Local propensity of the central hydrophobic residue of the BB sub-networks affecting the 2D-structure prediction.

<p>Local propensity of the central hydrophobic residue of the BB sub-networks affecting the 2D-structure prediction.</p

Protein oligomers containing a β-interface.

<p><b>A.</b> The 1Q3S octameric bacterial chaperone <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0032558#pone.0032558-Shomura1" target="_blank">[67]</a> and <b>B.</b> The 1PVN tetrameric protozoa oxidoreductase <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0032558#pone.0032558-Gan1" target="_blank">[68]</a>. Both structures are represented using RasMol. The chains are colored in light grey and the secondary-structures are represented by helices and strands. The β-strands of the interfaces are colored in black and dark grey in ribbons.</p

x-ray structures of the protein oligomers of the dataset.

<p>The respective PDB codes are indicated above the structures. The figure was made using RasMol. Each chain is shown in a different color.</p

Anti-parallel BB sub-network and intramolecular hydrogen bond network.

<p><b>A.</b> Gemini graph of an anti-parallel intermolecular β-interface <b>B.</b> Schematics of the hydrogen bond network of anti-parallel intramolecular β-sheet. <b>C.</b> Ladder pattern observed in BB sub-network and also visible in anti-parallel intramolecular β-sheet.</p

Schematic of the charge distribution in β-interactions.

<p>The amino acids are indicated using the single letter code.</p

Histogram of the whole chain lengths.

<p>The length of the whole chain (range) is indicated on the x axis as the total number of amino acids.</p

Chemical composition of the interactions (amino acid -i- of segment 1 with amino acid -j- of segment 2 or vice-versa, data are added together) in the SC and in the BB (bracket) networks of the β-interfaces.

<p>Chemical composition of the interactions (amino acid -i- of segment 1 with amino acid -j- of segment 2 or vice-versa, data are added together) in the SC and in the BB (bracket) networks of the β-interfaces.</p

Statistics on the lengths of the dataset.

a<p>SD stands for standard deviation.</p>b<p>Q stands for quartile. The statistics are defined in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0032558#s2" target="_blank">materials and methods</a>.</p

Absence of correlation between the lengths of the whole chains and of the β-interfaces.

<p>The length of the β-interface (sum of the amino acids of the two segments) of each protein of the dataset is plotted against the length of its respective whole chain (•, ‘all amino acids’ and ◊, ‘X’, respectively). If there was a correlation between the size of the whole chain and the size of its interface or the size of its hot spot numbers, the points would appear on the dashed line.</p

Central hydrophobic residues and percentage of BB interactions.

<p>The number of hydrophobic amino acids of the BB (β) or of the SC sub-networks (•) located centrally in the full networks are plotted against the percentage of BB interactions.</p