Imura, T., & Tomonaga, M. (2003). Perception of depth from shading in infant chimpanzees ( Pan troglodytes). Anim. Cogn., 6(4), 253–258.
Abstract: We investigated the ability to perceive depth from shading, one of the pictorial depth cues, in three chimpanzee infants aged 4-10 months old, using a preferential reaching task commonly used to study pictorial depth perception in human infants. The chimpanzee infants reached significantly more to three-dimensional toys than to pictures thereof and more to the three-dimensional convex than to the concave. Furthermore, two of the three infants reached significantly more to the photographic convex than to the photographic concave. These infants also looked longer at the photographic convex than the concave. Our results suggest that chimpanzees perceive, at least as early as the latter half of the first year of life, pictorial depth defined by shading information. Photographic convexes contain richer information about pictorial depth (e.g., attached shadow, cast shadow, highlighted area, and global difference in brightness) than simple computer-graphic graded patterns. These cues together might facilitate the infants' perception of depth from shading.
|
Uzawa, T., Akiyama, S., Kimura, T., Takahashi, S., Ishimori, K., Morishima, I., et al. (2004). Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness. Proc. Natl. Acad. Sci. U.S.A., 101(5), 1171–1176.
Abstract: The characterization of protein folding dynamics in terms of secondary and tertiary structures is important in elucidating the features of intraprotein interactions that lead to specific folded structures. Apomyoglobin (apoMb), possessing seven helices termed A-E, G, and H in the native state, has a folding intermediate composed of the A, G, and H helices, whose formation in the submillisecond time domain has not been clearly characterized. In this study, we used a rapid-mixing device combined with circular dichroism and small-angle x-ray scattering to observe the submillisecond folding dynamics of apoMb in terms of helical content (f(H)) and radius of gyration (R(g)), respectively. The folding of apoMb from the acid-unfolded state at pH 2.2 was initiated by a pH jump to 6.0. A significant collapse, corresponding to approximately 50% of the overall change in R(g) from the unfolded to native conformation, was observed within 300 micros after the pH jump. The collapsed intermediate has a f(H) of 33% and a globular shape that involves >80% of all its atoms. Subsequently, a stepwise helix formation was detected, which was interpreted to be associated with a conformational search for the correct tertiary contacts. The characterized folding dynamics of apoMb indicates the importance of the initial collapse event, which is suggested to facilitate the subsequent conformational search and the helix formation leading to the native structure.
|
