20.500.12556/RUL-148272 The mechanism of self-association of human ▫$\gamma$▫-D crystallin from molecular dynamics simulations The aggregation of human $\gamma$-D crystallin is associated with the age-onset cataract formation. Here, we extensively investigated the self-association mechanism of human $\gamma$-D crystallin through molecular dynamics computer simulations. By mutating the protein surface we found that electrostatic interactions between charged amino acids play a crucial role in its self-association. We have confirmed the two-fold role of arginine molecules. If they are located as residues on the protein surface they can initiate protein contacts and contribute to their stickiness with noteworthy hydrophobic interactions through stacking of their methylene groups. But if they are added as free arginine in the protein solution they can also stabilize it, by associating with the protein surface and also with themselves to form effective inter-protein spacers that obstruct protein aggregation. γ-D crystallin self-assembly arginine MD simulation gama-D-kristalin samozdruževanje arginin simulacija molekulske dinamike true false true Angleški jezik Slovenski jezik Članek v reviji 2023-08-09 10:07:03 2023-08-09 10:07:05 2024-02-06 11:23:42 0000-00-00 00:00:00 2023 0 0 8 str. Vol. 386, art. 122461 15 Sep. 2023 0000-00-00 Zaloznikova Objavljeno NiDoloceno 0000-00-00 0000-00-00 0000-00-00 577.322 0167-7322 10.1016/j.molliq.2023.122461 157958915 1-s2.0-S0167732223012655-main.pdf 1-s2.0-S0167732223012655-main.pdf 1 DB2DA928DE5E7338806FEEFD6E464971 4bd62b4c3c93fbda65ae87e39d7fe0ede6e34f934e79adbf3cdcb48846c15fac 43dbc277-368d-11ee-aeaf-00155dcfd717 https://repozitorij.uni-lj.si/Dokument.php?lang=slv&id=172348 https://www.sciencedirect.com/science/article/pii/S0167732223012655 1 b2ae928c-368b-11ee-aeaf-00155dcfd717 https://repozitorij.uni-lj.si/Dokument.php?lang=slv&id=172347 Fakulteta za kemijo in kemijsko tehnologijo 0 0 0