This title appears in the Scientific Report :
2015
Please use the identifier:
http://dx.doi.org/10.1093/nar/gkv254 in citations.
Please use the identifier: http://hdl.handle.net/2128/9665 in citations.
The structural impact of DNA mismatches
The structural impact of DNA mismatches
The structure and dynamics of all the transversion and transition mismatches in three different DNA environments have been characterized by molecular dynamics simulations and NMR spectroscopy. We found that the presence of mismatches produced significant local structural alterations, especially in t...
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Personal Name(s): | Rossetti, G. |
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Dans, P. D. / Gomez-Pinto, I. / Ivani, I. / Gonzalez, C. / Orozco, M. (Corresponding author) | |
Contributing Institute: |
Computational Biomedicine; INM-9 Computational Biomedicine; IAS-5 Jülich Supercomputing Center; JSC |
Published in: | Nucleic acids symposium series, 43 (2015) 8, S. 4309 - 4321 |
Imprint: |
Oxford
Oxford Univ. Press69994
2015
|
DOI: |
10.1093/nar/gkv254 |
Document Type: |
Journal Article |
Research Program: |
Computational Science and Mathematical Methods |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/9665 in citations.
The structure and dynamics of all the transversion and transition mismatches in three different DNA environments have been characterized by molecular dynamics simulations and NMR spectroscopy. We found that the presence of mismatches produced significant local structural alterations, especially in the case of purine transversions. Mismatched pairs often show promiscuous hydrogen bonding patterns, which interchange among each other in the nanosecond time scale. This therefore defines flexible base pairs, where breathing is frequent, and where distortions in helical parameters are strong, resulting in significant alterations in groove dimension. Even if the DNA structure is plastic enough to absorb the structural impact of the mismatch, local structural changes can be propagated far from the mismatch site, following the expected through-backbone and a previously unknown through-space mechanism. The structural changes related to the presence of mismatches help to understand the different susceptibility of mismatches to the action of repairing proteins. |