Uttam Pal - Sequence Complexity of Amyloidogenic Regions in Intrinsically Disordered Human Proteins

Document created by Uttam Pal on Dec 25, 2015
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  Publication Details (including relevant citation   information):

  Das, Swagata, Pal, Uttam, Das, Supriya, Bagga, Khyati, Roy,   Anupam, Mrigwani, Arpita, Maiti, Nakul C. 9 (3) e89781-

  Abstract: 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.

  Address (URL): http://dx.doi.org/10.1371/journal.pone.0089781