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| Author |
Cho, K.C.; Chan, K.K. |
| Title |
Kinetics of cold-induced denaturation of metmyoglobin |
Type |
Journal Article |
| Year |
1984 |
Publication |
Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology |
Abbreviated Journal |
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| Volume |
786 |
Issue |
1-2 |
Pages |
103-108 |
| Keywords |
Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart) |
| Abstract |
Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order. |
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refbase @ user @ |
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3978 |
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| Author |
Koenen, E.P.C.; van Veldhuizen, A.E.; Brascamp, E.W. |
| Title |
Genetic parameters of linear scored conformation traits and their relation to dressage and show-jumping performance in the Dutch Warmblood Riding Horse population |
Type |
Journal Article |
| Year |
1995 |
Publication |
Livestock Production Science |
Abbreviated Journal |
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| Volume |
43 |
Issue |
1 |
Pages |
85-94 |
| Keywords |
Horse; Heritability; Conformation; Dressage; Show jumping |
| Abstract |
In this study genetic parameters of linear scored conformation traits of the Dutch Warmblood Riding Horse were estimated in relation to performance in competition. Observations on 10 665 mares were analyzed with an animal model including the fixed effects age, classifier, location and percentage of thoroughbred. Using restricted maximum likelihood algorithms, heritabilities of 26 linear scored conformation traits were estimated in the range 0.09-0.28. Several conformation traits had high up to very high mutual genetic correlations. Competition results of 3476 horses with performance in dressage and 3220 horses with performance in show-jumping were linked to the conformation data to estimate the genetic relationship between conformation and performance in competition. The model for the evaluation of the competition results included the fixed effects riding club, age and sex. Estimated heritabilities for dressage and show-jumping were 0.17 +/- 0.05 and 0.19 +/- 0.04, respectively. Genetic correlations between conformation and performance were low to moderate. The length of the neck, length and position of the shoulders, shape and length of croup and muscularity of the haunches had a significant moderate genetic correlation with dressage. Muscularity of the neck, shape of the croup and muscularity of the haunches had a significant genetic correlation with show-jumping. The results indicate that, due to the low genetic correlations with performance traits, indirect selection for performance using conformation results is of limited value. |
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refbase @ user @ |
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3961 |
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| Author |
Koenen, E.P.C.; Aldridge, L.I.; Philipsson, J. |
| Title |
An overview of breeding objectives for warmblood sport horses |
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Journal Article |
| Year |
2004 |
Publication |
Livestock Production Science |
Abbreviated Journal |
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88 |
Issue |
1-2 |
Pages |
77-84 |
| Keywords |
Breeding objective; Sport horse; Sport performance; Conformation; Specialisation |
| Abstract |
The aim of this paper is to review the current breeding objectives of organisations that run a selection programme for warmblood riding horses in the light of an increasing trend in trade of semen across countries. In a questionnaire, 19 horse breeding organisations provided information on breeding objective traits. Variation both in length and amount of details used to define individual breeding objectives was large, reflecting that many traits in sport horse breeding are not easy to measure, and therefore, have to be defined in a subjective way. The majority of the breeding objectives included conformation, gaits and performance in show jumping and dressage. Some breeding objectives also included behaviour, soundness, health and fertility. However, several organisations did not specify the sport discipline and the level of competition (amateur, national or international level) in the breeding objective. In general, relative weightings of the traits within the verbally presented breeding objectives were not given, but were assessed by the organisations in response to this study. The relevance of more information on expected future production circumstances and on the genetic parameters of the traits of interest are discussed. A further review of the consistency, completeness and the number of traits of the present breeding objectives for sport horses is recommended to optimise the efficiency of selection decisions. |
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3954 |
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| Author |
Tsong, T.Y. |
| Title |
Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
Type |
Journal Article |
| Year |
1977 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
| Volume |
252 |
Issue |
24 |
Pages |
8778-8780 |
| Keywords |
*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
| Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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PMID:200618 |
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no |
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refbase @ user @ |
Serial |
3882 |
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| Author |
Pierce, M.M.; Nall, B.T. |
| Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
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Journal Article |
| Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
| Volume |
298 |
Issue |
5 |
Pages |
955-969 |
| Keywords |
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 |
| Abstract |
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. |
| Address |
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. |
| 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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0022-2836 |
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PMID:10966803 |
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no |
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Equine Behaviour @ team @ |
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3790 |
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Bayley, P.; Martin, S.; Anson, M. |
| Title |
Temperature-jump circular dichroism: observation of chiroptical relaxation processes at millisecond time resolution |
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Journal Article |
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1975 |
Publication |
Biochemical and Biophysical Research Communications |
Abbreviated Journal |
Biochem Biophys Res Commun |
| Volume |
66 |
Issue |
1 |
Pages |
303-308 |
| Keywords |
*Alcohol Oxidoreductases/metabolism; Animals; Circular Dichroism; Horses; Kinetics; Liver/enzymology; Mathematics; Protein Conformation; Temperature; Time Factors |
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0006-291X |
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PMID:1172440 |
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no |
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Equine Behaviour @ team @ |
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3816 |
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Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. |
| Title |
Nature of the fast and slow refolding reactions of iron(III) cytochrome c |
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Journal Article |
| Year |
1981 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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20 |
Issue |
6 |
Pages |
1622-1630 |
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Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis |
| Abstract |
The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding. |
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0006-2960 |
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PMID:6261802 |
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no |
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Equine Behaviour @ team @ |
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3809 |
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Dyson, H.J.; Beattie, J.K. |
| Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
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Journal Article |
| Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
| Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
| Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
| Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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0021-9258 |
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PMID:6277891 |
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no |
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Equine Behaviour @ team @ |
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3807 |
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Steinhoff, H.J.; Lieutenant, K.; Redhardt, A. |
| Title |
Conformational transition of aquomethemoglobin: intramolecular histidine E7 binding reaction to the heme iron in the temperature range between 220 K and 295 K as seen by EPR and temperature-jump measurements |
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Journal Article |
| Year |
1989 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
| Volume |
996 |
Issue |
1-2 |
Pages |
49-56 |
| Keywords |
Animals; Electron Spin Resonance Spectroscopy; Heme; Histidine; Horses; Humans; Hydrogen-Ion Concentration; Methemoglobin/*ultrastructure; Motion; Protein Conformation; Temperature; Thermodynamics; Water |
| Abstract |
Temperature-dependent EPR and temperature-jump measurements have been carried out, in order to examine the high-spin to low-spin transition of aquomethemogobin (pH 6.0). Relaxation rates and equilibrium constants could be determined as a function of temperature. As a reaction mechanism for the high-spin to low-spin transition, the binding of N epsilon of His E7 to the heme iron had been proposed; the same mechanism had been suggested for the ms-effect, found in temperature-jump experiments on aquomethemoglobin. A comparison of the thermodynamic quantities, deduced form the measurements in this paper, gives evidence that indeed the same reaction is investigated in both cases. Our results and most of the findings of earlier studies on the spin-state transitions of aquomethemoglobin, using susceptibility, optical, or EPR measurements, can be explained by the transition of methemoglobin with H2O as ligand (with high-spin state at all temperatures) and methemoglobin with ligand N epsilon of His E7 (with a low-spin ground state). Thermal fluctuations of large amplitude have to be postulated for the reaction to take place, so this reaction may be understood as a probe for the study of protein dynamics. |
| Address |
Institut fur Biophysik, Ruhr-Universitat Bochum, F.R.G |
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Edition |
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0006-3002 |
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| Notes |
PMID:2544230 |
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no |
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Equine Behaviour @ team @ |
Serial |
3803 |
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