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Abramson, J. Z., Hernández-Lloreda, V., Call, J., & Colmenares, F. (2013). Experimental evidence for action imitation in killer whales (Orcinus orca). Animal Cognition, 16(1), 11–22.
Abstract: Comparative experimental studies of imitative learning have focused mainly on primates and birds. However, cetaceans are promising candidates to display imitative learning as they have evolved in socioecological settings that have selected for large brains, complex sociality, and coordinated predatory tactics. Here we tested imitative learning in killer whales, Orcinus orca. We used a ‘do-as-other-does’ paradigm in which 3 subjects witnessed a conspecific demonstrator’s performance that included 15 familiar and 4 novel behaviours. The three subjects (1) learned the copy command signal ‘Do that’ very quickly, that is, 20 trials on average; (2) copied 100 % of the demonstrator’s familiar and novel actions; (3) achieved full matches in the first attempt for 8–13 familiar behaviours (out of 15) and for the 2 novel behaviours (out of 2) in one subject; and (4) took no longer than 8 trials to accurately copy any familiar behaviour, and no longer than 16 trials to copy any novel behaviour. This study provides experimental evidence for body imitation, including production imitation, in killer whales that is comparable to that observed in dolphins tested under similar conditions. These findings suggest that imitative learning may underpin some of the group-specific traditions reported in killer whales in the field.
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Connor, R. C., Mann, J., Tyack, P. L., & Whitehead, H. (1998). Social evolution in toothed whales. Trends. Ecol. Evol, 13(6), 228–232.
Abstract: Two contrasting results emerge from comparisons of the social systems of several odontocetes with terrestrial mammals. Researchers have identified remarkable convergence in prominent features of the social systems of odontocetes such as the sperm whale and bottlenose dolphin with a few well-known terrestrial mammals such as the elephant and chimpanzee. In contrast, studies on killer whales and Baird's beaked whale reveal novel social solutions to aquatic living. The combination of convergent and novel features in odontocete social systems promise a more general understanding of the ecological determinants of social systems in both terrestrial and aquatic habitats, as well as the relationship between relative brain size and social evolution.
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Connor, R. C., Wells, R. S., Mann, J., & Read, A. J. (2000). The bottlenose dolphin: Social relationships in a fission-fusion society. In J. Mann, R. C. Connor, P. L. Tyack, & H. Whitehead (Eds.), Cetacean Societies: Field Studies of Dolphins and Whales. (pp. 91–126). Chicago: University of Chicago Press.
Abstract: Book Description
“Part review, part testament to extraordinary dedication, and part call to get involved, Cetacean Societies highlights the achievements of behavioral ecologists inspired by the challenges of cetaceans and committed to the exploration of a new world.”-from the preface by Richard Wrangham Long-lived, slow to reproduce, and often hidden beneath the water's surface, whales and dolphins (cetaceans) have remained elusive subjects for scientific study even though they have fascinated humans for centuries. Until recently, much of what we knew about cetaceans came from commercial sources such as whalers and trainers for dolphin acts. Innovative research methods and persistent efforts, however, have begun to penetrate the depths to reveal tantalizing glimpses of the lives of these mammals in their natural habitats. Cetacean Societies presents the first comprehensive synthesis and review of these new studies. Groups of chapters focus on the history of cetacean behavioral research and methodology; state-of-the-art reviews of information on four of the most-studied species: bottlenose dolphins, killer whales, sperm whales, and humpback whales; and summaries of major topics, including group living, male and female reproductive strategies, communication, and conservation drawn from comparative research on a wide range of species. Written by some of the world's leading cetacean scientists, this landmark volume will benefit not just students of cetology but also researchers in other areas of behavioral and conservation ecology as well as anyone with a serious interest in the world of whales and dolphins. Contributors are Robin Baird, Phillip Clapham, Jenny Christal, Richard Connor, Janet Mann, Andrew Read, Randall Reeves, Amy Samuels, Peter Tyack, Linda Weilgart, Hal Whitehead, Randall S. Wells, and Richard Wrangham. |
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Gulotta, M., Rogatsky, E., Callender, R. H., & Dyer, R. B. (2003). Primary folding dynamics of sperm whale apomyoglobin: core formation. Biophys J, 84(3), 1909–1918.
