HIV-1 carries its genetic information on a single-stranded RNA that is reverse transcribed into double-stranded DNA before integration into the host cell’s genome. Reverse transcription involves a complicated series of biochemical reactions and strand transfer events. The strand-exchange reactions are facilitated by NC protein due to its nucleic acid chaperone activity, i.e., the ability to catalyze nucleic acid conformational rearrangements that lead to the most thermodynamically stable structure. My research focuses on the role of NC protein (i) in the destabilization of nucleic acid secondary structure (i.e., duplex, quadruplex), and (ii) strand-exchange kinetics using various thermodynamic (ITC, DSC, optical unfolding) and spectroscopic techniques (UV, CD, fluorescence).
614 – 688-8799