Records |
Author |
Steinhoff, H.J.; Schrader, J.; Schlitter, J. |
Title |
Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals |
Type |
Journal Article |
Year |
1992 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
Volume |
1121 |
Issue |
3 |
Pages |
269-278 |
Keywords |
Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry |
Abstract |
Association equilibria and association kinetics of the thiocyanate binding reaction to methemoglobin in single crystals and solution are studied using temperature-jump technique and polarized absorption spectroscopy. Different kinetic constants are found for the reaction in solution and crystal phase for the alpha- and beta-subunits of the methemoglobin tetramer. The reduction of the reactivity of the alpha- and beta-subunits in crystalline phase is 6-fold and 2.4-fold, respectively, compared to the values found in solution. The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals. Our results suggest that crystallization of hemoglobin has little influence on small-scale structural fluctuations which are necessary for ligands to get to the binding sites and large-scale structural motions are suppressed. |
Address |
Institut fur Biophysik, Ruhr-Universitat Bochum, Germany |
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English |
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ISSN |
0006-3002 |
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PMID:1627604 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3800 |
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Author |
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. |
Title |
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods |
Type |
Journal Article |
Year |
1994 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
Volume |
19 |
Issue |
2 |
Pages |
110-119 |
Keywords |
Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea |
Abstract |
The refolding kinetics of horse cyanometmyoglobin induced by concentration jump of urea was investigated by five optical probe stopped-flow methods: absorption at 422 nm, tryptophyl fluorescence at around 340 nm, circular dichroism (CD) at 222 nm, CD at 260 nm, and CD at 422 nm. In the refolding process, we detected three phases with rate constants of > 1 x 10(2) s-1, (4.5-9.3) s-1, and (2-5) x 10(-3) s-1. In the fastest phase, a substantial amount of secondary structure (approximately 40%) is formed within the dead time of the CD stopped-flow apparatus (10.7 ms). The kinetic intermediate populated in the fastest phase is shown to capture a hemindicyanide, suggesting that a “heme pocket precursor” recognized by hemindicyanide must be constructed within the dead time. In the middle phase, most of secondary and tertiary structures, especially around the captured hemindicyanide, have been constructed. In the slowest phase, we detected a minor structural rearrangement accompanying the ligand-exchange reaction in the fifth coordination of ferric iron. We present a possible model for the refolding process of myoglobin in the presence of the heme group. |
Address |
Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan |
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ISSN |
0887-3585 |
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Notes |
PMID:8090705 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3799 |
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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 |
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English |
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ISSN |
0027-8424 |
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Notes |
PMID:8650166 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3798 |
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Author |
Galloux, P.; Barrey, E. |
Title |
Components of the total kinetic moment in jumping horses |
Type |
Journal Article |
Year |
1997 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
Volume |
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Issue |
23 |
Pages |
41-44 |
Keywords |
Algorithms; Animals; Exertion/*physiology; Female; Gravitation; Horses/*physiology; Kinetics; Locomotion/*physiology; Male; Models, Biological; Movement/*physiology; Video Recording |
Abstract |
Thirty horses were filmed with a panning camera operating at 50 frames/s as they jumped over a 1.20 x 1.20 m fence. The markers of 9 joints on the horse and 7 joints on the rider were tracked in 2D with the TrackEye system. The centre of gravity and moment of inertia of each segment were calculated using a geometric algorithm and a cylindric model, respectively. The kinetic moment of each part of the horse was calculated after filtering, and resampling of data. This method showed the relative contribution of each body segment to the body overall rotation during the take-off, jump and landing phases. It was found that the trunk, hindlimbs and head-neck had the greatest influence. The coordination between the motion of the body segments allowed the horse to control its angular speed of rotation over the fence. This remained nearly constant during the airborne phase (120 +/- 5 degrees/s). During the airborne phase, the kinetic moment was constant because its value was equal to the moment of the external forces (722 +/- 125 kg x m2/s). |
Address |
Ecole Nationale d'Equitation, Terrefort, Saumur, France |
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English |
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Notes |
PMID:9354287 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3797 |
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Author |
Barrey, E.; Galloux, P. |
Title |
Analysis of the equine jumping technique by accelerometry |
Type |
Journal Article |
Year |
1997 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
Volume |
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Issue |
23 |
Pages |
45-49 |
Keywords |
*Acceleration; Analysis of Variance; Animals; Forelimb/physiology; Hindlimb/physiology; Horses/*physiology; Locomotion/*physiology; Movement/physiology; Time Factors |
Abstract |
The purpose of this study was to demonstrate the relationships between jumping technique and dorsoventral acceleration measured at the sternum. Eight saddle horses of various jumping abilities competed on a selective experimental show jumping course including 14 obstacles. An accelerometric belt fastened onto the thorax continuously measured the dorsoventral acceleration during the course. At each jump, 11 locomotor parameters (acceleration peaks, durations and stride frequency) were obtained from the dorsoventral acceleration-time curves. The type of obstacle significantly influenced the hindlimb acceleration peak at take-off and the landing acceleration peak (P<0.01). The poor jumpers exhibited a higher mean forelimb acceleration peak at take-off, a higher forelimb/hindlimb ratio between peaks of acceleration (F/H), and a lower approach stride frequency than good jumpers. Knocking over an obstacle was significantly associated with a low hindlimb acceleration peak at take-off and a high F/H ratio (P<0.01). In order to observe the continuous changes in the frequency domain of the dorsoventral acceleration during the approach and take-off phase, a Morlet's wavelet analysis was computed for each horse jumping over a series of 3 vertical obstacles. Different patterns of time-frequency images obtained by wavelet analysis were found when the horse either knocked over a vertical obstacle or cleared it. In the latter case, the image pattern showed an instantaneous increase in stride frequency at the end of the approach phase, and a marked energy content in the middle frequency range at take-off. |
