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Author |
Alexander, F.; Benzie, D. |
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Title |
A radiological study of the digestive tract of the foal |
Type |
Journal Article |
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Year |
1951 |
Publication |
Quarterly journal of experimental physiology and cognate medical sciences |
Abbreviated Journal  |
Q J Exp Physiol Cogn Med Sci |
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Volume |
36 |
Issue |
4 |
Pages |
213-217 |
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Keywords |
Gastrointestinal Tract/*radiography; *Horses; *GASTROINTESTINAL SYSTEM/radiography; *Horses; *MYOCARDITIS/etiology and pathogenesis |
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0033-5541 |
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PMID:14892238 |
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no |
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Call Number |
refbase @ user @ |
Serial |
129 |
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Author |
Lynch, J.J.; Fregin, G.F.; Mackie, J.B.; Monroe, R.R.J. |
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Title |
Heart rate changes in the horse to human contact |
Type |
Journal Article |
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Year |
1974 |
Publication |
Psychophysiology |
Abbreviated Journal |
Psychophysiology |
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Volume |
11 |
Issue |
4 |
Pages |
472-478 |
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Keywords |
Animals; Behavior, Animal; Electrocardiography/veterinary; *Heart Rate; Horses/*physiology; Humans; *Social Behavior; *Touch |
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0048-5772 |
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PMID:4852234 |
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no |
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refbase @ user @ |
Serial |
1965 |
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Author |
Miyashita, Y.; Nakajima, S.; Imada, H. |
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Title |
Panel-touch behavior of horses established by an autoshaping procedure |
Type |
Journal Article |
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Year |
1999 |
Publication |
Psychological Reports |
Abbreviated Journal |
Psychol Rep |
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Volume |
85 |
Issue |
3 Pt 1 |
Pages |
867-868 |
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Keywords |
Animals; Behavior, Animal/*physiology; Conditioning (Psychology)/*physiology; Horses/physiology; *Touch |
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Abstract |
Panel-touch behavior of 3 geldings was successfully established by a response-termination type of autoshaping procedure. An omission or negative contingency introduced after the training of an animal, however, decreased the response rate to a near-zero level. |
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Department of Psychology, Kwansei Gakuin University, Nishinomiya, Japan |
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0033-2941 |
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PMID:10672748 |
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no |
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Call Number |
refbase @ user @ |
Serial |
1926 |
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Author |
Permyakov, S.E.; Khokhlova, T.I.; Nazipova, A.A.; Zhadan, A.P.; Morozova-Roche, L.A.; Permyakov, E.A. |
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Title |
Calcium-binding and temperature induced transitions in equine lysozyme: new insights from the pCa-temperature “phase diagrams” |
Type |
Journal Article |
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Year |
2006 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
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Volume |
65 |
Issue |
4 |
Pages |
984-998 |
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Keywords |
Animals; Apoproteins/chemistry/metabolism; Binding Sites; Calcium/chemistry/*metabolism; Cattle; Edetic Acid/metabolism; Horses/metabolism; Hydrogen-Ion Concentration; Lactalbumin/chemistry/metabolism; Muramidase/*chemistry/*metabolism; Protein Denaturation; Spectrometry, Fluorescence; *Temperature; Thermodynamics; Tryptophan/chemistry/metabolism |
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Abstract |
The most universal approach to the studies of metal binding properties of single-site metal binding proteins, i.e., construction of a “phase diagram” in coordinates of free metal ion concentration-temperature, has been applied to equine lysozyme (EQL). EQL has one relatively strong calcium binding site and shows two thermal transitions, but only one of them is Ca(2+)-dependent. It has been found that the Ca(2+)-dependent behavior of the low temperature thermal transition (I) of EQL can be adequately described based upon the simplest four-states scheme of metal- and temperature-induced structural changes in a protein. All thermodynamic parameters of this scheme were determined experimentally and used for construction of the EQL phase diagram in the pCa-temperature space. Comparison of the phase diagram with that for alpha-lactalbumin (alpha-LA), a close homologue of lysozyme, allows visualization of the differences in thermodynamic behavior of the two proteins. The thermal stability of apo-EQL (transition I) closely resembles that for apo-alpha-LA (mid-temperature 25 degrees C), while the thermal stabilities of their Ca(2+)-bound forms are almost indistinguishable. The native state of EQL has three orders of magnitude lower affinity for Ca(2+) in comparison with alpha-LA while its thermally unfolded state (after the I transition) has about one order lower (K = 15M(-1)) affinity for calcium. Circular dichroism studies of the apo-lysozyme state after the first thermal transition show that it shares common features with the molten globule state of alpha-LA. |
