Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
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| Title |
Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins
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| Creator |
Das, Swagata
Pal, Uttam Das, Supriya Bagga, Khyati Roy, Anupam Mrigwani, Arpita Maiti, Nakul Chandra |
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| Subject |
Structural Biology & Bioinformatics
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| 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 a-helix, b-sheet/strand and coil conformations.
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| Date |
2014
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/2053/1/PLOS_ONE__Volume_9__(_3)___Article_Number_e89781;2014[49].pdf
Das, Swagata and Pal, Uttam and Das, Supriya and Bagga, Khyati and Roy, Anupam and Mrigwani, Arpita and Maiti, Nakul Chandra (2014) Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins. PLOS ONE, 9 (3). e89781. |
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| Relation |
http://dx.doi.org/10.1371/journal.pone.0089781
http://www.eprints.iicb.res.in/2053/ |
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