| Records |
| Author |
Santamaria, S.; Back, W.; van Weeren, P.R.; Knaap, J.; Barneveld, A. |
| Title |
Jumping characteristics of naive foals: lead changes and description of temporal and linear parameters |
Type |
Journal Article |
| Year |
2002 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
| Volume |
|
Issue |
34 |
Pages |
302-307 |
| Keywords |
Animals; Animals, Newborn/*physiology; Biomechanics; Female; Forelimb/physiology; Gait/*physiology; Hindlimb/physiology; Horses/*physiology; Locomotion/*physiology; Male |
| Abstract |
The selection of foals as future showjumpers remains a subjective process based on qualitative parameters; and hence, frequently suffers from disparity in the criteria used by experts in the field. A detailed biomechanical description of foals while jumping would be most helpful in providing a better basis for the accurate assessment of their future athletic ability. The Qualisys Pro Reflex system was used to capture 3-dimensional kinematics of 41 Dutch Warmblood foals age 6 months free jumping a vertical fence, preceded by a cross pole fence. The left lead was the most preferred lead for both the fore- and hindlimbs, from the landing following the cross poles to the first move-off stride after clearing the vertical fence. The foals displayed a high incidence of rotary gallop during both the jump stride (divided into take-off, jump suspension and landing) and the first move-off stride, while change of lead was frequently observed during jump suspension. At the take-off side of the fence, the trailing forelimb in the last approach stride was placed furthest from the fence, whereas the trailing hindlimb at take-off was placed closest (P<0.05). At the landing side, the trailing forelimb was the closest and the leading hindlimb of the move-off stride 1 was the furthest (P<0.05). The trailing forelimb in the approach stride 1 had a significantly longer stance phase duration than the leading forelimb. At landing, the leading forelimb stance phase lasted longer than that of the trailing forelimb (P<0.05). The hindlimbs did not differ in their stance phase duration at take-off. The height reached by the hooves above the fence top was significantly greater in the hind limbs (P<0.05). In addition, the hindlimbs (97.1 +/- 2.6%) shortened more than the forelimbs (92.6 +/- 5.7%) (P<0.05). It is concluded that the overall jumping technique of foals is similar to that reported in literature for mature horses. If the patterns are consistent throughout the rearing period, the quantitative analysis of the kinematics of free jumping foals may provide a valid quantitative basis for early selection. |
| Address |
Department of Equine Sciences, Faculty of Veterinary Medicine, Utrecht, The Netherlands |
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English |
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| Notes |
PMID:12405705 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3784 |
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| Author |
Haruta, N.; Kitagawa, T. |
| Title |
Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin |
Type |
Journal Article |
| Year |
2002 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
| Volume |
41 |
Issue |
21 |
Pages |
6595-6604 |
| 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 |
| 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. |
| Address |
School of Mathematical and Physical Sciences, The Graduate University for Advanced Studies, Myodaiji, Okazaki 444-8585, Japan |
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English |
Summary Language |
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Edition |
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0006-2960 |
ISBN |
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Conference |
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| Notes |
PMID:12022863 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3785 |
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| Author |
Meershoek, L.S.; Schamhardt, H.C.; Roepstorff, L.; Johnston, C. |
| Title |
Forelimb tendon loading during jump landings and the influence of fence height |
Type |
Journal Article |
| Year |
2001 |
Publication |
Equine Veterinary Journal. Supplement |
Abbreviated Journal |
Equine Vet J Suppl |
| Volume |
|
Issue |
33 |
Pages |
6-10 |
| Keywords |
Animals; Biomechanics; Forelimb/injuries/physiology; Horses/injuries/*physiology; Lameness, Animal/etiology; Ligaments, Articular/*physiology; Locomotion/*physiology; Physical Conditioning, Animal; Tendon Injuries/complications/physiopathology/veterinary; Tendons/*physiology; Weight-Bearing/physiology |
| Abstract |
Lameness in athletic horses is often caused by forelimb tendon injuries, especially in the interosseus tendon (TI) and superficial digital flexor tendon (SDF), but also in the accessory ligament (AL) of the deep digital flexor tendon (DDF). In an attempt to explain the aetiology of these injuries, the present study investigated the loading of the tendons during landing after a jump. In jumping horses, the highest forces can be expected in the trailing limb during landing. Therefore, landing kinematics and ground reaction forces of the trailing forelimb were measured from 6 horses jumping single fences with low to medium heights of 0.80, 1.00 and 1.20 m. The tendon forces were calculated using inverse dynamics and an in vitro model of the lower forelimb. Calculated peak forces in the TI, SDF and DDF + AL during landing were 15.8, 13.9 and 11.7 kN respectively. The relative loading of the tendons (landing forces compared with failure forces determined in a separate study) increased from DDF to TI to SDF and was very high in SDF. This explains the low injury incidence of the DDF and the high injury incidence of the SDF. Fence height substantially influenced SDF forces, whereas it hardly influenced TI forces and did not influence AL strain. Reduction of fence height might therefore limit the risks for SDF injuries, but not for TI and AL injuries. |
| Address |
Department of Veterinary Anatomy and Physiology, Institute for Fundamental and Clinical Human Movement Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands |
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English |
Summary Language |
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Expedition |
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Conference |
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| Notes |
PMID:11721571 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3786 |
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| Author |
Meershoek, L.S.; Roepstorff, L.; Schamhardt, H.C.; Johnston, C.; Bobbert, M.F. |
| Title |
Joint moments in the distal forelimbs of jumping horses during landing |
Type |
Journal Article |
| Year |
2001 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
| Volume |
33 |
Issue |
4 |
Pages |
410-415 |
| Keywords |
Animals; Biomechanics; Forelimb/physiology; Gait/*physiology; Horses/*physiology; Joints/*physiology; Physical Conditioning, Animal; Tendons/*physiology; Weight-Bearing |
| Abstract |
