Abstract: Summary Spatial orientation has played an extremely important role in the development of ideas about the behavioral capacities of animals. Indeed, as the modern scientific study of animal behavior emerged from its roots in zoology and experimental psychology, studies of spatial orientation figured in the work of many of the pioneering researchers, including Tinbergen (), von ), Watson () and .

Abstract: Summary In this chapter I want to stand back from the splendid empirical work on animal cognitive capacities that is the focus of this book, and look at the broader context of cognitive concerns within which the work can be viewed. Indeed even the term `cognitive ethology' currently connotes and denotes more than is represented here, as other collections of articles, such as and , exemplify. I include the current descendants of behavioristic learning theory, evolutionary epistemology, evolutionary psychology and the recent comparative turn that has been taken in cognitive science. These several approaches, despite their considerable overlap, often appear independent and even ignorant of one another. Like the proverbial blind men feeling the hide of an elephant, they touch hands from time to time, yet collectively have only a piecemeal and distributed understanding of the shape of the whole. Although each approach may indeed need the space to work out its own conceptual and methodological preoccupations without confounding interference from other views, a utopian spirit envisages an ultimate coming together, a more comprehensive realization of the synthetic approach to animal cognition that is this book's theme.

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.