S. PRASANTH KUMAR 1, RAVI G. KAPOPARA 1,YOGESH T. JASRAI 1 AND RAKESH M. RAWAL 2.
1. Bioinformatics Laboratory, Department of Botany, University School of Sciences,
Ahmedabad- 380 009. 2. Division of Medicinal Chemistry and Pharmacogenomics, Department of Cancer Biology, Cancer & Research Institute (GCRI), Ahmedabad- 380 016.
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http://www.ijpbs.net/vol-3/issue-1/bio/B%20-%2068.pdf
Copyrights Reserved- International Journal of Pharma and Bio Sciences.
ABSTRACT:
It has been elucidated through in vitro studies that core histone tail domains preferentially interact with linker DNA. In the present study, we studied these interaction computationally using molecular docking and isocontour-based electrostatic map approach in order to identify the domains and regions of H3 and H4 tails and DNA contributing for the physical associativeness. We also explored the interaction made by the linker DNA containing methylated CpG dinucleotides (CpG island) with the normal and post-translational modified histone tails. We report that these interactions are electrostatically unfavored if one of the biomolecular partners is methylated thereby negatively charged zones of DNA and histone tails are required to be absent nearby.
KEYWORDS: Core histone tail domain, linker DNA, CpG island, Molecular docking, Isocontour-based
electrostatic potential map.
Here is the snapshot of a study undergone:
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