To draw general conclusions about the effects of different amino acid substitutions, we analyzed 34,373 mutations in fourteen proteins whose effects were measured using large-scale mutagenesis approaches. Methionine was the most tolerated substitution while proline was the least tolerated. Histidine and asparagine best recapitulated the effects of other substitutions, even when the identity of the wild type amino acid was considered. Furthermore, highly disruptive substitutions like aspartic and glutamic acid had the most discriminatory power for detecting ligand interface positions. Our work highlights the utility of large-scale mutagenesis data, and our conclusions can help guide future mutagenesis studies.
Here, we present the code used to generate figures found in "Analysis of Large-Scale Mutagenesis Data To Assess the Impact of Single Amino Acid Substitutions".
To use, open our R Markdown file, edit the line (i.e., data <- read.csv("~/informativeAA_20170404.csv", header = TRUE) that points to the provided .csv file and then run the code.