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Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow region 142290, Russia |
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ISSN |
1097-0134 |
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Notes |
PMID:17022083 |
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no |
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Call Number |
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Serial |
1858 |
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Author |
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. |
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Title |
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods |
Type |
Journal Article |
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Year |
1994 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
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Volume |
19 |
Issue |
2 |
Pages |
110-119 |
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Keywords |
Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea |
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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. |
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Address |
Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan |
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English |
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ISSN |
0887-3585 |
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Notes |
PMID:8090705 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3799 |
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Author |
Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. |
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Title |
Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c |
Type |
Journal Article |
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Year |
2004 |
Publication |
The Protein Journal |
Abbreviated Journal |
Protein J |
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Volume |
23 |
Issue |
8 |
Pages |
519-527 |
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Keywords |
Animals; Cytochromes c/*chemistry; Enzyme Activation; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry |
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Abstract |
We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal. |
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Address |
Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 7/A 43100 Parma, Italy |
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English |
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Edition |
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ISSN |
1572-3887 |
ISBN |
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Notes |
PMID:15648974 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3770 |
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Author |
Hartmann, E.; Christensen, J.W.; McGreevy, P.D. |
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Title |
Dominance and Leadership: Useful Concepts in Human-Horse Interactions? |
Type |
Journal Article |
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Year |
2017 |
Publication |
Journal of Equine Veterinary Science |
Abbreviated Journal |
Proceedings of the 2017 Equine Science Symposium |
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Volume |
52 |
Issue |
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Pages |
1-9 |
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Keywords |
Horse; Social order; Dominance hierarchy; Aggression; Injury; Learning; Training |
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Abstract |
Dominance hierarchies in horses primarily influence priority access to limited resources of any kind, resulting in predictable contest outcomes that potentially minimize aggressive encounters and associated risk of injury. Levels of aggression in group-kept horses under domestic conditions have been reported to be higher than in their feral counterparts but can often be attributed to suboptimal management. Horse owners often express concerns about the risk of injuries occurring in group-kept horses, but these concerns have not been substantiated by empirical investigations. What has not yet been sufficiently addressed are human safety aspects related to approaching and handling group-kept horses. Given horse's natural tendency to synchronize activity to promote group cohesion, questions remain about how group dynamics influence human-horse interactions. Group dynamics influence a variety of management scenarios, ranging from taking a horse out of its social group to the prospect of humans mimicking the horse's social system by taking a putative leadership role and seeking after an alpha position in the dominance hierarchy to achieve compliance. Yet, there is considerable debate about whether the roles horses attain in their social group are of any relevance in their reactions to humans. This article reviews the empirical data on social dynamics in horses, focusing on dominance and leadership theories and the merits of incorporating those concepts into the human-horse context. This will provide a constructive framework for informed debate and valuable guidance for owners managing group-kept horses and for optimizing human-horse interactions. |
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ISSN |
0737-0806 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
6712 |
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Author |
Jansen, T.; Forster, P.; Levine, M.A.; Oelke, H.; Hurles, M.; Renfrew, C.; Weber, J.; Olek, K. |
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Title |
Mitochondrial DNA and the origins of the domestic horse |
Type |
Journal Article |
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Year |
2002 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
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Volume |
99 |
Issue |
16 |
Pages |
10905-10910 |
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Keywords |
