Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins
| Autor: | Supriya Das, Nakul C. Maiti, Uttam Pal, Anupam Roy, Swagata Das, Khyati Bagga, Arpita Mrigwani |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Proteomics
Amyloid Microtubule-associated protein Science Molecular Sequence Data Protein aggregation Biology Bioinformatics Intrinsically disordered proteins DNA-binding protein Protein Structure Secondary Protein sequencing Protein structure Humans Amino Acid Sequence Theoretical Biology Peptide sequence Sequence (medicine) Multidisciplinary Computational Biology Intrinsically Disordered Proteins Biophysics Medicine Research Article Neuroscience |
| Zdroj: | PLoS ONE, Vol 9, Iss 3, p e89781 (2014) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins. More than 80% human proteins in the disordered protein databases (DisProt+IDEAL) contained one or more ARs. With decrease of protein disorder, AR content in the protein sequence was decreased. A probability density distribution analysis and discrete analysis of AR sequences showed that ∼8% residue in a protein sequence was in AR and the region was in average 8 residues long. The residues in the AR were high in sequence complexity and it seldom overlapped with low complexity regions (LCR), which was largely abundant in disorder proteins. The sequences in the AR showed mixed conformational adaptability towards α-helix, β-sheet/strand and coil conformations. |
| Databáze: | OpenAIRE |
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