Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.
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 (D...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24594841/pdf/?tool=EBI |
| _version_ | 1818574056254865408 |
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| author | Swagata Das Uttam Pal Supriya Das Khyati Bagga Anupam Roy Arpita Mrigwani Nakul C Maiti |
| author_facet | Swagata Das Uttam Pal Supriya Das Khyati Bagga Anupam Roy Arpita Mrigwani Nakul C Maiti |
| author_sort | Swagata Das |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-15T00:21:21Z |
| format | Article |
| id | doaj.art-c19c22ef9cf44656a643ca17c93af8ae |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-15T00:21:21Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-c19c22ef9cf44656a643ca17c93af8ae2022-12-21T22:42:18ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0193e8978110.1371/journal.pone.0089781Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.Swagata DasUttam PalSupriya DasKhyati BaggaAnupam RoyArpita MrigwaniNakul C MaitiAn 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.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24594841/pdf/?tool=EBI |
| spellingShingle | Swagata Das Uttam Pal Supriya Das Khyati Bagga Anupam Roy Arpita Mrigwani Nakul C Maiti Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. PLoS ONE |
| title | Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. |
| title_full | Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. |
| title_fullStr | Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. |
| title_full_unstemmed | Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. |
| title_short | Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. |
| title_sort | sequence complexity of amyloidogenic regions in intrinsically disordered human proteins |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24594841/pdf/?tool=EBI |
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