A theoretical study on noncovalent interactions involving posttranscriptional modifications and protein contact in context of RNA

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The major part of the present thesis is focused on the understanding the noncovalent hydrogen-bonding interactions between RNA and proteins. Despite the fact that hydrogen bonding has greater strength, specificity and thereby functional importance, limited studies are accomplished in literature on analysis of hydrogen bonds between RNA nucleotides and protein amino-acid residues. However, the availability of enhanced structural diversity in the now-available dataset of associated structures can help better understand these interactions. In addition to canonical (A, C, G and U) nucleobases, RNA contains a number of post-transcriptionally modified bases which occur in all types of RNA. A part of the present thesis analyzes the effect of methyl modification of nucleobases on their stacking abilities. Specifically, the study helps to explore the trends involving the positional effect of methyl modification of nucleobases through analysis of

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