<p>All the proteins detected in any kind of pairwise interactions in the IntAct database were taken into consideration. The percentage intrinsic disorder for each protein was calculated from disorder predicted by IUPred. The occurrence in each disorder range (with increments of 5% disorder) is given in % values, too, so that the area under each disorder curve amounts to 100. The median disorder values for the two sets of proteins are indicated in parentheses. (A) Bacteria (mostly <i>E. coli</i>). (B) Unicellular eukaryotes (mostly yeast). (C) Metazoa proteins.</p
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
<p>The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteo...
<p>The ratio of proteins which only bind chaperone to those which also bind non-chaperone partner(s)...
<p>The occurrence in each disorder range is given in % values, too, as in <a href="http://www.plosco...
<p>The ratio of chaperone-binding and non-chaperone-binding proteins was divided by the ratio of pro...
<p>Fractions of proteins with long regions of disorder (here ≥30 consecutive residues) were predicte...
<p>Left: percentages of disordered proteins (disordered proteins criterion: those proteins containin...
<p>Comparison of disorder contents (%) predicted by the IUPred method between proteins involved in t...
<div><p>Intrinsically disordered proteins and intrinsically disordered protein regions are highly ab...
Intrinsically disordered proteins and protein regions lack a stable three-dimensional structure unde...
Intrinsically disordered proteins and protein regions lack a stable three-dimensional structure unde...
<p>The two box plots compare the ratios of disordered residues across major taxonomic groups. The Pf...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
Intrinsically disordered proteins and protein regions lack a stable three-dimensional structure unde...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
<p>The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteo...
<p>The ratio of proteins which only bind chaperone to those which also bind non-chaperone partner(s)...
<p>The occurrence in each disorder range is given in % values, too, as in <a href="http://www.plosco...
<p>The ratio of chaperone-binding and non-chaperone-binding proteins was divided by the ratio of pro...
<p>Fractions of proteins with long regions of disorder (here ≥30 consecutive residues) were predicte...
<p>Left: percentages of disordered proteins (disordered proteins criterion: those proteins containin...
<p>Comparison of disorder contents (%) predicted by the IUPred method between proteins involved in t...
<div><p>Intrinsically disordered proteins and intrinsically disordered protein regions are highly ab...
Intrinsically disordered proteins and protein regions lack a stable three-dimensional structure unde...
Intrinsically disordered proteins and protein regions lack a stable three-dimensional structure unde...
<p>The two box plots compare the ratios of disordered residues across major taxonomic groups. The Pf...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
Intrinsically disordered proteins and protein regions lack a stable three-dimensional structure unde...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
An automatic method for recognizing natively disordered regions from amino acid sequence is describe...
<p>The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteo...