Tekin, E. Deniz; Calisir, MetinTekin, Emine Deniz2024-06-252024-06-2520221292-8941https://acikarsiv.thk.edu.tr/handle/123456789/1165Human beta-defensins present in saliva have a broad spectrum of antimicrobial activities that work against infections in oral cavity. To provide a better understanding of these molecules' properties and functions at the molecular level, we have investigated and compared the important structural properties of human beta-defensin-1, -2 and -3 using molecular dynamics simulations. Our results have shown that human beta-defensin-3 has a more flexible structure in water than the other two because of its high hydrophilicity, low beta-sheet content and high repulsive forces between its charged residues. Moreover, we found that the location of the salt bridges is important in protein's stability in water.EnglishRANGE ELECTROSTATIC INTERACTIONS; ANTIMICROBIAL PEPTIDES; HUMAN BETA-DEFENSIN-2; EXPRESSION; STABILITY; CRYSTALS; HBD-1Article