Ghrelin is a peptide hormone made up of 28 amino acids. It is involved in various biological processes, including the stimulation of growth hormone release, control of food intake, and metabolic and cytoprotective eff ects. In 1999, this hormone was identifi ed as a ligand for the GHSR1a growth hormone secretagogue receptor. Ghrelin hormone-receptor complexes have been modeled in a few previous in-silico studies, but none of them have investigated the eff ects of the gene variation rs34911341/(R51Q) on the full-length ghrelin model and on the hormone-receptor binding. It was established that the full-length ghrelin model’s secondary structure was unaff ected by the R to Q amino acid substitution. Additionally, the mutant hormone-receptor complex exhibited better outcomes and altered the molecular interactions between the mutant ligand and the receptor by creating novel interactions, according to the post-molecular dynamic simulation analysis.