Computational molecular explanation of Soybean AHAS resistance from P197S mutation

17 November 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Crop management through the use of herbicides is an integral part of modern high-yield farming. The identification of resistant mutated strains of normal plants amongst a background of weeds is important to the usage of herbicides, their development, and resistance. In this work a computational study of a point mutation of Proline-197-Serine of the Soybean AHAS enzyme explains the latter’s S197 resistance to the commonly used Chlorsulfuron. Just as a small molecular change to a therapeutic can alter drastically the binding and efficacy of a drug, a small substitution of one amino acid in a target can alter the binding and efficacy of an herbicide through conformation and binding changes of the bound inhibitor, e.g., eliminating a dominant bound herbicide conformation and de-localization generally of the binding. The computational approach here using large scale sampling and distributions from protein-ligand docking and AlphaFold generated protein structures is easily scaled to scan over the mutation possibilities of protein binding sites, similar to screening compounds for potential hits in therapeutic design.


AHAS (ALS) enzyme
protein-ligand interactions
small molecule inhibitors
crop management
protein engineering

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