Abstract 2940 Comparing the structure, function, and stability of engineered homeodomains and natural variants

The improvement of stability of engineered proteins is an important area of research given several applications that require proteins to be very stable. Biocatalysts need to be stable in environments required for chemical reactions. Proteins used as therapeutics, such as antibodies and nanobodies, need to have long shelf-lives to minimize costs. It is known that there is a generally inverse relationship between protein stability and flexibility. Proteins move around in solution and have intrinsic flexibility, which, in turn, is critical for their functionality.