| 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). |
