Abstract: Social monitoring has been hypothesized to be an important component of primate social behavior. If the gaze direction of one animal can redirect the gaze of another, visual scanning of conspecifics can provide a more efficient means of locating food or predators than directly scanning the entire nonsocial environment. Social monitoring also allows distance regulation between members of a group, reducing the likelihood of agonistic encounters. Although assessment of gaze direction in freely moving primates is problematic, we were successful in assessing amounts of visual scanning among adult females of a captive, socially housed group of patas monkeys (Erythrocebus patas) using a focal sampling technique with on-the-dot recording (5-s sampling intervals). In study 1, relative amounts of scanning were assessed as subjects gazed at any other member of the group. Percentages of agreement between observers ranged from 80% to 92%, with corresponding &#115 values ranging from 0.74 to 0.92. In study 2, relative amounts of visual scanning were assessed so that specific targets of gaze were identified. The resultant data supported a long-standing prediction about the role of social monitoring in primate group dynamics. Lower-ranking animals gazed toward higher-ranking animals more often than vice versa. Although the specific cues eliciting social monitoring remain to be determined, visual attention in this social primate group appeared to be systematically related to hierarchical ranks, assessed by displacements. Minimally, these results suggest that patas monkeys structure their visual attention based on previous encounters with other members of their social group. While simple discrimination learning could account for these results, the demonstration of a systematic relationship between visual attention and primate social dynamics is relevant to current discussions of a primate's understanding of conspecific gaze direction.

Abstract: The equilibrium unfolding and the kinetics of unfolding and refolding of equine lysozyme, a Ca2+-binding protein, were studied by means of circular dichroism spectra in the far and near-ultraviolet regions. The transition curves of the guanidine hydrochloride-induced unfolding measured at 230 nm and 292.5 nm, and for the apo and holo forms of the protein have shown that the unfolding is well represented by a three-state mechanism in which the molten globule state is populated as a stable intermediate. The molten globule state of this protein is more stable and more native-like than that of α-lactalbumin, a homologous protein of equine lysozyme. The kinetic unfolding and refolding of the protein were induced by concentration jumps of the denaturant and measured by stopped-flow circular dichroism. The observed unfolding and refolding curves both agreed well with a single-exponential function. However, in the kinetic refolding reactions below 3 M guanidine hydrochloride, a burst-phase change in the circular dichroism was present, and the burst-phase intermediate in the kinetic refolding is shown to be identical with the molten globule state observed in the equilibrium unfolding. Under a strongly native condition, virtually all the molecules of equine lysozyme transform the structure from the unfolded state into the molten globule, and the subsequent refolding takes place from the molten globule state. The transition state of folding, which may exist between the molten globule and the native states, was characterized by investigating the guanidine hydrochloride concentration-dependence of the rate constants of refolding and unfolding. More than 80% of the hydrophobic surface of the protein is buried in the transition state, so that it is much closer to the native state than to the molten globule in which only 36% of the surface is buried in the interior of the molecule. It is concluded that all the present results are best explained by a sequential model of protein folding, in which the molten globule state is an obligatory folding intermediate on the pathway of folding.