concentration. Spectra are normalized to the same center line height and are 100 G wide.

Article Snippet: Surprisingly, the K d values for the N‐terminal edge sites studied are consistently weaker, with L45R1 data showing a K d value >200 μM due to a linear data set unable to be fit by a saturable binding curve and T32R1 and I36R1 data resulting in K d values of 119 μM and 137 μM, respectively. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 4 caption a7 Plots of the data points generated from the deconvolution of the EPR spectra containing varying amounts of LPS and the resulting fits using a single‐site ligand binding model in SigmaPlot (Systat Software, San Jose, CA).

Techniques: Labeling, Protein Concentration

Journal: Protein Science : A Publication of the Protein Society

Article Title: Lipopolysaccharide binding to the periplasmic protein L pt A

doi: 10.1002/pro.3177

Figure Lengend Snippet: Overlays of X‐band CW EPR spectra of 2 µM LptA in the absence (black) and presence (blue) of 198 µM LPS. Spectra are normalized to the same center line height and are 100 G wide.

Article Snippet: Surprisingly, the K d values for the N‐terminal edge sites studied are consistently weaker, with L45R1 data showing a K d value >200 μM due to a linear data set unable to be fit by a saturable binding curve and T32R1 and I36R1 data resulting in K d values of 119 μM and 137 μM, respectively. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 4 caption a7 Plots of the data points generated from the deconvolution of the EPR spectra containing varying amounts of LPS and the resulting fits using a single‐site ligand binding model in SigmaPlot (Systat Software, San Jose, CA).

Techniques:

Journal: Protein Science : A Publication of the Protein Society

Article Title: Lipopolysaccharide binding to the periplasmic protein L pt A

doi: 10.1002/pro.3177

Figure Lengend Snippet: Plots of the data points generated from the deconvolution of the EPR spectra containing varying amounts of LPS and the resulting fits using a single‐site ligand binding model in SigmaPlot (Systat Software, San Jose, CA). Data are plotted for (A) Center and C‐terminal and (B) N‐terminal LptA sites in the WT (solid circles) and Q148A/K149A LptA (open circles) backgrounds. K d values are indicated and listed in Table 1 with standard errors and B max values; L45R1 data do not yield finite values. Protein structures highlight in black the locations of the LptA sites studied for each panel.

Article Snippet: Surprisingly, the K d values for the N‐terminal edge sites studied are consistently weaker, with L45R1 data showing a K d value >200 μM due to a linear data set unable to be fit by a saturable binding curve and T32R1 and I36R1 data resulting in K d values of 119 μM and 137 μM, respectively. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window Figure 4 caption a7 Plots of the data points generated from the deconvolution of the EPR spectra containing varying amounts of LPS and the resulting fits using a single‐site ligand binding model in SigmaPlot (Systat Software, San Jose, CA).

Techniques: Generated, Ligand Binding Assay, Software