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• W2039482020 startingPage "1136" @default.
• W2039482020 abstract "Abstract The DNA binding domain of transposon Tn916 integrase (INT‐DBD) binds to DNA target site by positioning the face of a three‐stranded antiparallel β‐sheet within the major groove. As the negatively charged DNA directly interacts with the positively charged residues (such as Arg and Lys) of INT‐DBD, the electrostatic interaction is expected to play an important role in the dynamical stability of the protein–DNA binding complex. In the current work, the combined use of quantum‐based polarized protein‐specific charge (PPC) for protein and polarized nucleic acid‐specific charge (PNC) for DNA were employed in molecular dynamics simulation to study the interaction dynamics between INT‐DBD and DNA. Our study shows that the protein–DNA structure is stabilized by polarization and the calculated protein–DNA binding free energy is in good agreement with the experimental data. Furthermore, our study revealed a positive correlation between the measured binding energy difference in alanine mutation and the occupancy of the corresponding residue's hydrogen bond. This correlation relation directly relates the contribution of a specific residue to protein–DNA binding energy to the strength of the hydrogen bond formed between the specific residue and DNA. © 2013 Wiley Periodicals, Inc." @default.
• W2039482020 created "2016-06-24" @default.
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• W2039482020 creator A5088349481 @default.
• W2039482020 date "2013-02-05" @default.
• W2039482020 modified "2023-10-12" @default.
• W2039482020 title "Molecular dynamics study of DNA binding by INT-DBD under a polarized force field" @default.
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• W2039482020 doi "https://doi.org/10.1002/jcc.23244" @default.
• W2039482020 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23386461" @default.
• W2039482020 hasPublicationYear "2013" @default.
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