Sequence complexity of disordered protein
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Summary
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.
- Type
- article
- Published
- 2001-01-01
- Cited by
- 1,711
- References
- 84
- Access
- Open access
- OpenAlex
- https://openalex.org/W2049476357
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1842005
Keywords
Intrinsically disordered proteins, Sequence (biology), Amino acid, Protein Data Bank, Peptide sequence
References
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- Dominant and recessive deafness caused by mutations of a novel gene, TMC1, required for cochlear hair-cell function
- Structure-Related Statistical Singularities along Protein Sequences: A Correlation Study
- Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae.
- Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase.
- Calcium-dependent Conformational Flexibility of a CUB Domain Controls Activation of the Complement Serine Protease C1r*
- Intrinsic disorder and coiled coil formation in prostate apoptosis response factor-4 (Par-4) : submitted in fulfilment of the requirements of the degree of Doctor of Philosphy, Institute of Fundamental Sciences, Massey University, New Zealand
- The NMR structure of FliK, the trigger for the switch of substrate specificity in the flagellar type III secretion apparatus.
- NMR spectroscopy to study the dynamics and interactions of CFTR.
- Conformational propensities and residual structures in unfolded peptides and proteins.
- Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector
- N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case.
- Intrinsic disorder mediates hepatitis C virus core–host cell protein interactions
- Intrinsic disorder and metal binding in UreG proteins from Archae hyperthermophiles: GTPase enzymes involved in the activation of Ni(II) dependent urease
- Multivalent IDP Assemblies: Unique properties of LC8-associated, IDP duplex scaffolds
- Evidence for the residual tertiary structure in the urea-unfolded form of bacteriophage T5 endolysin
- RGG/RG Motif Regions in RNA Binding and Phase Separation.
- Global analysis of methionine oxidation provides a census of folding stabilities for the human proteome
- Structural and biochemical studies of Sporosarcina pasteurii UreE: a nickel-chaperone involved in the urease activation process
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