Abstract: The structure, thermodynamics, and kinetics of heat-induced unfolding of sperm whale apomyoglobin core formation have been studied. The most rudimentary core is formed at pH(*) 3.0 and up to 60 mM NaCl. Steady state for ultraviolet circular dichroism and fluorescence melting studies indicate that the core in this acid-destabilized state consists of a heterogeneous composition of structures of approximately 26 residues, two-thirds of the number involved for horse heart apomyoglobin under these conditions. Fluorescence temperature-jump relaxation studies show that there is only one process involved in Trp burial. This occurs in 20 micro s for a 7 degrees jump to 52 degrees C, which is close to the limits placed by diffusion on folding reactions. However, infrared temperature jump studies monitoring native helix burial are biexponential with times of 5 micro s and 56 micro s for a similar temperature jump. Both fluorescence and infrared fast phases are energetically favorable but the slow infrared absorbance phase is highly temperature-dependent, indicating a substantial enthalpic barrier for this process. The kinetics are best understood by a multiple-pathway kinetics model. The rapid phases likely represent direct burial of one or both of the Trp residues and parts of the G- and H-helices. We attribute the slow phase to burial and subsequent rearrangement of a misformed core or to a collapse having a high energy barrier wherein both Trps are solvent-exposed.
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Haruta, N., & Kitagawa, T. (2002). Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin. Biochemistry, 41(21), 6595–6604.
Abstract: The 244-nm excited transient UV resonance Raman spectra are observed for the refolding intermediates of horse apomyoglobin (h-apoMb) with a newly constructed mixed flow cell system, and the results are interpreted on the basis of the spectra observed for the equilibrium acid unfolding of the same protein. The dead time of mixing, which was determined with the appearance of UV Raman bands of imidazolium upon mixing of imidazole with acid, was 150 micros under the flow rate that was adopted. The pH-jump experiments of h-apoMb from pH 2.2 to 5.6 conducted with this device demonstrated the presence of three folding intermediates. On the basis of the analysis of W3 and W7 bands of Trp7 and Trp14, the first intermediate, formed before 250 micros, involved incorporation of Trp14 into the alpha-helix from a random coil. The frequency shift of the W3 band of Trp14 observed for this process was reproduced with a model peptide of the A helix when it forms the alpha-helix. In the second intermediate, formed around 1 ms after the start of refolding, the surroundings of both Trp7 and Trp14 were significantly hydrophobic, suggesting the formation of the hydrophobic core. In the third intermediate appearing around 3 ms, the hydrophobicity was relaxed to the same level as that of the pH 4 equilibrium intermediate, which was investigated in detail with the stationary state technique. The change from the third intermediate to the native state needs more time than 40 ms, while the appearance of the native spectrum after the mixing of the same solutions was confirmed separately.
Keywords: Animals; Apoproteins/*chemistry; Circular Dichroism; Holoenzymes/chemistry; Horses; Hydrochloric Acid/chemistry; Hydrogen-Ion Concentration; Imidazoles/chemistry; Kinetics; Models, Molecular; Myoglobin/*chemistry; Peptide Fragments/chemistry; *Protein Folding; Protein Structure, Secondary; Spectrum Analysis, Raman/*methods; Tryptophan/*chemistry; Ultraviolet Rays; Whales
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Mercado, E. 3rd, Herman, L. M., & Pack, A. A. (2005). Song copying by humpback whales: themes and variations. Anim. Cogn., 8(2), 93–102.
Abstract: Male humpback whales (Megaptera novaeangliae) produce long, structured sequences of sound underwater, commonly called “songs.” Humpbacks progressively modify their songs over time in ways that suggest that individuals are copying song elements that they hear being used by other singers. Little is known about the factors that determine how whales learn from their auditory experiences. Song learning in birds is better understood and appears to be constrained by stable core attributes such as species-specific sound repertoires and song syntax. To clarify whether similar constraints exist for song learning by humpbacks, we analyzed changes over 14 years in the sounds used by humpback whales singing in Hawaiian waters. We found that although the properties of individual sounds within songs are quite variable over time, the overall distribution of certain acoustic features within the repertoire appears to be stable. In particular, our findings suggest that species-specific constraints on temporal features of song sounds determine song form, whereas spectral variability allows whales to flexibly adapt song elements.
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