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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.
Highlights
The available genome sequences and several computational methods have revealed a unique presence of some proteins which remain disordered under physiological condition and resemble their own functional states [1,2,3,4,5,6,7,8,9]
Further we have found that the sequences in amyloidogenic region (AR) are highly complex and they rarely overlap with low complexity regions (LCR)
The current investigation was focused on sequence complexity and content of AR present in proteins which were partially or fully disordered
Summary
The available genome sequences and several computational methods have revealed a unique presence of some proteins which remain disordered under physiological condition and resemble their own functional states [1,2,3,4,5,6,7,8,9]. These proteins are known by different names like intrinsically disordered [10], natively denatured [11], natively unfolded protein and intrinsically unstructured proteins [3], [10]. The functional domain varies from DNA binding to cell cycle regulation, membrane transport, different molecular recognition processes, and other important cellular functions [19], [21,22,23]
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