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    • Dynamic light scattering study of peanut agglutinin: Size, shape and urea denaturation

      Sagarika Dev Avadhesha Surolia

      Volume 31 Issue 5 December 2006 pp 551-556

    • Fulltext

       

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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/031/05/0551-0556

    • Keywords

       

      Chaotropic denaturation; DLS; hydrodynamic radius; PNA

    • Abstract

       

      Peanut agglutinin (PNA) is a homotetrameric protein with a unique open quaternary structure. PNA shows non-two state profile in chaotrope induced denaturation. It passes through a monomeric molten globule like state before complete denaturation (Reddyet al 1999). This denaturation profile is associated with the change in hydrodynamic radius of the native protein. Though the molten globule-like state is monomeric in nature it expands in size due to partial denaturation. The size and shape of the native PNA as well as the change in hydrodynamic radius of the protein during denaturation has been studied by dynamic light scattering (DLS). The generation of two species is evident from the profile of hydrodynamic radii. This study also reveals the extent of compactness of the intermediate state.

    • Author Affiliations

       

      Sagarika Dev1 Avadhesha Surolia1

      1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore - 560 012, India

    • Dates

       
      Published
      December 2006
      Manuscript received
      6 June 2006
      Accepted
      26 September 2006

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