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• W2533862664 abstract "The significant improvement of KE07 series in catalytic activities shows the great success of computational design approaches combined with directed evolution in protein design. Understanding the protein dynamics in the evolutionary optimization process of computationally designed enzyme will provide profound implication to study enzyme function and guide protein design. Here, side chain squared generalized order parameters and entropy of each protein are calculated using 50 ns molecular dynamics simulation data in both apo and bound states. Our results show a correlation between the increase of side chain motion amplitude and catalytic efficiency. By analyzing the relationship between these two values, we find side chain squared generalized order parameter is linearly related to side chain entropy, which indicates the computationally designed KE07 series have similar dynamics property with natural enzymes." @default.
• W2533862664 created "2016-10-28" @default.
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• W2533862664 date "2016-12-01" @default.
• W2533862664 modified "2023-10-17" @default.
• W2533862664 title "Side-chain dynamics analysis of KE07 series" @default.
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• W2533862664 doi "https://doi.org/10.1016/j.compbiolchem.2016.09.007" @default.
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