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Volume 11
Journal of Proteomics & Bioinformatics
ISSN: 0974-276X
Structural Biology 2018
September 24-26, 2018
September 24-26, 2018 | Berlin, Germany
14
th
International Conference on
Structural Biology
Exhaustive mutation screens:
In silico
approaches for inferring the role of single and double amino
acid substitutions on protein structural stability
Filip Jagodzinski
Western Washington University, USA
U
nderstanding 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.
J Proteomics Bioinform 2018, Volume 11
DOI: 10.4172/0974-276X-C2-116