Valdebenito-Maturana, BraulioReyes-Suarez, Jose AntonioHenriquez, JaimeHolmes, David S.Quatrini, RaquelPohl, EhmkeArenas-Salinas, Mauricio2024-06-262024-06-262017-03Journal of computational chemistry Volume 38, Issue 7, Pages 467 - 47415 March 20171096-987Xhttps://repositorio.unab.cl/handle/ria/57991Indexación: ScopusThe electrostatic potential plays a key role in many biological processes like determining the affinity of a ligand to a given protein target, and they are responsible for the catalytic activity of many enzymes. Understanding the effect that amino acid mutations will have on the electrostatic potential of a protein, will allow a thorough understanding of which residues are the most important in a protein. MutantElec, is a friendly web application for in silico generation of site-directed mutagenesis of proteins and the comparison of electrostatic potential between the wild type protein and the mutant(s), based on the three-dimensional structure of the protein. The effect of the mutation is evaluated using different approach to the traditional surface map. MutantElec provides a graphical display of the results that allows the visualization of changes occurring at close distance from the mutation and thus uncovers the local and global impact of a specific change. © 2017 Wiley Periodicals, Inc. © 2017 Wiley Periodicals, Inc.enbioinformaticsElectrostatic potentialp53PDBprotein engineeringrational protein designsite-directed mutagenesisArtículoATRIBUCIÓN 4.0 INTERNACIONAL CC BY 4.0 Deed10.1002/jcc.24712