ArticleJournal of biosciences2026
Effects of acetylation on human insulin structure, and dynamics at different temperatures: A molecular dynamics simulation study.
Article in Journal of biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Insulin was used as a model protein to investigate the effects of acetylation, a significant post-translational modification. Acetylation typically targets terminal and side-chain amine groups, which, in insulin, correspond to three specific sites. Molecular dynamics simulations were conducted at pH 5.0 and three different temperatures on various acetylated insulin forms, in both monomeric and dimeric states. Two acetylation states - modification of the B-chain N-terminus alone, and modification of both the B-chain N-terminus and Lys29 - exhibited distinct properties compared with other acetylation variants. Overall, the results indicate that chemical acetylation can enhance structural compactness and reduce the propensity for protein-protein association. Key evaluated parameters included root-mean-square deviation, root-mean-square fluctuation, complex formation energy, radius of gyration, secondary structure content, and solvent-accessible surface area. At pH 5.0 and 323 K, insulin showed increased structural flexibility, accompanied by a transition from α-helix to 3
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