The relationship between observing behavior and food-key response rates under mixed and multiple schedules of reinforcement

Pigeons were trained under an observing response procedure in which pecks on one key (food key) were reinforced under a mixed fixed-interval 30-sec extinction schedule. A response on a second (observing) key replaced the mixed-schedule stimulus with either of two multiple-schedule stimuli (red and green keylights) for 5 sec. Observing response rates were positively correlated with food-key response rates in the presence of multiple-schedule stimuli and inversely related to food-key response rates in the presence of mixed-schedule stimuli. These results suggest that observing response output is controlled not only by the stimuli produced by observing responses but also by the stimuli in the presence of which observing responses occur. The possibility that observing responses alter the probability of reinforcement is advanced

Hinge-Like Motions in RNA Kink-Turns: The Role of the Second A-Minor Motif and Nominally Unpaired Bases

Kink-turn (K-turn) motifs are asymmetric internal loops found at conserved positions in diverse RNAs, with sharp bends in phosphodiester backbones producing V-shaped structures. Explicit-solvent molecular dynamics simulations were carried out for three K-turns from 23S rRNA, i.e., Kt-38 located at the base of the A-site finger, Kt-42 located at the base of the L7/L12 stalk, and Kt-58 located in domain III, and for the K-turn of human U4 snRNA. The simulations reveal hinge-like K-turn motions on the nanosecond timescale. The first conserved A-minor interaction between the K-turn stems is entirely stable in all simulations. The angle between the helical arms of Kt-38 and Kt-42 is regulated by local variations of the second A-minor (type I) interaction between the stems. Its variability ranges from closed geometries to open ones stabilized by insertion of long-residency waters between adenine and cytosine. The simulated A-minor geometries fully agree with x-ray data. Kt-58 and Kt-U4 exhibit similar elbow-like motions caused by conformational change of the adenosine from the nominally unpaired region. Despite the observed substantial dynamics of K-turns, key tertiary interactions are stable and no sign of unfolding is seen. We suggest that some K-turns are flexible elements mediating large-scale ribosomal motions during the protein synthesis cycle