DisorderMat | R Documentation |
The Disorder40, Disorder60, and Disorder85 Matrices were
developed and described in
Brown et al. (2009).
In short: There are substitution scoring matrices used to align proteins
or regions which experience intrinsic disorder. The matrices were
calculated using pairwise sequence alignments of protein families
which here identified from 287 experimentally confirmed Intrinsically
Disordered Proteins (IDPs). The IDPs contained at least 30 sequential
residues of intrinsic disorder and protein families were found using
BLAST.
There was not a comprehensive comparison to other frequently
used substitution matrices (like BLOSUM and PAM) in terms of improving IDP
sequence alignments. The authors note that the purpose of these
matrices were made to compare evolutionary characteristics of disordered
and ordered proteins. Please see the source material for additional
information.
Trivedi and
Nagarajaram (2019) compared EDSSMat62 against all three Disordered
Matrices. Disorder40 and Disorder85 attain lower E-values for
highly disordered proteins, on average, when compared to EDSSMat62.
EDSSMat62 attained lower E-values when compared to Disorder60 for aligning
highly disordered proteins.
EDSSMat62 preforms better than all three Disorder matrices for IDPs
enriched in ordered regions. Please
see the referenced paper, specifically Supplementary Figures S18-20, for
additional information and original comparison.
Additionally, please cite the source article when using Disorder40,
Disorder60, or Disorder85.
Disorder40 Disorder60 Disorder85
All matrices are symmetric. 24 residues are represented:
Each of the standard 20 standard amino acids
Four ambiguous residues:
B: Asparagine or Aspartic Acid (Asx)
Z: Glutamine or Glutamic Acid (Glx)
X: Unspecified or unknown amino acid
*: Stop
An object of class matrix
(inherits from array
) with 24 rows and 24 columns.
An object of class matrix
(inherits from array
) with 24 rows and 24 columns.
An object of class matrix
(inherits from array
) with 24 rows and 24 columns.
As mentioned in the Description, the intended use of these matrices was not to improve sequence alignments. Therefore, no gap penalty values are provided.
It should also be noted that a more recent work, Trivedi and Nagarajaram (2019), determined optimal parameters based on the disordered content of query sequences, as reported in the paper's Supplementary Table S5.
Matrix Name | Gap Open (LD) | Gap Extension (LD) | Gap Open (MD) | Gap Extension (MD) | Gap Open (HD) | Gap Extension (HD) |
Disorder40 | -20 | -1 | -7 | -1 | -7 | -1 |
Disorder60 | -20 | -1 | -16 | -1 | -11 | -2 |
Disorder85 | -20 | -1 | -16 | -1 | -7 | -2 |
Please see the referenced paper for additional information and original
reporting. Additionally, please see EDSSMat
.
Trivedi, R., Nagarajaram, H.A. Amino acid substitution scoring matrices specific to intrinsically disordered regions in proteins. Sci Rep 9, 16380 (2019). https://doi.org/10.1038/s41598-019-52532-8
Brown, C. J., Johnson, A. K., & Daughdrill, G. W. (2009). Comparing Models of Evolution for Ordered and Disordered Proteins. Molecular Biology and Evolution, 27(3), 609-621. doi:10.1093/molbev/msp277
Disordered Matrices Vignette within the idpr package and EDSSMat62
Other IDP-based Substitution Matrices:
DUNMat
,
EDSSMat
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