RNA conformational transitions and RNA chaperone activity

Chaperone proteins help RNAs adopt their relevant functional states. However, little is known about the mechanistic details of RNA chaperone activity. We used a combination of real-time and steady-state NMR methods to decipher the RNA duplex formation pathways of two complementary RNA hairpins, as well as the chaperone activity of the small bacterial cold shock protein CspA on this folding reaction.
Collaborations : C. Kreutz (Innsbruck, Austria), R. Konrat (Vienna, Austria)