NCBR seminar: David Bednář

Abstract:

Protein stability is a key factor in understanding function, designing therapeutics, and engineering enzymes for biotechnological applications. The FireProt approach combines computational predictions with experimental validation to optimize protein stability efficiently. Using integrated computational methods, including energy calculations and evolutionary analysis, FireProt identifies stabilizing mutations while minimizing negative effects on protein function. This strategy enables the rational design of robust proteins for industrial, medical, and research purposes. The approach has been applied to a variety of enzymes, demonstrating significant improvements in thermal and chemical stability. By combining structural modeling with high-throughput mutational analysis, the workflow accelerates protein engineering while reducing experimental costs. The method also considers protein dynamics and folding pathways to ensure mutations support natural conformational flexibility. FireProt provides a framework for predicting synergistic effects of multiple mutations, leading to highly stable variants. Its computational efficiency allows rapid screening of candidate mutations before laboratory testing. Overall, FireProt exemplifies how computational tools can transform protein engineering and facilitate the design of proteins with enhanced stability and function.