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Sequence complexity of disordered protein
TLDR
The Swiss Protein database of sequences exhibits significantly higher amounts of both low‐complexity and predicted‐to‐be‐disordered segments as compared to a non‐redundant set of sequences from the Protein Data Bank, providing additional data that nature is richer in disordered and low-complexity segments compared to the commonness of these features in the set of structurally characterized proteins.
Intrinsically disordered protein.
TLDR
The sequence-structure relationships indicate that disorder is an encoded property, and the predictions strongly suggest that proteins in nature are much richer in intrinsic disorder than are those in the Protein Data Bank.
The importance of intrinsic disorder for protein phosphorylation.
TLDR
A new web-based tool for the prediction of protein phosphorylation sites, DISPHOS (DISorder-enhanced PHOSphorylation predictor, http://www.ist. edu/DISPHOS), which observes that amino acid compositions, sequence complexity, hydrophobicity, charge and other sequence attributes of regions adjacent to phosphate sites are very similar to those of intrinsically disordered protein regions.
Length-dependent prediction of protein intrinsic disorder
TLDR
The VSL2 predictors are applicable to disordered regions of any length and can accurately identify the short dis ordered regions that are often misclassified by the previous disorder predictors.
DisProt: the Database of Disordered Proteins
TLDR
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs) by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs.
Optimizing Long Intrinsic Disorder Predictors with Protein Evolutionary Information
TLDR
This work focuses on improving sequence-based predictions of long (>30 amino acid residues) regions lacking specific 3-D structure by means of four new neural-network-based Predictors Of Natural Disordered Regions (PONDRs): VL3, VL 3H, V l3P, and Vl3E.
Intrinsic disorder in cell-signaling and cancer-associated proteins.
TLDR
The data suggest that intrinsically unstructured proteins play key roles in cell-signaling, regulation and cancer, where coupled folding and binding is a common mechanism.
Exploiting heterogeneous sequence properties improves prediction of protein disorder
TLDR
A two‐level model called VSL1, which consists of two specialized predictors, one of which was optimized for long disordered regions (>30 residues) and the other for short dis ordered regions (≤30 residues), and has achieved the highest accuracy yet and significantly improved performance on shortdisordered regions.
Intrinsic protein disorder in complete genomes.
TLDR
Overall, intrinsic disorder appears to be a common, with eucaryotes perhaps having a higher percentage of native disorder than archaea or bacteria, and bacteria and archaea in various archaea ranged from 2 to 11%, plus an apparently anomalous 18% in bacteria.
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