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Figure 2: (Figure 2A) HSA crystal structure showing the fatty acid-binding sites which have been resolved in the crystal structure. Figure 2B. Panel A: 9 resonances observed from 13C-OA binding to HSA (2 mM OA, 0.5 mM HSA) bound sites. Panels B, C, D show a decrease in NMR signal from binding pockets corresponding to peaks A, E, and F as the OA is displaced by increasing testosterone concentrations. Red resonances in panels B, C, and D are from sites that are occupied by OA in the presence of testosterone. Panel A shows the spectra obtained from 4:1 ratio of OA: HSA in absence of testosterone; Panel B: in presence of 0.5 molar equivalents of testosterone, Panel C: upon addition of 1 molar equivalent of testosterone; and Panel D: in presence of 2 molar equivalents of testosterone. Panel E shows the four spectra analyzed using CCPNMR software to determine the peak intensity at corresponding concentrations of testosterone. [ATTACH=full]11379[/ATTACH]
Figure 2: (Figure 2A) HSA crystal structure showing the fatty acid-binding sites which have been resolved in the crystal structure. Figure 2B. Panel A: 9 resonances observed from 13C-OA binding to HSA (2 mM OA, 0.5 mM HSA) bound sites. Panels B, C, D show a decrease in NMR signal from binding pockets corresponding to peaks A, E, and F as the OA is displaced by increasing testosterone concentrations. Red resonances in panels B, C, and D are from sites that are occupied by OA in the presence of testosterone. Panel A shows the spectra obtained from 4:1 ratio of OA: HSA in absence of testosterone; Panel B: in presence of 0.5 molar equivalents of testosterone, Panel C: upon addition of 1 molar equivalent of testosterone; and Panel D: in presence of 2 molar equivalents of testosterone. Panel E shows the four spectra analyzed using CCPNMR software to determine the peak intensity at corresponding concentrations of testosterone.
[ATTACH=full]11379[/ATTACH]
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