Using the Malvern Zetasizer Nano for Protein Conformation Studies
News Nov 14, 2006
At the East Asian Biophysical Society meeting in Okinawa (12-16 November 2006) Kouhei Shiba, from Sysmex discussed the benefits of using the Malvern Zetasizer Nano to study conformational changes in proteins.
The Zetasizer Nano uses the technique of dynamic light scattering (DLS) to measure particle size.
Its sensitivity and temperature control are critical factors that allow thermally dependent structural changes to be detected at low volumes/concentrations.
Protein structure correlates closely with function and is a parameter of significant interest. Using DLS, conformational changes are detected by measuring small differences in the hydrodynamic diameter of the molecule.
The technique is shown to have some advantages over differential scanning calorimetry for the study of structural change, and can also be used to measure the affinity of carbohydrate binding proteins, such as Lectin, with monosaccharides.
The Zetasizer Nano is a protein characterization tool. Offering sensitivity it is designed to allow protein molecules with a hydrodynamic radius down to 0.3 nm to be measured at concentrations of 0.1 mg/ml or less.