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Author |
Christensen, J.W.; Søndergaard, E.; Thodberg, K.; Halekoh, U. |
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Title |
Effects of repeated regrouping on horse behaviour and injuries |
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Journal Article |
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Year |
2011 |
Publication |
Applied Animal Behaviour Science |
Abbreviated Journal |
Appl. Anim. Behav. Sci. |
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Volume |
133 |
Issue |
3 |
Pages |
199-206 |
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Keywords |
Group housing; Horse; Injuries; Regrouping; Social behaviour |
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Domestic horses are faced with social challenges throughout their lives due to limitations in social contact, space restrictions and frequent changes in social companionship. This is in contrast to natural conditions where horses live in relatively stable harem bands. Currently, little is known about how repeated regrouping affect horse behaviour and welfare, and it is unknown whether horses may adapt to regrouping. In this study, we aimed to investigate the effects of an unstable group structure, caused by weekly regroupings, on behaviour and frequency of injuries in young horses. Forty-five horses were included in the study and were randomly assigned to the treatments; Stable (S; seven groups of three horses) or Unstable (U; eight groups of three horses). The experimental period lasted 7 weeks, during which horses in Stable groups remained in the same group, whereas one horse was exchanged between Unstable groups every week. The groups were kept in 80m×80m grass-covered enclosures and were fed additional roughage on the ground daily. Social interactions were recorded in Unstable groups immediately after each regrouping (30min), and in both Stable and Unstable groups on day 1, 3 and 6 after each regrouping (2×20min/group/day). Injuries were scored by the end of the experimental period. The level of aggression shown by horses in Unstable groups immediately after regrouping was not affected by week (F5,35=0.42, P=0.83), indicating that horses neither habituated, nor sensitized, to repeated regrouping. Compared to horses in Stable groups, more agonistic behaviour was shown by horses in Unstable groups (i.e. non-contact agonistic; F1,65=5.60, P=0.02), whereas there was no treatment effect on other variables. The level of play behaviour appeared, however, to be more variable in Unstable groups. There was a significant effect of week on the level of contact agonistic interactions as well as greeting behaviour, due to a high occurrence in weeks 4-6. Non-contact agonistic interactions constituted the major part of agonistic interactions (66%). Possibly as consequence, no serious injuries were registered and there was no treatment effect (U=184; P=0.11). We conclude that the behaviour of young horses is affected by group management, and that horses appear not to adapt to weekly regroupings. |
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0168-1591 |
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Equine Behaviour @ team @ |
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6605 |
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Suagee-Bedore, J.K.; Linden, D.R.; Bennett-Wimbush, K. |
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Title |
Effect of Pen Size on Stress Responses of Stall-Housed Horses Receiving One Hour of Daily Turnout |
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Journal Article |
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Year |
2021 |
Publication |
Journal of Equine Veterinary Science |
Abbreviated Journal |
J. Equine Vet. Sci. |
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98 |
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103366 |
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Agonistic behaviors; Cortisol; Group turnout; Paddock sizes |
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Group turnout provides important socializing opportunities for horses, particularly those that are primarily stalled. A high percentage of equine injuries occur during group turnout, which could partly be due to the physical constraints of fencing. To investigate appropriate paddock sizes for group turnouts, horses (n = 12) from a single herd were divided into groups of 4, stalled for 24 hours, and then turned out for 1 hour into one of three differently sized pens: 342, 263, and 184 m2 per horse. Groups rotated through pens across 3 days, receiving one treatment per day. Blood was sampled for cortisol concentrations at 08:00 hours each morning, and then at 15 and 60 minutes into the turn out sessions, and 60 minutes after return to individual stalls. Groups rotated through three turnout times: 09:00, 12:00, 14:00 hours. Counts of agonistic behaviors (chasing, contact biting, and kicking) and low-level threats (pinned ears, tail swishing, bite and kick threats) were recorded. When turned out in pens that provided 342 m2 per horse, horses exhibited reduced plasma cortisol concentrations by 15 minutes after turnout and at 1 hour after return to their stalls (P < .05). Horses in pens providing 184 m2 per horse exhibited greater agonistic (P < .001) and low-level threat (P < .01) behaviors than horses in larger pens. These data provide insight into appropriate pen sizes for horses from established herds. Providing at least 342 m2 per horse may reduce the chance of injury in horses accustomed to group turnout. |
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0737-0806 |
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Equine Behaviour @ team @ |
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6694 |
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Anderson, C.; Franks, N.R. |
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Title |
Teams in animal societies |
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Journal Article |
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Year |
2001 |
Publication |
Behavioral Ecology |
Abbreviated Journal |
Behav. Ecol. |
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12 |
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5 |
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534-540 |
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animal societies, cooperation, division of labor, groups, invertebrates, task types, teams, vertebrates |
