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- W2130492893 abstract "Simulating antigen–antibody interactions is crucial in understanding the mechanics of antigen–antibody binding in medical science. In this study, molecular dynamics simulations are performed to analyse the dissociation of the P1053-0.5β antibody complex structure. The two-dimensional free energy profiles of the complex structure are extracted using the weighted histogram analysis method, and the binding pathway is then predicted using a modified form of the MaxFlux-PRM method. The simulation results suggest that 10 amino residues (i.e. Leu11, Val13, Asp34, Arg112, Thr101, Gly127, Val229, Ser231, Ile235 and Arg236) play a key role in relaxing the antibody structure, thereby facilitating the binding of the 0.5β antibody-P1053 peptide system." @default.
- W2130492893 created "2016-06-24" @default.
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- W2130492893 date "2011-02-01" @default.
- W2130492893 modified "2023-10-14" @default.
- W2130492893 title "Modelling and predicting the binding mechanics of HIV P1053-0.5β antibody complex" @default.
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- W2130492893 doi "https://doi.org/10.1080/08927022.2010.533274" @default.
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