Journal of Biosciences

, Volume 31, Issue 5, pp 551–556

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

Article

DOI: 10.1007/BF02708406

Cite this article as:
Dev, S. & Surolia, A. J Biosci (2006) 31: 551. doi:10.1007/BF02708406

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.

Keywords

Chaotropic denaturation DLS hydrodynamic radius PNA 

Copyright information

© Indian Academy of Sciences 2006

Authors and Affiliations

  1. 1.Molecular Biophysics UnitIndian Institute of ScienceBangaloreIndia

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