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Author Hrdy, S.B.
Title Male-male competition and infanticide among the langurs (Presbytis entellus) of Abu, Rajasthan Type Journal Article
Year 1974 Publication Folia Primatologica; International Journal of Primatology Abbreviated Journal Folia Primatol (Basel)
Volume 22 Issue 1 Pages 19-58
Keywords Aggression; Animals; Animals, Newborn; Coitus; *Competitive Behavior; Estrus; Feeding Behavior; Female; *Haplorhini; Homing Behavior; Humans; India; Infanticide; Leadership; Male; Maternal Behavior; Population Density; Pregnancy; Rain; Seasons; Sex Factors; Sexual Behavior, Animal; Social Behavior; Temperature; Vocalization, Animal
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0015-5713 ISBN Medium
Area Expedition Conference
Notes PMID:4215710 Approved no
Call Number Serial 2051
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Author Hughes, K.L.; Sulaiman, I.
Title The ecology of Rhodococcus equi and physicochemical influences on growth Type Journal Article
Year 1987 Publication Veterinary Microbiology Abbreviated Journal Vet Microbiol
Volume 14 Issue 3 Pages 241-250
Keywords Animals; Feces/microbiology; Horses; Hydrogen-Ion Concentration; Rhodococcus/*growth & development; *Soil Microbiology; Temperature
Abstract Growth of Rhodococcus equi was studied in vitro. Optimal growth occurred under aerobic conditions between pH 7.0 and 8.5, at 30 degrees C. R. equi survived better in a neutral soil (pH 7.3) than it did in two acid soils (pH less than 5.5). It grew substantially better in soils enriched with faeces than in soils alone. Simple organic acids in horse dung, especially acetate and propionate, appear to be important in supporting growth of R. equi in the environment. The ecology of R. equi can be best explained by an environmental cycle allowing its proliferation in dung, influenced by management, grazing behaviour and prevailing climatic conditions. Preventive measures should be aimed at reducing or avoiding focal areas of faecal contamination in the environment.
Address School of Veterinary Science, University of Melbourne, Parkville, Vic., Australia
Corporate Author Thesis (up)
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Language English Summary Language Original Title
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ISSN 0378-1135 ISBN Medium
Area Expedition Conference
Notes PMID:3672866 Approved no
Call Number Equine Behaviour @ team @ Serial 2678
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Author Chmel, L.; Hasilikova, A.; Hrasko, J.; Vlacilikova, A.
Title The influence of some ecological factors on keratinophilic fungi in the soil Type Journal Article
Year 1972 Publication Sabouraudia Abbreviated Journal Sabouraudia
Volume 10 Issue 1 Pages 26-34
Keywords Animals; Arthrodermataceae/growth & development/isolation & purification/metabolism; Carbohydrates; Czechoslovakia; Ecology; Fungi/growth & development/*isolation & purification/metabolism; Hair; Horses; Humic Substances; Humidity; Keratins/metabolism; Microsporum/isolation & purification; Mitosporic Fungi/isolation & purification; Phosphates; Seasons; Soil; *Soil Microbiology; Species Specificity; Temperature; Trichophyton/isolation & purification
Abstract
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Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0036-2174 ISBN Medium
Area Expedition Conference
Notes PMID:5063162 Approved no
Call Number Equine Behaviour @ team @ Serial 2719
Permanent link to this record
 
 
Author Duncan, I.J.H.; Widowski, T.M.; Malleau, A.E.; Lindberg, A.C.; Petherick, J.C.
Title External factors and causation of dustbathing in domestic hens Type Journal Article
Year 1998 Publication Behavioural Processes Abbreviated Journal Behav. Process.
Volume 43 Issue 2 Pages 219-228
Keywords Dustbathing; Illumination; Laying hens; Radiant heat; Social facilitation; Temperature
Abstract Dustbathing is known to be motivated by complex interactions between internal factors which build up over time and external factors, such as the sight of a dusty substrate. In this study, the effects of other external factors were investigated. Environmental temperature was shown to be important; frequencies of dustbathing were greater when hens were held at 22 than at 10[degree sign]C (P<0.01). In a second experiment, a radiant heat source or a radiant heat+light source, balanced to give the same radiant heat, resulted in more dustbathing behaviour during a 1-h stimulus period than during the same period with no stimulus (P<0.05). Components of dustbathing were increased more by the heat+light stimulus than by the heat stimulus alone (P<0.03). In a third experiment, the amount of dustbathing performed by individual hens in cages with dustbaths was increased by the presence of a group of hens dustbathing in an adjoining pen with a dustbath compared with the amount occurring when the hens were absent from the pen.
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ISSN ISBN Medium
Area Expedition Conference
Notes Approved no
Call Number Equine Behaviour @ team @ Serial 3607
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Author Balakrishnan, G.; Hu, Y.; Spiro, T.G.
Title Temperature-jump apparatus with Raman detection based on a solid-state tunable (1.80-2.05 microm) kHz optical parametric oscillator laser Type Journal Article
Year 2006 Publication Applied Spectroscopy Abbreviated Journal Appl Spectrosc
Volume 60 Issue 4 Pages 347-351
Keywords Animals; Cytochromes c/analysis; Horses; Lasers; Myoglobin/metabolism; Spectrum Analysis, Raman/*instrumentation/*methods; *Temperature
Abstract The operating characteristics of a pulsed (10 ns) tunable near-infrared (NIR) laser source are described for temperature-jump (T-jump) applications. A Q-switched Nd:YLF laser (approximately 10 ns pulses) with a 1 kHz repetition rate is used to pump a potassium titanyl arsenate (KTA) crystal-based optical parametric oscillator (OPO), producing approximately 1 mJ NIR pulses that are tunable (1.80-2.05 microm) across the 1.9 microm vibrational overtone band of water. This T-jump source has been coupled to a deep ultraviolet (UV) probe laser for Raman studies of protein dynamics. T-jumps of up to 30 degrees C, as measured via the O-H stretching Raman band of water, are readily achieved. Application to cytochrome c unfolding is demonstrated.
