<p>(<b>A</b>) Standard hydrophobicity of TF per residue <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0059683#pone.0059683-Monera1" target="_blank">[48]</a>, plotted as a coloured-barcode. The hydrophobicity scale varies from red – very hydrophilic (viz. ) – to green – very hydrophobic (viz. ). White-coloured residues are more likely to be hydrophobic than hydrophilic. (<b>B</b>) Standard hydrophobicity of TF residues, sequentially-averaged over groups of 5 residues. On the same hydrophobicity scale, hydrophobicity maps obtained from averaged (over 4 MD runs of 30 ns each) probability histograms of binding of hydrophobic probes to TF are also plotted, (<b>C</b>) in the extended conformation, (<b>D</b>) in the collaps...
<p>The plots show frequencies of hydrophobes on surface amino acids, both on protrusions (A, C, E, G...
Protein sequences may evolve to avoid highly hydrophobic local regions of sequence, in part because ...
Proteins tend to bury hydrophobic residues inside their core during the folding process to provide s...
<p>(<b>A</b>) Surface of Trigger factor colour-coded according to the red-white-green (RWG) hydropho...
<p>X-axis represents the sequence of this protein. Y-axis represents hydrophobicity density: theoret...
<p>Hydrophobicity plot based on Kyte & Doolittle's scale for the alignment of proteins F2/4JRU (blue...
<p>The largest significant correlation in each row is highlighted in bold.</p>a<p>Mean RSA of residu...
<p><b>A.</b> Contact probabilities of TF residues with MBP (top panel) and P2 (bottom panel). The ba...
<p><b>Notes:</b></p><p>1. Overall hydrophobicity is the algebraic sum of hydrophilicity (positive si...
<p><b>A.</b> Contact probabilities of TF residues with P1 in four TF-P1 Touching and Hugging Complex...
<p>The hydrophobicities of the residue 37 are, from left to right, Gly, Ala, Glu, Tyr and Trp <a hre...
<div><p>Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interact...
Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interacts with n...
<p>Individual amino acids on the X-axis are ordered according to the value of hydrophobicity in the ...
<p>Color indicates the protein family (black: PfEMP1, gray: RIFIN, light gray: STEVOR). Error bars g...
<p>The plots show frequencies of hydrophobes on surface amino acids, both on protrusions (A, C, E, G...
Protein sequences may evolve to avoid highly hydrophobic local regions of sequence, in part because ...
Proteins tend to bury hydrophobic residues inside their core during the folding process to provide s...
<p>(<b>A</b>) Surface of Trigger factor colour-coded according to the red-white-green (RWG) hydropho...
<p>X-axis represents the sequence of this protein. Y-axis represents hydrophobicity density: theoret...
<p>Hydrophobicity plot based on Kyte & Doolittle's scale for the alignment of proteins F2/4JRU (blue...
<p>The largest significant correlation in each row is highlighted in bold.</p>a<p>Mean RSA of residu...
<p><b>A.</b> Contact probabilities of TF residues with MBP (top panel) and P2 (bottom panel). The ba...
<p><b>Notes:</b></p><p>1. Overall hydrophobicity is the algebraic sum of hydrophilicity (positive si...
<p><b>A.</b> Contact probabilities of TF residues with P1 in four TF-P1 Touching and Hugging Complex...
<p>The hydrophobicities of the residue 37 are, from left to right, Gly, Ala, Glu, Tyr and Trp <a hre...
<div><p>Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interact...
Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interacts with n...
<p>Individual amino acids on the X-axis are ordered according to the value of hydrophobicity in the ...
<p>Color indicates the protein family (black: PfEMP1, gray: RIFIN, light gray: STEVOR). Error bars g...
<p>The plots show frequencies of hydrophobes on surface amino acids, both on protrusions (A, C, E, G...
Protein sequences may evolve to avoid highly hydrophobic local regions of sequence, in part because ...
Proteins tend to bury hydrophobic residues inside their core during the folding process to provide s...