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• W1996427863 abstract "Antigen-antibody interactions are critical for understanding antigen-antibody associations in immunology. To shed further light on this question, we studied a dissociation of the 19D9D6-HCV core protein antibody complex structure. However, forced separations in single molecule experiments are difficult, and therefore molecular simulation techniques were applied in our study. The stretching, that is, the distance between the center of mass of the HCV core protein and the 19D9D6 antibody, has been studied using the potential of mean force calculations based on molecular dynamics and the explicit water model. Our simulations indicate that the 7 residues Gly70, Gly72, Gly134, Gly158, Glu219, Gln221 and Tyr314, the interaction region (antibody), and the 14 interprotein molecular hydrogen bonds might play important roles in the antigen-antibody interaction, and this finding may be useful for protein engineering of this antigen-antibody structure. In addition, the 3 residues Gly134, Gly158 and Tyr314 might be more important in the development of bioactive antibody analogs." @default.
• W1996427863 created "2016-06-24" @default.
• W1996427863 creator A5005348783 @default.
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• W1996427863 date "2009-12-01" @default.
• W1996427863 modified "2023-10-14" @default.
• W1996427863 title "Potential of mean force of the hepatitis C virus core protein–monoclonal 19D9D6 antibody interaction" @default.
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• W1996427863 doi "https://doi.org/10.1016/j.bpc.2009.09.004" @default.
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