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• W2003374450 endingPage "834" @default.
• W2003374450 startingPage "823" @default.
• W2003374450 abstract "DNA repair enzymes induce base flipping in the process of damage recognition. Endonuclease V initiates the repair of cis, syn thymine dimers (TD) produced in DNA by UV radiation. The enzyme is known to flip the base opposite the damage into a non-specific binding pocket inside the protein. Uracil DNA glycosylase removes a uracil base from G·U mismatches in DNA by initially flipping it into a highly specific pocket in the enzyme. The contribution of base flipping to specific recognition has been studied by molecular dynamics simulations on the closed and open states of undamaged and damaged models of DNA. Analysis of the distributions of bending and opening angles indicates that enhanced base flipping originates in increased flexibility of the damaged DNA and the lowering of the energy difference between the closed and open states. The increased flexibility of the damaged DNA gives rise to a DNA more susceptible to distortions induced by the enzyme, which lowers the barrier for base flipping. The free energy profile of the base-flipping process was constructed using a potential of mean force representation. The barrier for TD-containing DNA is 2.5 kcal mol−1 lower than that in the undamaged DNA, while the barrier for uracil flipping is 11.6 kcal mol−1 lower than the barrier for flipping a cytosine base in the undamaged DNA. The final barriers for base flipping are approximately 10 kcal mol−1, making the rate of base flipping similar to the rate of linear scanning of proteins on DNA. These results suggest that damage recognition based on lowering the barrier for base flipping can provide a general mechanism for other DNA-repair enzymes." @default.
• W2003374450 created "2016-06-24" @default.
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• W2003374450 date "2002-11-01" @default.
• W2003374450 modified "2023-10-18" @default.
• W2003374450 title "Role of Base Flipping in Specific Recognition of Damaged DNA by Repair Enzymes" @default.
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• W2003374450 doi "https://doi.org/10.1016/s0022-2836(02)00999-3" @default.
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