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We review the existence of teams in animal societies. Teams have previously been dismissed in all but a tiny minority of insect societies. “Team” is a term not generally used in studies of vertebrates. We propose a new rigorous definition of a team that may be applied to both vertebrate and invertebrate societies. We reconsider what it means to work as a team or group and suggest that there are many more teams in insect societies than previously thought. A team task requires different subtasks to be performed concurrently for successful completion. There is a division of labor within a team. Contrary to previous reviews of teams in social insects, we do not constrain teams to consist of members of different castes and argue that team members may be interchangeable. Consequently, we suggest that a team is simply the set of individuals that performs a team task. We contrast teams with groups and suggest that a group task requires the simultaneous performance and cooperation of two or more individuals for successful completion. In a group, there is no division of labor--each individual performs the same task. We also contrast vertebrate and invertebrate teams and find that vertebrate teams tend to be associated with hunting and are based on individual recognition. Invertebrate teams occur in societies characterized by a great deal of redundancy, and we predict that teams in insect societies are more likely to be found in large polymorphic (“complex”) societies than in small monomorphic (“simple”) societies. |
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10.1093/beheco/12.5.534 |
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2070 |
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Shrader, A.M.; Kerley, G.I.H.; Kotler, B.P.; Brown, J.S. |
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Title |
Social information, social feding, and competition in group-living goats (Capra hircus) |
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Journal Article |
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Year |
2007 |
Publication |
Behavioral Ecology |
Abbreviated Journal |
Behav. Ecol. |
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18 |
Issue |
1 |
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103-107 |
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fear, group foraging, harvest rates, intraspecific competition, social information. |
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There are both benefits (e.g., social information) and costs (e.g., intraspecific competition) for individuals foraging in groups. To ascertain how group-foraging goats (Capra hircus) deal with these trade-offs, we asked 1) do goats use social information to make foraging decisions and 2) how do they adjust their intake rate in light of having attracted by other group members? To establish whether goats use social information, we recorded their initial choice of different quality food patches when they were ignorant of patch quality and when they could observe others foraging. After determining that goats use social information, we recorded intake rates while they fed alone and in the presence of potential competitors. Intake rate increased as the number of competitors increased. Interestingly, lone goats achieved an intake rate that was higher than when one competitor was present but similar to when two or more competitors were present. Faster intake rates may allow herbivores to ingest a larger portion of the available food before competing group members arrive at the patch. This however, does not explain the high intake rates achieved when the goats were alone. We provide 2 potential explanations: 1) faster intake rates are a response to greater risk incurred by lone individuals, the loss of social information, and the fear of being left behind by the group and 2) when foraging alone, intake rate is no longer a trade-off between reducing competition and acquiring social information. Thus, individuals are able to feed close to their maximum rate. |
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10.1093/beheco/arl057 |
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refbase @ user @ |
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814 |
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Author |
Pierce, M.M.; Nall, B.T. |
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Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
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Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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298 |
Issue |
5 |
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955-969 |
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Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/*chemistry/genetics/*metabolism; *Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/*metabolism; Histidine/genetics/*metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/*chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics |
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The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand. |
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Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA |
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0022-2836 |
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PMID:10801361 |
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refbase @ user @ |
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3853 |
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Hagen, S.J.; Eaton, W.A. |
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Two-state expansion and collapse of a polypeptide |
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Journal Article |
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2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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301 |
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4 |
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1019-1027 |
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Animals; Computer Simulation; Cytochrome c Group/*chemistry/*metabolism; Horses; Kinetics; Lasers; Models, Chemical; Peptides/*chemistry/*metabolism; Protein Conformation; Protein Denaturation; *Protein Folding; Spectrometry, Fluorescence; Temperature; Thermodynamics |
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The initial phase of folding for many proteins is presumed to be the collapse of the polypeptide chain from expanded to compact, but still denatured, conformations. Theory and simulations suggest that this collapse may be a two-state transition, characterized by barrier-crossing kinetics, while the collapse of homopolymers is continuous and multi-phasic. We have used a laser temperature-jump with fluorescence spectroscopy to measure the complete time-course of the collapse of denatured cytochrome c with nanosecond time resolution. We find the process to be exponential in time and thermally activated, with an apparent activation energy approximately 9 k(B)T (after correction for solvent viscosity). These results indicate that polypeptide collapse is kinetically a two-state transition. Because of the observed free energy barrier, the time scale of polypeptide collapse is dramatically slower than is predicted by Langevin models for homopolymer collapse. |
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Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Building 5, Bethesda, MD, 20892-0520, USA |
