A consensus approach for intrinsic disorder analysis for heat shock protein family

Abstract

Intrinsic Disorder (ID) regions arc implicated with various regulations, but, structure of few ID proteins is experimentally determined and huge amounts of such proteins are still unknown. Computational methods are novel ways to determine such ID regions rapidly and efficiently. There are some popular methods remain to predict that, although, their output varies. Present study attempted to take aggregated efforts to solve the problem. With that regard, we identified and analyzed the ID parts by a consensus approach for Heat Shock Protein (HSP) family and to interpret their significant functional relations. Heat shock proteins are also called tenseness proteins, are a group of protein, are present in all cells in all life lines. This family is very important for cellular function and regulations. Our approach is relevant with several others computational and experimental results. Results are considered only when ≥60% accuracy maintained with a common state parameters. From HSP analysis, we headed to conclude that ID prediction for HSP are more univocal and thus their functional implications what we interpreted deserve for good sense. ID possesses more Serine/Thiamine sites and functional domains which are related with disorders and phosphorylations. © 2009 Asian Network for Scientific Information.