Topic:Conformation
Conformation refers to the physical structure and alignment of a horse's body, encompassing aspects such as bone structure, musculature, and limb alignment. It is an important area of study for understanding how these physical characteristics can influence a horse's performance, movement, and susceptibility to injury. Conformation assessment involves evaluating various body parts, including the head, neck, back, shoulders, legs, and hooves, to determine their proportionality and functionality. This topic includes research on the genetic and developmental factors influencing conformation, as well as its impact on different equestrian disciplines. This page gathers peer-reviewed research studies and scholarly articles that explore the assessment, implications, and breeding considerations related to equine conformation.
A case of spermatic arteriovenous anastomosis in the horse. A large anastomosis of the spermatic artery and vein is described. This was found while surgically removing an abdominal testis. Before surgery the animal wanted to rear after exercise and could not stand on 3 legs for any length of time while being shod. This unusual behaviour disappeared after removal of the mass. The performance and conformation of the horse has also greatly improved.
Circular dichroic properties and conformation of thionicotinamide dinucleotides bound to horse-liver alcohol dehydrogenase. The interaction between horse liver alcohol dehydrogenase and the oxidized and reduced forms of the 3-thionicotinamide--adenine dinucleotide coenzyme analogues (sNAD and sNADH) has been investigated by ultraviolet absorption, fluorescence and circular dichroism. The fluorescence of sNADH is enhanced when bound to the enzyme, and the protein fluorescence is quenched by both sNADH (60--65%) and sNAD (65%). The possible origin of the larger quenching produced by sNAD with respect to that of NAD is discussed. Coenzyme dissociation constants have been determined by monitoring the quenching of the p...
Circular dichroism of porcine, bovine, and equine pancreatic phospholipases A2 and their zymogens. Unusual conformations simulating helix content. Conformation of porcine, bovine, and equine pancreatic phospholipases A2 (EC 3.1.1.4) and their zymogens was studied by the circular dichroism (CD) probe in the far and near ultraviolet spectral zones.
All these phospholipases and their zymogens displayed CD curves suggesting the presence of moderate amounts of α-helical conformation. However, on the basis of known primary structure and recent X-ray structural analysis of prophospholipase A2 crystals (Drenth, J., Enzing, C.M., Kalk, K.H. and Vessies, J.C.A. (1976) Nature 264, 373–377), it has to be concluded that the positive CD band cen...
Conformational energy refinement of horse-heart ferricytochrome c. The reported X-ray structure of horse-heart ferricytochrome c has been refined by conformational energy calculations, using a three-stage computational procedure. In stage I, the atomic positions are adjusted to conform to idealized bond lengths and bond angles characteristic of small amino acid derivatives, while yet remaining as close as possible to the X-ray coordinates. In stage II, atomic overlaps are eliminated by adjusting the backbone and side-chain dihedral angles to minimize the nonbonded energy, hydrogen-bonded energy, and rotational energy contributions. In the final stage of refin...
The influence of amino acid substitutions on the conformational energy of cytochrome c. Conformational energies have been evaluated for each of the staggered side-chain conformations associated with the 261 amino acid substitutions known to occur among 60 eucaryotic species. At least 86% of these substitutions can be sterically accommodated (one at a time) within the structure of horse-heart cytochrome c resulting from conformational energy refinement. Simultaneous incorporation of all pertinent amino acid substitutions found in eight representative species into the refined horse-heart structure is also shown to be sterically possible, with few exceptions. In two cases (Pekin duc...
Differences in subunit composition and iron content of isoferritins. Horse spleen ferritin was fractionated into its constituent isoferritins by isoelectric focusing. Separated isoferritins were stable and showed no tendency to redistribute when re-examined by analytical gel focusing. All of the isoferritins were immunologically indistinguishable when tested with antibodies raised against unfractionated horse spleen ferritin. The separated isoferritins also had similar conformations as determined by circular dichroism. Iron distribution studies, however, revealed a wide disparity among the isoferritins. The most acidic components had the lowest iron content but...
Mercuri-nitrophenol as a reporter group for the conformational change of hemoglobin. One mole of horse hemoglobin tetramer reacts with 2 moles of 2-chloromercuri-4-nitrophenol (MNP) at beta 93 cysteine. The difference spectra between NMP-bound hemoglobin and hemoglobin, measured with the aid of ascorbic acid and ascorate oxidase [EC 1.10.3.3] as deoxygenation reagents, indicate that the pK of the phenolic hydroxyl group of MNP increases by 0.6 to 0.8 pH unit on deoxygenation of the hemoglobin. The Hill constant of the modified hemoglobin changes with pH. It decreases from about 2.4 at pH 6.8 to about 1.0 at pH 9.0 This effect of the reagent is interpreted as inherent to the re...
Conformational studies of equilibrium structures in fragments of horse heart cytochrome c. Ultraviolet absorption and circular dichroism studies have been carried out on horse heart apo-cytochrome c and heme-free peptide fragments obtained by cyanogen bromide cleavage of the native protein. It was noted that the various peptides assume predominantly an unordered conformation in water solution. Increasing ionic strength and addition of 2-chloroethanol increase the right-handed helical content. Guanidinium hydrochloride favors the coil state. It was also demonstrated that two non-interacting helical regions of different stability are present in the apo-protein in 2-chloroethanol.
Measurement of ligand-induced conformational changes in hemoglobin by circular dichroism. The UV circular-dichroism spectra of human and horse hemoglobins have been determined at various degrees of partial saturation with oxygen. Spectra of the two native hemoglobins were compared with spectra of the corresponding proteins modified with a reagent known to eliminate the conformational rearrangement normally associated with cooperativity. Such comparison indicates that one region, around 260 mmu, is sensitive chiefly to the state of the hemes; changes in another region, around 285 mmu, may be correlated with the conformational transformation linked to cooperative interactions. All ci...