Secondary structure and secondary structure dynamics of DNA hairpins complexed with HIV-1 NC protein.

Reverse transcription of the HIV-1 RNA genome involves several complex nucleic acid rearrangement steps that are catalyzed by the HIV-1 nucleocapsid protein (NC), including for example, the annealing of the transactivation response (TAR) region of the viral RNA to the complementary region (TAR DNA) in minus-strand strong-stop DNA. We report herein single-molecule fluorescence resonance energy transfer measurements on single immobilized TAR DNA hairpins and hairpin mutants complexed with NC (i.e.

Nucleic acid conformational changes essential for HIV-1 nucleocapsid protein-mediated inhibition of self-priming in minus-strand transfer.

Reverse transcription of the HIV-1 genome is a complex multi-step process. HIV-1 nucleocapsid protein (NC) is a nucleic acid chaperone protein that has been shown to greatly facilitate the nucleic acid rearrangements that precede the minus-strand transfer step in reverse transcription. NC destabilizes the highly structured transactivation response region (TAR) present in the R region of the RNA genome, as well as a complementary hairpin structure ("TAR DNA") at the 3'-end of the newly synthesized minus-strand strong-stop DNA ((-) SSDNA).

Iron(VI) and iron(V) oxidation of thiocyanate.

Thiocyanate (SCN-) is used in many industrial processes and is commonly found in industrial and mining waste-waters. The removal of SCN- is required because of its toxic effects. The oxidation of thiocyanate (SCN-) by environmentally friendly oxidants, Fe(VI) and Fe(V), has been studied anaerobically using stopped-flow and premix pulse radiolysis techniques.