• Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins

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      https://www.ias.ac.in/article/fulltext/jbsc/045/0029

    • Keywords

       

      Aggregation; chaperone; intrinsically disordered proteins; protein–protein interactions; phase separation

    • Abstract

       

      Intrinsically disordered proteins (IDPs) are highly flexible and undergo disorder to order transition uponbinding. They are highly abundant in human proteomes and play critical roles in cell signaling and regulatoryprocesses. This review mainly focuses on the dynamics of disordered proteins including their conformationalheterogeneity, protein–protein interactions, and the phase transition of biomolecular condensates that arecentral to various biological functions. Besides, the role of RNA-mediated chaperones in protein folding andstability of IDPs were also discussed. Finally, we explored the dynamic binding interface of IDPs as noveltherapeutic targets and the effect of small molecules on their interactions.

    • Author Affiliations

       

      ANIL BHATTARAI1 ISAAC ARNOLD EMERSON1

      1. Bioinformatics Programming Laboratory, Department of Biotechnology, School of Biosciences and Technology, Vellore Institute of Technology, Vellore 632 014, India
    • Dates

       
  • Journal of Biosciences | News

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      Posted on July 25, 2019

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