title: Dynamic light scattering study of peanut agglutinin: size, shape and urea denaturation.
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 (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.
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
authors.forename: Sagarika
authors.initials: S
authors.lastname: Dev
authors.forename: Avadhesha
authors.initials: A
authors.lastname: Surolia
mesh_terms: D008027:Light; D008958:Models, Molecular; D019887:Peanut Agglutinin / Q000737:chemistry*; D011489:Protein Denaturation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D014508:Urea / Q000737:chemistry
chemical_list: D019887:Peanut Agglutinin; D014508:Urea