The response to selection in Glycoside Hydrolase Family 13 structures: A comparative quantitative genetics approach.

ABSTRACT: The Glycoside Hydrolase Family 13 (GH13) is both evolutionarily diverse and relevant to many industrial applications. Its members hydrolyze starch into smaller carbohydrates and members of the family have been bioengineered to improve catalytic function under industrial environments. We introduce a framework to analyze the response to selection of GH13 protein structures given some phylogenetic and simulated dynamic information. We find that the TIM-barrel (a conserved protein fold consisting of eight α-helices and eight parallel β-strands that alternate along the peptide backbone, common to all amylases) is not selectable since it is under purifying selection. We also show a method to rank important residues with higher inferred response to selection. These residues can be altered to effe

SUBMITTER: Hleap JS 

PROVIDER: S-EPMC5919626 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature