ISSN: 0974-276X
Filip Jagodzinski
Western Washington University, USA
Posters & Accepted Abstracts: J Proteomics Bioinform
Understanding how amino acid substitutions affect a protein's stability can aid in the design of pharmaceutical drugs that aim to counter the deleterious effects caused by protein mutants. Although mutagenesis experiments performed in a physical protein can provide precise insights about the role of a single amino acid, such experiments are laboriously difficult and may require months of wet lab work. Consequently, conducting exhaustive mutagenesis screens which involve mutating all residues to all other amino acids is impractical. To help guide such wet lab experiments, computational approaches are available but most do not permit an exhaustive screening of all residues and their impact on a protein when mutated. We have developed a suite of efficient algorithms for quickly generating mutants with one or more amino acid substitutions. In this presentation, we showcase our algorithms in the context of what others have done and we discuss progress in algorithms for exhaustive mutation screens assessing the role of two or three amino acid substitutions.