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0022-2836 |
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PMID:10966803 |
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Equine Behaviour @ team @ |
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3790 |
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Author |
Morton, D.B. |
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Self-consciousness and animal suffering |
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Journal Article |
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2000 |
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Biologist (London, England) |
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Biologist (London) |
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47 |
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2 |
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77-80 |
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Animal Population Groups/*psychology; Animal Welfare/*standards; Animals; Behavior, Animal; *Consciousness; Dogs; *Ego; Horses/psychology; Pain/psychology/*veterinary; Pan troglodytes/psychology; Parrots; Pongo pygmaeus/psychology; Self Concept |
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Animals with relatively highly developed brains are likely to experience some degree of self-awareness and the ability to think. As well as being interesting in its own right, self-consciousness matters from an ethical point of view, since it can give rise to forms of suffering above and beyond the immediate physical sensations of pain or distress. This article surveys the evidence for animal self-consciousness and its implications for animal welfare. |
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Division of Primary Care, Public and Occupational Health, School of Medicine, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. d.b.morton@bham.ac.uk |
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0006-3347 |
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PMID:11190233 |
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refbase @ user @ |
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618 |
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Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
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Journal Article |
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2001 |
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Journal of the American Chemical Society |
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J Am Chem Soc |
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123 |
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27 |
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6649-6653 |
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Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
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We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding. |
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Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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0002-7863 |
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PMID:11439052 |
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Equine Behaviour @ team @ |
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3788 |
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Author |
Conradt, L.; Roper, T.J. |
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Group decision-making in animals |
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Journal Article |
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2003 |
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Nature |
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Nature |
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421 |
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6919 |
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155-158 |
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Animals; Behavior, Animal/*physiology; *Decision Making; Democracy; Group Processes; *Models, Biological; Population Density; Social Behavior |
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Groups of animals often need to make communal decisions, for example about which activities to perform, when to perform them and which direction to travel in; however, little is known about how they do so. Here, we model the fitness consequences of two possible decision-making mechanisms: 'despotism' and 'democracy'. We show that under most conditions, the costs to subordinate group members, and to the group as a whole, are considerably higher for despotic than for democratic decisions. Even when the despot is the most experienced group member, it only pays other members to accept its decision when group size is small and the difference in information is large. Democratic decisions are more beneficial primarily because they tend to produce less extreme decisions, rather than because each individual has an influence on the decision per se. Our model suggests that democracy should be widespread and makes quantitative, testable predictions about group decision-making in non-humans. |
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School of Biological Sciences, University of Sussex, Brighton BN1 9QG, UK. l.conradt@sussex.ac.uk |
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0028-0836 |
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PMID:12520299 |
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Equine Behaviour @ team @ |
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5136 |
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Author |
Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. |
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Title |
Folding units govern the cytochrome c alkaline transition |
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Journal Article |
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Year |
2003 |
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Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
331 |
Issue |
1 |
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37-43 |
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Animals; Cytochrome c Group/*chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; *Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry |
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The alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways. |
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Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu |
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0022-2836 |
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PMID:12875834 |
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Equine Behaviour @ team @ |
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3781 |
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