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Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program <t>ImageQuant</t> from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.
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Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program ImageQuant from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.

Journal:

Article Title: Topology of RbsC, the Membrane Component of the Escherichia coli Ribose Transporter †

doi: 10.1128/JB.185.17.5234-5239.2003

Figure Lengend Snippet: Fluorescence intensities of the N157C, E19C, and V309C proteins on the SDS-PAGE gel described in the legend to Fig. ​Fig.2.2. Intensity traces of the N157C and E19C protein lanes of the gel in Fig. ​Fig.22 were created with the gel analysis program ImageQuant from Molecular Dynamics. Fluorescence intensity is plotted versus distance from an arbitrary point near the leading edge of the gel; thus, bands on the gel moved from right to left. RbsC is at about 340 pixels.

Article Snippet: Intensity traces of the N157C and E19C protein lanes of the gel in Fig. were created with the gel analysis program ImageQuant from Molecular Dynamics.

Techniques: Fluorescence, SDS Page