Figure 1.
Scatter plot for amino acid frequencies (A) and exchangeablilities (B) in SwissProt data set.
Error bars are standard deviations. Order promoting amino acids are green, disorder promoting ones yellow. Exchangeabilities between order and disorder promoting residues are gray.
Figure 2.
Amino acid exchangeability matrices and amino acid frequencies for ordered and disordered regions derived from the SwissProt data set: here, the area of each bubble represents the rate of a substitution or the amino acid frequency.
(A) Model estimates for IDRs. (B) Model estimates for ordered regions. (C) Relative difference () between the corresponding values for disordered and ordered models (plots A and B).
and
stand for the relative evolutionary rates in ordered and disordered regions, respectively. Order promoting amino acids are green, disorder promoting ones yellow. Exchangeabilities between order and disorder promoting residues are gray. Bubbles with red border correspond to negative values, i.e. have a lower frequency in IDRs.
Table 1.
Comparison of disorder prediction.
Table 2.
Comparison of evolutionary rates.
Table 3.
Overlaps between rate estimate classes.
Table 4.
Intrinsic disorder and tandem repeats.
Figure 3.
In murine SOCS3 the IDR (yellow) between the SH2 domain and the SOCS box is little conserved.
It presumably just has an effect in the degradation of the protein. This structure is available as PDB identifier 2BBU.
Figure 4.
In rat GNMP the N-terminal IDRs (yellow) are strongly conserved.
They give access to the active sites (red) in the presence of AdoHcy. This structure is available as PDB identifier 2IDJ.