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• W2024015808 abstract "Proteins recognize specific DNA sequences not only through direct contact between amino acids and bases, but also indirectly based on the sequence-dependent conformation and deformability of the DNA (indirect readout). We used molecular dynamics simulations to analyze the sequence-dependent DNA conformations of all 136 possible tetrameric sequences sandwiched between CGCG sequences. The deformability of dimeric steps obtained by the simulations is consistent with that by the crystal structures. The simulation results further showed that the conformation and deformability of the tetramers can highly depend on the flanking base pairs. The conformations of xATx tetramers show the most rigidity and are not affected by the flanking base pairs and the xYRx show by contrast the greatest flexibility and change their conformations depending on the base pairs at both ends, suggesting tetramers with the same central dimer can show different deformabilities. These results suggest that analysis of dimeric steps alone may overlook some conformational features of DNA and provide insight into the mechanism of indirect readout during protein-DNA recognition. Moreover, the sequence dependence of DNA conformation and deformability may be used to estimate the contribution of indirect readout to the specificity of protein-DNA recognition as well as nucleosome positioning and large-scale behavior of nucleic acids." @default.
• W2024015808 created "2016-06-24" @default.
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• W2024015808 date "2007-08-30" @default.
• W2024015808 modified "2023-10-11" @default.
• W2024015808 title "Sequence-dependent DNA deformability studied using molecular dynamics simulations" @default.
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• W2024015808 doi "https://doi.org/10.1093/nar/gkm627" @default.
• W2024015808 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2094071" @default.
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• W2024015808 hasPublicationYear "2007" @default.
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