Animals; Animals, Domestic/classification/*genetics; Base Sequence; DNA, Complementary; *DNA, Mitochondrial; *Evolution, Molecular; Horses/classification/*genetics; Molecular Sequence Data; Phylogeny |
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Abstract |
The place and date of the domestication of the horse has long been a matter for debate among archaeologists. To determine whether horses were domesticated from one or several ancestral horse populations, we sequenced the mitochondrial D-loop for 318 horses from 25 oriental and European breeds, including American mustangs. Adding these sequences to previously published data, the total comes to 652, the largest currently available database. From these sequences, a phylogenetic network was constructed that showed that most of the 93 different mitochondrial (mt)DNA types grouped into 17 distinct phylogenetic clusters. Several of the clusters correspond to breeds and/or geographic areas, notably cluster A2, which is specific to Przewalski's horses, cluster C1, which is distinctive for northern European ponies, and cluster D1, which is well represented in Iberian and northwest African breeds. A consideration of the horse mtDNA mutation rate together with the archaeological timeframe for domestication requires at least 77 successfully breeding mares recruited from the wild. The extensive genetic diversity of these 77 ancestral mares leads us to conclude that several distinct horse populations were involved in the domestication of the horse. |
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Address |
Biopsytec Analytik GmbH, Marie-Curie-Strasse 1, 53359 Rheinbach, Germany. jansen@biopsytec.com |
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English |
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Series Issue |
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Edition |
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ISSN |
0027-8424 |
ISBN |
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Notes |
PMID:12130666 |
Approved |
no |
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Call Number |
refbase @ user @ |
Serial |
772 |
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Author |
Uzawa, T.; Akiyama, S.; Kimura, T.; Takahashi, S.; Ishimori, K.; Morishima, I.; Fujisawa, T. |
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Title |
Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness |
Type |
Journal Article |
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Year |
2004 |
Publication |
Proceedings of the National Academy of Sciences of the United States of America |
Abbreviated Journal |
Proc. Natl. Acad. Sci. U.S.A. |
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Volume |
101 |
Issue |
5 |
Pages |
1171-1176 |
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Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Cytochromes c/chemistry; Horses; Myoglobin/*chemistry; *Protein Folding; *Protein Structure, Secondary; Scattering, Radiation |
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Abstract |
The characterization of protein folding dynamics in terms of secondary and tertiary structures is important in elucidating the features of intraprotein interactions that lead to specific folded structures. Apomyoglobin (apoMb), possessing seven helices termed A-E, G, and H in the native state, has a folding intermediate composed of the A, G, and H helices, whose formation in the submillisecond time domain has not been clearly characterized. In this study, we used a rapid-mixing device combined with circular dichroism and small-angle x-ray scattering to observe the submillisecond folding dynamics of apoMb in terms of helical content (f(H)) and radius of gyration (R(g)), respectively. The folding of apoMb from the acid-unfolded state at pH 2.2 was initiated by a pH jump to 6.0. A significant collapse, corresponding to approximately 50% of the overall change in R(g) from the unfolded to native conformation, was observed within 300 micros after the pH jump. The collapsed intermediate has a f(H) of 33% and a globular shape that involves >80% of all its atoms. Subsequently, a stepwise helix formation was detected, which was interpreted to be associated with a conformational search for the correct tertiary contacts. The characterized folding dynamics of apoMb indicates the importance of the initial collapse event, which is suggested to facilitate the subsequent conformational search and the helix formation leading to the native structure. |
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Address |
Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Nishikyo, Kyoto 615-8510, Japan |
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English |
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0027-8424 |
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Notes |
PMID:14711991 |
Approved |
no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3779 |
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Author |
Ballew, R.M.; Sabelko, J.; Gruebele, M. |
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Title |
Direct observation of fast protein folding: the initial collapse of apomyoglobin |
Type |
Journal Article |
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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. |
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Volume |
93 |
Issue |
12 |
Pages |
5759-5764 |
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Keywords |
Animals; Apoproteins/*chemistry; Circular Dichroism; Horses; Kinetics; Muscle, Skeletal/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Temperature |
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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. |
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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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0027-8424 |
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Notes |
PMID:8650166 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3798 |
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