Protein stability is essential to protein function, therefore knowledge about stabilizing conditions must be acquired prior to perform further studies on a protein of interest (POI; i.e. structure determination, activity, interactions or folding). When large libraries of mutant proteins are generated for the screening of new or improved functions, it is also desirable to quickly determine the stability of these proteins. This typically requires expensive biophysical instrumentation and large quantities of purified proteins. The monitoring of protein stability has also major applications in the screening of protein-ligand interactions. Thermal denaturation-based methods such as thermofluor are currently used for this purpose in drug discovery programs.
展开▼
