of Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors

of Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factor

Additional file 1: Table S1. of Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors

RNA-binding proteins in 19 E. coli proteomes. All the RBPs obtained in the GWS of 19 E. coli strains have been listed in this table. The pathogenic and non-pathogenic E. coli strains have been highlighted in red and green, respectively. (DOC 115 kb

RMSF of each sector of hand-like structure of TdT <i>viz</i>. thumb, finger, index finger and loop1 (Increased RMSF values are marked in bold).

Loop1 RMSF values reduce in TdT-long (wild and mutant). Simulations performed at 311 K for 100 ns except for the mutated TdT-long form.</p

Deviations within different subdomains (except within Loop1) observed in TdT-short and long isoform.

<p>RMSD of subdomains of TdT-short and TdT-long for simulations runs at 311 K for 100 ns. Index: TdT-short (run1: black, run2: red), TdT-long form (run1: green, run2: blue).</p

Average difference in binding energies (kcal/mol) of odorants to 10 human-mouse OR pairs.

<p>The average binding energies of 125 odorants to each of the ORs were calculated and the difference in the average energy between each human-mouse OR pair has been reported. The OR pair 2 (with the highest sequence identity of 84%) has the minimum difference in binding energy.</p

The distribution of odorants (125) into different chemical classes.

<p>The odorants belonged to different chemical classes with varying length of carbon chains. Few specific odorants that induce responses from insect ORs and mammalian ORs were grouped separately to understand their receptor binding activity.</p

The binding mode of eugenol to mOR-EG.

<p>The figure shows the binding site of eugenol to mOR-EG. Phe 182 residue forms a H-bond with the—OH group. Other interacting residues are Tyr 260 and Asn 264, while other residues contribute to the hydrophobic pocket required for odorant binding. The figure is obtained using the “Ligand Interaction Diagram” of the GLIDE software (<b>Schrödinger Release 2013–1</b>:, version 2.6, Schrödinger, LLC, New York, NY, 2013).</p

Supplementary_Material – Supplemental material for Genome-Wide Search for Tyrosine Phosphatases in the Human Genome Through Computational Approaches Leads to the Discovery of Few New Domain Architectures

Supplemental material, Supplementary_Material for Genome-Wide Search for Tyrosine Phosphatases in the Human Genome Through Computational Approaches Leads to the Discovery of Few New Domain Architectures by Teerna Bhattacharyya and Ramanathan Sowdhamini in Evolutionary Bioinformatics</p

Best binding mode of Helional to OR.

<p>This interaction has the highest score in the IFD runs. There are three H-bonds and one salt bridge interaction between the odorant and the residues of the olfactory receptor. The figure is obtained using the “Ligand Interaction Diagram” of the GLIDE software (<b>Schrödinger Release 2013–1</b>:, version 2.6, Schrödinger, LLC, New York, NY, 2013).</p

of Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factors

of Bioinformatics comparisons of RNA-binding proteins of pathogenic and non-pathogenic Escherichia coli strains reveal novel virulence factor