TKSA-MC: A Web Server for rational mutation through the optimization of protein charge interactions
- Resource Type
- Authors
- Vitor B. P. Leite; Bruno R. Fernandes; Vinícius M. de Oliveira; Gabriel G. Slade; Vinícius G. Contessoto
- Source
- Subject
- 0301 basic medicine
Protein Folding
Web server
Protein Conformation
Static Electricity
Monte Carlo method
Protonation
computer.software_genre
Biochemistry
03 medical and health sciences
Structural Biology
Native state
Side chain
Thermal stability
Molecular Biology
Thermostability
Physics
Residue (complex analysis)
Internet
030102 biochemistry & molecular biology
Protein Stability
Chemistry
Proteins
Protein engineering
Positive energy
030104 developmental biology
Mutation
Thermodynamics
Biological system
Monte Carlo Method
computer
Software
- Language
- English
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 (São Paulo State University - DF/IBILCE): http://tksamc.df.ibilce.unesp.br.