Dev, Sagarika and Surolia, Avadhesha (2006) Dynamic light scattering study of peanut agglutinin: Size, shape and urea denaturation. In: Journal of Biosciences, 31 (5). pp. 551-556.
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 (Reddy et 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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Indian Academy of Sciences.|
|Keywords:||Chaotriopic Denaturation;DLS;Hydrodynamic Radius;PNA|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||25 Aug 2008|
|Last Modified:||19 Sep 2010 04:34|
Actions (login required)