Protein characterisation is a broad term which involves creating a profile or fingerprint of the protein molecule’s physical, chemical, and biological properties. It has been transformed by modern analytical technologies such as Dual Polarisation Interferometry for the determination of protein structure and function. Other useful spectroscopic techniques include UV/Visible and FTIR spectroscopy and Circular Dichroism to show folding of the protein. However, not all techniques are applicable to all proteins. Membrane proteins are difficult to crystallise, so their three dimensional structures cannot readily be determined.
Click here to contact usUnderstanding the state of a protein in solution and how it behaves under various conditions. is also important. Under certain solution conditions, proteins tend to aggregate or even precipitate. Dynamic light scattering (DLS) is a rapid technique for sizing aggregation. Sizing with DLS reveals the oligomeric state and homogeneity of a protein (monomer, dimer, oligomer, or a mixture), which can be important for the safe administration of protein drugs.
Detecting aggregation using DLS is useful for determining optimal crystallisation conditions for x-ray crystallography studies of protein structure. Protein molecular size and weight can be accurately measured by combining a light scattering detector with Gel Permeation Chromatography. Another property that can be measured with light-scattering is zeta potential, which is related to the charge on the molecule and is relevant to developing a stable protein drug formulation.
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