Date of Submission
Spring 2011
Academic Program
Chemistry
Advisor
Swapan Jain
Abstract/Artist's Statement
Protein enzymes are the predominant catalytic molecules in modern day cellular systems.
However, it is widely believed that in the precellular world, RNA polymers used to be the
primary molecules for both catalysis and retention of genetic information. It’s a mystery how
these RNA polymers assembled and replicated during not only the RNA world but also the
transitionary period when polypeptides started to emerge. Watson-Crick base pairing and
hydrophobic stacking alone could not have sufficiently stabilized an assembly of nucleotides. It
is possible that small and flat intercalating molecules were used for the assembly of the
nucleotides, until more specific enzymes took over. For our studies, we have shown that
proflavine (a flat intercalator) can enhance the coupling efficiency of two short oligonucleotide
strands, catalyzed by a biological ligase enzyme
Distribution Options
Access restricted to On-Campus only
Recommended Citation
Velissaris, Stavros, "ENHANCEMENT OF A TEMPLATE-DIRECTED ENZYMATIC REACTION BY INTERCALATING MOLECULES" (2011). Senior Projects Spring 2011. 91.
https://digitalcommons.bard.edu/senproj_s2011/91
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