Base flip in DNA studied by molecular dynamics simulations of differently-oxidized forms of methyl-cytosine
Helabad MB, Kanaan N, Imhof P (2014)
Publication Type: Journal article
Publication year: 2014
Journal
Book Volume: 15
Pages Range: 11799-11816
Journal Issue: 7
Abstract
Distortions in the DNA sequence, such as damage or mispairs, are specifically recognized and processed by DNA repair enzymes. Many repair proteins and, in particular, glycosylases flip the target base out of the DNA helix into the enzyme's active site. Our molecular dynamics simulations of DNA with intact and damaged (oxidized) methyl-cytosine show that the probability of being flipped is similar for damaged and intact methyl-cytosine. However, the accessibility of the different 5-methyl groups allows direct discrimination of the oxidized forms. Hydrogen-bonded patterns that vary between methyl-cytosine forms carrying a carbonyl oxygen atom are likely to be detected by the repair enzymes and may thus help target site recognition. © 2014 by the authors; licensee MDPI, Basel, Switzerland.
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Germany (DE)How to cite
APA:
Helabad, M.B., Kanaan, N., & Imhof, P. (2014). Base flip in DNA studied by molecular dynamics simulations of differently-oxidized forms of methyl-cytosine. International Journal of Molecular Sciences, 15(7), 11799-11816. https://dx.doi.org/10.3390/ijms150711799
MLA:
Helabad, Mahdi Bagherpoor, Natalia Kanaan, and Petra Imhof. "Base flip in DNA studied by molecular dynamics simulations of differently-oxidized forms of methyl-cytosine." International Journal of Molecular Sciences 15.7 (2014): 11799-11816.
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