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Sequence complexity of disordered protein
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.
The importance of intrinsic disorder for protein phosphorylation.
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
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.
PONDR-FIT: a meta-predictor of intrinsically disordered amino acids.
DisProt: the Database of Disordered Proteins
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
- Kang Peng, S. Vucetic, P. Radivojac, C. Brown, A. Dunker, Z. Obradovic
- BiologyJ. Bioinform. Comput. Biol.
- 1 February 2005
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.
Classification of Intrinsically Disordered Regions and Proteins
Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes and is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood.
Exploiting heterogeneous sequence properties improves prediction of protein disorder
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.