  Mechanical unfolding trajectories, generated by applying constant force in
optical tweezer experiments, show that RNA hairpins and the P5abc subdomain of
the group I intron unfold reversibly. We use coarse-grained Go-like models for
RNA hairpins to explore forced-unfolding over a broad range of temperatures. A
number of predictions that are amenable to experimental tests are made. At the
critical force the hairpin jumps between folded and unfolded conformations
without populating any discernible intermediates. The phase diagram in the
force-temperature (f,T) plane shows that the hairpin unfolds by an all-or-none
process. The cooperativity of the unfolding transition increases dramatically
at low temperatures. Free energy of stability, obtained from time averages of
mechanical unfolding trajectories, coincide with ensemble averages which
establishes ergodicity. The hopping time between the the native basin of
attraction (NBA) and the unfolded basin increases dramatically along the phase
boundary. Thermal unfolding is stochastic whereas mechanical unfolding occurs
in "quantized steps" with great variations in the step lengths. Refolding
times, upon force quench, from stretched states to the NBA is "at least an
order of magnitude" greater than folding times by temperature quench. Upon
force quench from stretched states the NBA is reached in at least three stages.
In the initial stages the mean end-to-end distance decreases nearly
continuously and only in the last stage there is a sudden transition to the
NBA. Because of the generality of the results we propose that similar behavior
should be observed in force quench refolding of proteins.
