Stability and Structural Reversibility of Proteins Exposed to High Temperatures

This application note illustrates how the UNit can be used to assess protein stability and structural reversibility under elevated temperatures. The UNit can execute range of software-managed heating and cooling profiles in small volumes of sample, whilst simultaneously assessing protein structure via intrinsic fluorescence measurement and aggregation state using static light scattering (SLS). Yhis article highlights the benefits of UNit including precise and flexible temperature control, allowing multiple temperature profiles and highly responsive real-time analytical measurements for understanding protein stability.