Address Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA
Corporate Author Thesis (up)
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0003-7028 ISBN Medium
Area Expedition Conference
Notes PMID:16613628 Approved no
Call Number Equine Behaviour @ team @ Serial 3764
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Author Miksovska, J.; Larsen, R.W.
Title Photothermal studies of pH induced unfolding of apomyoglobin Type Journal Article
Year 2003 Publication Journal of Protein Chemistry Abbreviated Journal J Protein Chem
Volume 22 Issue 4 Pages 387-394
Keywords Acoustics; Animals; Apoproteins/*chemistry/metabolism; Circular Dichroism; Horses; Myocardium/chemistry; Myoglobin/*chemistry/metabolism; Photolysis; Protein Conformation/radiation effects; Protein Denaturation/radiation effects; *Protein Folding; Temperature; Thermodynamics
Abstract Conformational dynamic and enthalpy changes associated with pH induced unfolding of apomyoglobin were studied using photoacoustic calorimetry and photothermal beam deflection methods. The transition between the native state and the I intermediate was induced by a nanosecond pH jump from o-nitrobenzaldehyde photolysis. Deconvolution of photoacoustic waves indicates two kinetic processes. The fast phase (T < 50 ns) is characterized by a volume expansion of 8.8 ml mol(-1). This process is followed by a volume contraction of about -22 ml mol(-1) (tau approximately 500 ns). Photothermal beam deflection measurements do not reveal any volume changes on the time scale between approximately 100 micros and 5 ms. We associate the volume contraction with structural changes occurring during the transition between the native state and the I intermediate. The lack of any processes on the ms time scale may indicate the absence of structural events involving larger conformational changes of apomyoglobin after the pH jump.
Address Department of Chemistry, University of South Florida, Tampa, Florida 33620, USA
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Language English Summary Language Original Title
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ISSN 0277-8033 ISBN Medium
Area Expedition Conference
Notes PMID:13678303 Approved no
Call Number Equine Behaviour @ team @ Serial 3780
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Author Gulotta, M.; Rogatsky, E.; Callender, R.H.; Dyer, R.B.
Title Primary folding dynamics of sperm whale apomyoglobin: core formation Type Journal Article
Year 2003 Publication Biophysical Journal Abbreviated Journal Biophys J
Volume 84 Issue 3 Pages 1909-1918
Keywords Animals; Apoproteins/*chemistry; Crystallography/*methods; Horses; Myocardium/chemistry; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Species Specificity; Structure-Activity Relationship; Temperature; Whales
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.
Address Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA. gulotta@aecom.yu.edu
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ISSN 0006-3495 ISBN Medium
Area Expedition Conference
Notes PMID:12609893 Approved no
Call Number Equine Behaviour @ team @ Serial 3783
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Author Hagen, S.J.; Eaton, W.A.
Title Two-state expansion and collapse of a polypeptide Type Journal Article
Year 2000 Publication Journal of Molecular Biology Abbreviated Journal J Mol Biol
Volume 301 Issue 4 Pages 1019-1027
Keywords 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
Abstract 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.
Address Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Building 5, Bethesda, MD, 20892-0520, USA
Corporate Author Thesis (up)
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0022-2836 ISBN Medium
Area Expedition Conference
Notes PMID:10966803 Approved no
Call Number Equine Behaviour @ team @ Serial 3790
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Author Gilmanshin, R.; Callender, R.H.; Dyer, R.B.
Title The core of apomyoglobin E-form folds at the diffusion limit Type Journal Article
Year 1998 Publication Nature Structural Biology Abbreviated Journal Nat Struct Biol
Volume 5 Issue 5 Pages 363-365
Keywords Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature
Abstract The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation.
Address
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Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 1072-8368 ISBN Medium
Area Expedition Conference
Notes PMID:9586997 Approved no
Call Number Equine Behaviour @ team @ Serial 3795
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Author Ballew, R.M.; Sabelko, J.; Gruebele, M.
Title Direct observation of fast protein folding: the initial collapse of apomyoglobin Type Journal Article
Year 1996 Publication Proceedings of the National Academy of Sciences of the United States of America Abbreviated Journal Proc. Natl. Acad. Sci. U.S.A.
Volume 93 Issue 12 Pages 5759-5764
Keywords Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature
Abstract The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state are observed and are complete in under 20 micros. Experiments on mutants and consideration of steady-state CD and fluorescence spectra indicate that the observed microsecond phase monitors assembly of an A x (H x G) helix subunit. Measurements at different viscosities indicate diffusive behavior even at low viscosities, in agreement with motions of a solvent-exposed protein during the initial collapse.
Address School of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, 61801, USA
Corporate Author Thesis (up)
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0027-8424 ISBN Medium
Area Expedition Conference
Notes PMID:8650166 Approved no
Call Number Equine Behaviour @ team @ Serial 3798
Permanent link to this record