Record Details

Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins

EPrints@IICB

View Archive Info
 
 
Field Value
 
Title Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins
 
Creator Das, Swagata
Pal, Uttam
Das, Supriya
Bagga, Khyati
Roy, Anupam
Mrigwani, Arpita
Maiti, Nakul Chandra
 
Subject Structural Biology & Bioinformatics
 
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.
 
Date 2014
 
Type Article
PeerReviewed
 
Format application/pdf
 
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.
 
Relation http://dx.doi.org/10.1371/journal.pone.0089781
http://www.eprints.iicb.res.in/2053/