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Malvern's TDAmax Enables Protein Scientists Determine Oligomerisation and Conjugation in Protein Samples

A new presentation on the Malvern Instruments website discusses how the company's Viscotek TDAmax multiple detection size exclusion chromatography (SEC) system enables protein scientists to determine the degree of oligomerisation, aggregation, conformation, and conjugation in protein samples.

By combining data from light scattering, UV, refractive index (RI), and viscometer detection, the TDAmax delivers efficient measurement of absolute molecular weight and molecular size, as well as information about protein structure that is simply not available using more traditional systems. The presentation can be viewed at

The Viscotek TDAmax incorporates RI, light scattering and viscometer detectors, processing all three signals together at each data slice (5 Hz). By incorporating a combination of both low angle (7°) and right angle (90°) light scattering detectors, it can measure the absolute molecular weight (Mw) of a sample directly as it elutes from the column, without extrapolation or any additional modelling. Molecular weight, intrinsic viscosity and molecular size are determined across the entire distribution, state-of-the-art software enabling the results to be visualized graphically for ease of interpretation. The addition of a fourth detector, a UV or Diode Array UV, adds in compositional analysis - a very powerful tool for proteins scientists.

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