MOESM1 of Plasmodium malariae in the Colombian Amazon region: you don’t diagnose what you don’t suspect

Additional file 1: Table S1. Primer sequences and amplicon sizes of the Plasmodium spp. identified and the β-globin gene

MOESM2 of Plasmodium malariae in the Colombian Amazon region: you don’t diagnose what you don’t suspect

Additional file 2: Table S2. Comparing TBS and PCR diagnosis regarding the type of infection. Frequencies according to the amount of species detected per sample by PCR assay compared to TBS test

The probability of the risk of the women in this cohort acquiring <i>C</i>. <i>trachomatis</i> infection as time elapsed.

<p>The probability of the risk of the women in this cohort acquiring <i>C</i>. <i>trachomatis</i> infection as time elapsed.</p

The time taken to clear <i>Chlamydia trachomatis</i> infection in the cohort of females initially infected by HPV and <i>C</i>. <i>trachomatis</i>.

<p>The time taken to clear <i>Chlamydia trachomatis</i> infection in the cohort of females initially infected by HPV and <i>C</i>. <i>trachomatis</i>.</p

Internal backbone dynamics of PCNA in solution measured by ¹⁵N relaxation.

<p>The order parameter S² for backbone HN bonds are plotted for those residues whose ¹⁵N T₁, T₂, and ¹⁵N{¹H} NOE values could be measured and analyzed. The location of the secondary structure elements along the PCNA sequence is indicated by red and blue boxes for α-helices and β-strands, respectively. The last five residues at the C-terminal end are not seen in the crystal structure and therefore an order parameter was not calculated, but these residues have the smallest heteronuclear NOEs and the largest T₂ times, indicating that they are the most flexible residues in the protein (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048390#pone.0048390.s001" target="_blank">Figure S1</a>). The regions of the graph corresponding to the IDCL (residues 117–134), the βD2−βE2 loop (184–195), and the C-terminus (252–261) are shaded in yellow. Inset: Representation of the PCNA backbone structure as a coil whose thickness is proportional to the order parameter S² of the backbone NH bond of the corresponding residue. For simplicity only one of the protomers is shown, but the data correspond to measurements done on the homotrimer. For the residues whose order parameter could not be calculated the thickness was interpolated based on the solid line joining the available values plotted in the graph. Helices and strands are colored in red and blue, and the three most flexible regions are colored in yellow (as in the graph). The loops with high relative disorder are labeled using the same nomenclature as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0048390#pone-0048390-g001" target="_blank">Figure 1</a>.</p

Chemical shift perturbations of PCNA backbone amide resonances caused by PIP-box peptides.

<p>The top and middle panels show the CSP values for each PCNA residue in the presence of a 1.2 or 1.6 excess (on a monomer basis) of p21²⁰ or p21¹² peptides, respectively. Under the experimental conditions used PCNA is saturated with the peptides (we calculate that 99.9 and 99.8% of the PCNA molecules are bound to the p21²⁰ or the p21¹² peptide, respectively). The bottom panel represents the CSP values in the presence of a 7.8 excess of the ING1²² peptide. The inset shows the CSP experienced by PCNA residue H44 at increasing concentrations of the peptide with error bars spanning twice the estimated uncertainty in the CSP values (±0.005 ppm), which is the average CSP value. The line is the best fit to a model of one set of identical binding sites.</p