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...

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Autores principales:	Swagata Das, Uttam Pal, Supriya Das, Khyati Bagga, Anupam Roy, Arpita Mrigwani, Nakul C Maiti
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c19c22ef9cf44656a643ca17c93af8ae
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spelling	oai:doaj.org-article:c19c22ef9cf44656a643ca17c93af8ae2021-11-18T08:30:07ZSequence complexity of amyloidogenic regions in intrinsically disordered human proteins.1932-620310.1371/journal.pone.0089781https://doaj.org/article/c19c22ef9cf44656a643ca17c93af8ae2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24594841/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203An 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.Swagata DasUttam PalSupriya DasKhyati BaggaAnupam RoyArpita MrigwaniNakul C MaitiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 3, p e89781 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q 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.
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.
format	article
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
title	Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.
title_short	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_sort	sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/c19c22ef9cf44656a643ca17c93af8ae
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Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.

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