<p>Left: percentages of disordered proteins (disordered proteins criterion: those proteins containing at least 50% disordered residues based on Disopred predictions). Right: average percentages of disordered residues involved in binding (DBRs), as predicted by ANCHOR. The stars denote significant differences evaluated with the same Chi-square tests described in the Methods section and illustrated in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0055524#pone-0055524-g001" target="_blank">Figure 1</a> but using all proteins (i.e. not restricted to a particular GO functional class).</p
Disordered regions are sequences within proteins that fail to fold into a xed tertiary structure and...
Recent proteome-wide screening approaches have provided a wealth of information about interacting pr...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
<p>Results shown for Disopred (disorder prediction) and ANCHOR (Disorder binding regions, DBRs). For...
<p>For each organism (Arabidopsis (green) and human (blue)) protein sequences and their correspondin...
<p>We represent the protein disorder content for the organisms in similar habitats (left panel) and ...
<p>Disordered proteins here are again those with 1 or more LDWs based on Disopred predictions. Same ...
<p>Fractions of proteins with long regions of disorder (here ≥30 consecutive residues) were predicte...
<p>All the proteins detected in any kind of pairwise interactions in the IntAct database were taken ...
The precise prediction of protein intrinsically disordered regions, which play a crucial role in bio...
Abstract: The role and function of a given protein is dependent on its structure. In recent years, h...
The role and function of a given protein is dependent on its structure. In recent years, however, n...
<p>Disorder prediction values for the given residues are plotted against the amino acid residue numb...
Abstract: Intrinsically disordered proteins, defying the traditional protein structure–function para...
Copyright © 2013 Tong-Hui Zhao et al.This is an open access article distributed under the Creative C...
Disordered regions are sequences within proteins that fail to fold into a xed tertiary structure and...
Recent proteome-wide screening approaches have provided a wealth of information about interacting pr...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
<p>Results shown for Disopred (disorder prediction) and ANCHOR (Disorder binding regions, DBRs). For...
<p>For each organism (Arabidopsis (green) and human (blue)) protein sequences and their correspondin...
<p>We represent the protein disorder content for the organisms in similar habitats (left panel) and ...
<p>Disordered proteins here are again those with 1 or more LDWs based on Disopred predictions. Same ...
<p>Fractions of proteins with long regions of disorder (here ≥30 consecutive residues) were predicte...
<p>All the proteins detected in any kind of pairwise interactions in the IntAct database were taken ...
The precise prediction of protein intrinsically disordered regions, which play a crucial role in bio...
Abstract: The role and function of a given protein is dependent on its structure. In recent years, h...
The role and function of a given protein is dependent on its structure. In recent years, however, n...
<p>Disorder prediction values for the given residues are plotted against the amino acid residue numb...
Abstract: Intrinsically disordered proteins, defying the traditional protein structure–function para...
Copyright © 2013 Tong-Hui Zhao et al.This is an open access article distributed under the Creative C...
Disordered regions are sequences within proteins that fail to fold into a xed tertiary structure and...
Recent proteome-wide screening approaches have provided a wealth of information about interacting pr...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...