a<p>Mutations to the wild type <i>algD</i> binding site are notated by the bolded nucleotides in each mutant sequence.</p>b<p>The K<sub>d</sub> was calculated by fitting the hyperbolic equation for a single ligand binding model with saturation (eq 2) to the data in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1002648#ppat.1002648.s003" target="_blank">Figure S3</a>, which were averaged from four independent experiments.</p>c<p>Fold over (wild type) WT <i>algD</i> is defined by (K<sub>d</sub> of sample)/(K<sub>d</sub> of wild type) for each sample.</p
<p>(A), BRET shift between 80 ku of RXR-Luc and 40 ku of PPARG2-EYFP-WT or mutants PPARG2-EYFP-C142R...
<p>(A) Starting structure used for the FEP simulations, with explicit representation of residues sub...
<p>(A) Starting structure used for the FEP simulations with TM helices shown and colored according t...
<p>(A) Alignment of the <i>amrZ1</i> and <i>algD</i> DNA sequences that have been derived from previ...
<p>Binding affinities (<i>K</i><sub>d</sub>) of Ang II and R compounds to AT<sub>1</sub> wild-type (...
<p>The response time of mutant (a) homozygotes and (b) heterozygotes are shown. Different values of ...
<p><b>Bold</b> denotes measured affinity improvements, or specificity changes, greater than 3-fold.<...
<p>Binding affinities (<i>K</i><sub>d</sub>) of Ang II, olmesartan, R239470 and R794847 to AT<sub>1<...
<p>Binding affinities (<i>K</i><sub>d</sub>) of Ang II, olmesartan, R239470 and R794847 to AT<sub>1<...
<p>Binding affinities (K<sub>D</sub>) of the single mutants for MD2 were measured from the associati...
a<p>Dissociation constant (<i>K</i><sub>d</sub>) of binding of AraR and AraR mutants (Y5F, E30A) to ...
1<p>All experiments were repeated 3 times and average and standard deviation for K<sub>d</sub> is re...
<p>Fold change was determined for RNA binding by comparing each mutant K<sub>D</sub> value to wild-t...
<p>Distribution of binding site strength achieved in evolutionary simulations for haploids (gray) an...
<p>(A) Enzyme activity assay is performed in the presence and the absence of N-TIMP2 and the fractio...
<p>(A), BRET shift between 80 ku of RXR-Luc and 40 ku of PPARG2-EYFP-WT or mutants PPARG2-EYFP-C142R...
<p>(A) Starting structure used for the FEP simulations, with explicit representation of residues sub...
<p>(A) Starting structure used for the FEP simulations with TM helices shown and colored according t...
<p>(A) Alignment of the <i>amrZ1</i> and <i>algD</i> DNA sequences that have been derived from previ...
<p>Binding affinities (<i>K</i><sub>d</sub>) of Ang II and R compounds to AT<sub>1</sub> wild-type (...
<p>The response time of mutant (a) homozygotes and (b) heterozygotes are shown. Different values of ...
<p><b>Bold</b> denotes measured affinity improvements, or specificity changes, greater than 3-fold.<...
<p>Binding affinities (<i>K</i><sub>d</sub>) of Ang II, olmesartan, R239470 and R794847 to AT<sub>1<...
<p>Binding affinities (<i>K</i><sub>d</sub>) of Ang II, olmesartan, R239470 and R794847 to AT<sub>1<...
<p>Binding affinities (K<sub>D</sub>) of the single mutants for MD2 were measured from the associati...
a<p>Dissociation constant (<i>K</i><sub>d</sub>) of binding of AraR and AraR mutants (Y5F, E30A) to ...
1<p>All experiments were repeated 3 times and average and standard deviation for K<sub>d</sub> is re...
<p>Fold change was determined for RNA binding by comparing each mutant K<sub>D</sub> value to wild-t...
<p>Distribution of binding site strength achieved in evolutionary simulations for haploids (gray) an...
<p>(A) Enzyme activity assay is performed in the presence and the absence of N-TIMP2 and the fractio...
<p>(A), BRET shift between 80 ku of RXR-Luc and 40 ku of PPARG2-EYFP-WT or mutants PPARG2-EYFP-C142R...
<p>(A) Starting structure used for the FEP simulations, with explicit representation of residues sub...
<p>(A) Starting structure used for the FEP simulations with TM helices shown and colored according t...