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On the other hand, regions of long disorder do not appear to be robust under mutation.
At any significant error rate, long disorder disappeared in the native.
Our analysis clearly suggests two different answers for regular secondary structure and long disorder.
We analyzed many alternatives to choose the threshold for long disorder, and found most to be redundant.
IUPred has three options (long, short and glob); we chose short for short and long for long disorder.
Regions with long disorder behaved differently in that significantly fewer such regions were predicted after a few mutation steps.
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It has been estimated that two thirds of all signalling proteins have long disordered regions21, 22.
Long disordered binding regions (more than 30 residues) can also associate with globular partners.
As short and long disorders have different physical traits, we need length thresholds.
Proteins with disorder are highly abundant in nature, with ∼25 30% of eukaryotic proteins being mostly disordered, and with >50% of eukaryotic proteins and >70% of signaling proteins having long disordered regions.
According to computational predictions based on genomes, ∼30% of eukaryotic proteins are mostly disordered, and more than 50% eukaryotic proteins have long disordered regions consisting of more than 40 consecutive amino acid residues.
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