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Study of conformational changes in proteins

A Malvern Instruments product story
Edited by the Manufacturingtalk editorial team Nov 14, 2006

Kouhei Shiba, from Sysmex will discuss the benefits of using the Malvern Zetasizer Nano to study conformational changes in proteins.

At the East Asian Biophysical Society meeting in Okinawa Kouhei Shiba, from Sysmex will discuss 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 rapidly and accurately measure particle size.

Its high sensitivity and precision temperature control are critical factors that allow thermally dependent structural changes to be detected at very 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 powerful easy-to-use protein characterisation tool.

Offering exceptional sensitivity and accuracy it allows protein molecules with a hydrodynamic radius down to 0.3 nm to be measured at concentrations of 0.1 mg/ml or less.

Incorporating a facility for absolute molecular weight measurement, user-friendly software and automated analysis protocols it is the ideal choice for protein laboratories.

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