Address |
INRA Station de Genetique Quantitative et Appliquee, Groupe cheval, Jouy-en-Josas, France |
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English |
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Notes |
PMID:9354288 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3796 |
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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. |
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English |
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ISSN |
1072-8368 |
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Notes |
PMID:9586997 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3795 |
Permanent link to this record |
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Author |
Birch, H.L.; Bailey, A.J.; Goodship, A.E. |
Title |
Macroscopic 'degeneration' of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition |
Type |
Journal Article |
Year |
1998 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
Volume |
30 |
Issue |
6 |
Pages |
534-539 |
Keywords |
Animals; Collagen/analysis; DNA/analysis; Extracellular Matrix/*chemistry; Glycosaminoglycans/analysis; Horses/injuries/*physiology; Immunohistochemistry; Rupture/veterinary; Tendon Injuries/metabolism/pathology/veterinary; Tendons/chemistry/*pathology; Water/analysis |
Abstract |
Injuries to the superficial digital flexor tendon are common in horses required to gallop and jump at speed. Partial rupture of this tendon usually occurs in the central core of the midmetacarpal region and may be preceded by localised degenerative changes. Post mortem examination of apparently normal equine flexor tendons has revealed an abnormal macroscopic appearance in the central core, characterised by a reddish discolouration. We have previously shown that there is also physical damage to the collagen fibres. In the present study we tested the hypothesis that the abnormal appearance is accompanied by changes in the composition of the extracellular matrix of the tendon. Biochemical analysis of the extracellular matrix demonstrated an increase in total sulphated glycosaminoglycan content, increase in the proportion of type III collagen and decrease in collagen linked fluorescence in the central core of 'degenerated' tendons relative to tissue from the peripheral region of the same tendon. Dry matter content and total collagen content were not significantly different between tendon zones or normal and 'degenerated' tendons. These changes suggest a change in cell metabolism and matrix turnover in the central core of the tendon and are likely to contribute to a decrease in mechanical properties in this part of the tendon, predisposing to the characteristic partial rupture of the tendon. |
Address |
Veterinary Basic Sciences, Royal Veterinary College, North Mymms, Hatfield, UK |
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English |
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ISSN |
0425-1644 |
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Notes |
PMID:9844973 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3794 |
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Author |
Grandin, T. |
Title |
Safe handling of large animals |
Type |
Journal Article |
Year |
1999 |
Publication |
Occupational Medicine (Philadelphia, Pa.) |
Abbreviated Journal |
Occup Med |
Volume |
14 |
Issue |
2 |
Pages |
195-212 |
Keywords |
Accidents, Occupational/*prevention & control/statistics & numerical data; Aggression/physiology/psychology; Animal Husbandry/*methods; Animals; *Behavior, Animal/physiology; Cattle; Conditioning, Operant/physiology; Crowding/psychology; Fear/physiology/psychology; Female; *Horses/physiology/psychology; Humans; Male; Movement/physiology; *Occupational Health; Risk Factors; *Ruminants/physiology/psychology |
Abstract |
The major causes of accidents with cattle, horses, and other grazing animals are: panic due to fear, male dominance aggression, or the maternal aggression of a mother protecting her newborn. Danger is inherent when handling large animals. Understanding their behavior patterns improves safety, but working with animals will never be completely safe. Calm, quiet handling and non-slip flooring are beneficial. Rough handling and excessive use of electric prods increase chances of injury to both people and animals, because fearful animals may jump, kick, or rear. Training animals to voluntarily cooperate with veterinary procedures reduces stress and improves safety. Grazing animals have a herd instinct, and a lone, isolated animal can become agitated. Providing a companion animal helps keep an animal calm. |
Address |
Department of Animal Science, Colorado State University, Fort Collins 80526, USA |
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English |
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ISSN |
0885-114X |
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PMID:10329901 |
Approved |
no |
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Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3793 |
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Author |
Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
Title |
Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump |
Type |
Journal Article |
Year |
2000 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
Volume |
78 |
Issue |
1 |
Pages |
405-415 |
Keywords |
Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence |
Abstract |
Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation. |
Address |
Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia |
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English |
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ISSN |
0006-3495 |
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Notes |
PMID:10620304 |
Approved |
no |
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Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3792 |
Permanent link to this record |
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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 |
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English |
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ISSN |
0022-2836 |
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PMID:10966803 |
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no |
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Equine Behaviour @ team @ |
Serial ![sorted by Serial field, descending order (down)](img/sort_desc.gif) |
3790 |
Permanent link to this record |