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      https://www.ias.ac.in/article/fulltext/jcsc/129/08/1267-1276

    • Keywords

       

      Concanavalin A; jelly roll motif; sodium dodecyl sulphate; guanidine hydrochloride; molten globule conformation

    • Abstract

       

      Concanavalin A (ConA) is a plant lectin having industrial and biological applications. Concanavalin A changes conformation upon exposure to different stress conditions, like exposure to sodium dodecyl sulphate, guanidine hydrochloride, varying hydronium ion potential, etc. The conformational changes were studied using circular dichroism spectroscopy and the structural rigidity of ConA was explored using fluorescence spectroscopy, taking tryptophan as an intrinsic and 8-anilino-1-naphthalenesulfonic acid as an extrinsic fluorescence probes, in different stress conditions. ConA loses the quaternary structure in all the studied stress conditions, which further leads to denaturation of the protein. However, the mechanism of denaturation varied with the studied conditions, like different SDS concentrations and hydronium ion potentials, wherein the proteinundergoes a conformational rearrangement from β-sheet to α-helix. Moreover, GdnHCl triggered complete denaturation of ConA into a predominantly random coil conformation. The results suggested that denaturation of ConA follows different pathways depending on the chemical properties and concentrations of the denaturants used.

    • Author Affiliations

       

      SHREYASI ASTHANA1 SUJIT KUMAR BHUTIA1 HAREKRUSHNA SAHOO2 SUMAN JHA1

      1. Department of Life Science, National Institute of Technology Rourkela, Odisha 769 008, India
      2. Department of Chemistry, National Institute of Technology Rourkela, Odisha 769 008, India
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