Tendon injuries are an important problem in athletic horses and are probably caused by excessive loading of the tendons during demanding activities. As a first step towards understanding these injuries, the tendon loading was quantified during jump landings. Kinematics and ground reaction forces were collected from the leading and trailing forelimbs of 6 experienced jumping horses. Joint moments were calculated using inverse dynamic analysis. It was found that the variation of movement and loading patterns was small, both within and between horses. The peak flexor joint moments in the coffin and fetlock joints were larger in the trailing limb (-0.62 and -2.44 Nm/kg bwt, respectively) than in the leading limb (-0.44 and -1.93 Nm/kg bwt, respectively) and exceeded literature values for trot by 82 and 45%. Additionally, there was an extensor coffin joint moment in the first half of the stance phase of the leading limb (peak value 0.26+/-0.18 Nm/kg bwt). From these results, it was concluded that the loading of the flexor tendons during landing was higher in the trailing than in the leading limb and that there was an unexpected loading of the extensor tendon in the leading limb. |
| Address |
Department of Veterinary Anatomy and Physiology, Faculty of Veterinary Medicine, Utrecht University, The Netherlands |
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Thesis |
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Place of Publication |
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Editor |
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| Language |
English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0425-1644 |
ISBN |
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Conference |
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| Notes |
PMID:11469776 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3787 |
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| Author |
Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
| Title |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
Type |
Journal Article |
| Year |
2001 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
| Volume |
123 |
Issue |
27 |
Pages |
6649-6653 |
| Keywords |
Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
| Abstract |
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. |
| Address |
Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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Place of Publication |
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English |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0002-7863 |
ISBN |
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Medium |
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Conference |
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| Notes |
PMID:11439052 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3788 |
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| Author |
Gulotta, M.; Gilmanshin, R.; Buscher, T.C.; Callender, R.H.; Dyer, R.B. |
| Title |
Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape |
Type |
Journal Article |
| Year |
2001 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
| Volume |
40 |
Issue |
17 |
Pages |
5137-5143 |
| Keywords |
Animals; Apoproteins/*chemistry; Computer Simulation; Horses; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; *Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence/instrumentation/methods; Thermodynamics; Tryptophan/chemistry |
| Abstract |
An acid-destabilized form of apomyoglobin, the so-called E state, consists of a set of heterogeneous structures that are all characterized by a stable hydrophobic core composed of 30-40 residues at the intersection of the A, G, and H helices of the protein, with little other secondary structure and no other tertiary structure. Relaxation kinetics studies were carried out to characterize the dynamics of core melting and formation in this protein. The unfolding and/or refolding response is induced by a laser-induced temperature jump between the folded and unfolded forms of E, and structural changes are monitored using the infrared amide I' absorbance at 1648-1651 cm(-1) that reports on the formation of solvent-protected, native-like helix in the core and by fluorescence emission changes from apomyoglobin's Trp14, a measure of burial of the indole group of this residue. The fluorescence kinetics data are monoexponential with a relaxation time of 14 micros. However, infrared kinetics data are best fit to a biexponential function with relaxation times of 14 and 59 micros. These relaxation times are very fast, close to the limits placed on folding reactions by diffusion. The 14 micros relaxation time is weakly temperature dependent and thus represents a pathway that is energetically downhill. The appearance of this relaxation time in both the fluorescence and infrared measurements indicates that this folding event proceeds by a concomitant formation of compact secondary and tertiary structures. The 59 micros relaxation time is much more strongly temperature dependent and has no fluorescence counterpart, indicating an activated process with a large energy barrier wherein nonspecific hydrophobic interactions between helix A and the G and H helices cause some helix burial but Trp14 remains solvent exposed. These results are best fit by a multiple-pathway kinetic model when U collapses to form the various folded core structures of E. Thus, the results suggest very robust dynamics for core formation involving multiple folding pathways and provide significant insight into the primary processes of protein folding. |
| Address |
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA |
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English |
Summary Language |
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0006-2960 |
ISBN |
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| Notes |
PMID:11318635 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3789 |
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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 |
Summary Language |
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Original Title |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0006-3495 |
ISBN |
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Conference |
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| Notes |
PMID:10620304 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3792 |
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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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Place of Publication |
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English |
Summary Language |
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Original Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0885-114X |
ISBN |
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| Notes |
PMID:10329901 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3793 |
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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 |
Summary Language |
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Series Title |
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Abbreviated Series Title |
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Series Issue |
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Edition |
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| ISSN |
0425-1644 |
ISBN |
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Conference |
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| Notes |
PMID:9844973 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3794 |
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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 |
Summary Language |
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Series Title |
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Edition |
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| ISSN |
1072-8368 |
ISBN |
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| Notes |
PMID:9586997 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3795 |
| Permanent link to this record |
