Application Note: Thermal Ramp Experiments Measure Protein Conformational Stability and Propensity to Aggregate
4 February 2017

This application note describes the use of UNit to carry out thermal ramp experiments to define multiple stability-defining parameters, including Tm and Tagg. The UNit heats samples to a defined temperature range at a defined rate, exploiting the fluorescent properties of the protein to monitor unfolding and calculate the Tm and the intensity of static light scattering (SLS) to calculate Tagg. The ability to obtain information on both conformational stability and aggregation propensity provides more detail on degradation mechanism of a protein sample.

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