TKSA-MC: A Web Server for rational mutation through the optimization of protein charge interactions

Abstract

The TKSAMC is a web server which calculates protein charge-charge interactions via the Tanford-Kirkwood Surface Accessibility model with the Monte Carlo method for sampling different protein protonation states. The optimization of charge-charge interactions via directed mutations has successfully enhanced the thermal stability of different proteins and could be a key to protein engineering improvement. The server presents the electrostatic free energy contribution of each polar-charged residue to protein native state stability. The server also indicates which residues contribute to destabilizing the protein native state with positive energy and the side chain exposed to solvent. This residue is a candidate for mutation to increase protein thermostability as a function of the chosen pH condition. The web server is freely available at UNESP (Sao Paulo State University - DF/IBILCE): http://tksamc.df.ibilce.unesp.br.