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Biomedical subjects

W Traub

Publications and source records attributed to W Traub.

At least 19 recordsLinked to original sources
PubMed1994

Ultrastructural studies of bones from patients with osteogenesis imperfecta.

Bone samples from patients suffering from osteogenesis imperfecta (OI) types I, II, III and IV, as well as normal controls, were studied by scanning (SEM) and transmission electron microscopy (TEM). SEM views of normal bone at low magnification show coherent structure, with regular striations due to a lamellar plywood-like arrangement of the mineralized collagen fibrils. Compact lamellar bone was also found in various OI specimens, but in limited disconnected regions separated by open spaces. Furthermore, some OI, but not normal, bones have regions of loose unconnected fibers and others of apparently abnormally dense mineral deposition. High resolution TEM studies of OI bone fragments have served to elucidate the structures of these different textures. There appears to be a substantial, though reduced, proportion of normal lamellar bone even in quite severe OI. However, the regions of loose fibers are largely unmineralized and probably contain abnormal collagen. Other regions are overmineralized, with generally small unorganized apatite crystals deposited onto fibril surfaces or in separate clusters. These structural abnormalities, together with the paucity of normal bone, may explain the fragility of OI bones.

Adolescent↗
PubMed1992

Bone structure: from angstroms to microns.

Bone has a complex hierarchical structure, which despite much investigation, is still not well understood. Here we bring together pieces of this complicated puzzle, albeit from different sources, to present a tentative overview of bone structure. The basic building blocks are the extremely small plate-shaped crystals of carbonate apatite, just hundreds of angstroms long and wide and some 20-30 A thick. They are arranged in parallel layers within the collagenous framework. At the next hierarchical level these mineral-filled collagen fibrils are ordered into arrays in which the fibril axes and the crystal layers are all organized into a 3-dimensional structure that makes up a single layer or lamella of bone a few microns thick. The orientations of the collagen fibrils and the crystal layers in alternating lamellae of rat bone differ such that in the thinner lamellae, the fibrils and the crystal layers are parallel to the lamellar boundaries. In the thicker lamellae the fibrils are parallel to the boundary, but the crystal layers are rotated out of the plane of the boundary. In many bones these alternating lamellae are organized into even larger ordered structures to produce what is truly a remarkably ordered material, all the way from the molecular scale to the macroscopic product.

Animals↗
PubMed1992

Dentin phosphophoryn binding to collagen fibrils.

The interaction of rat incisor phosphophoryn with native turkey tendon collagen fibers has been examined by electron microscopy. The binding of phosphophoryn to the tendon fibril surfaces is quite selective. The phosphophoryn is seen as positively or negatively stained globular particles predominantly at the "e" band in the collagen gap region in transmission electron micrographs of the phosphophoryn-reacted fibrils. The selectivity of binding to the fibrils was obtained in the presence of calcium ions, which bind avidly to phosphophoryn. The specific association of phosphophoryn at the "e" band suggests a possible regulation of mineral deposition within the gap regions of the collagen fibrils.

Animals↗
PubMed1992

Origin of mineral crystal growth in collagen fibrils.

Collagen fibrils from young turkey-leg tendons, just beginning to mineralize, were stained with uranyl acetate and examined by electron microscopy. Small needle-like mineral crystals were observed and located, in relation to the collagen banding pattern, as originating at the e band in the gap region and near the surface of the fibrils. These are evidently the sites of crystal nucleation. They lie near binding locations on collagen fibrils of two glycosylated proteins believed to be implicated in the mineralization process, as well as the sites of early crystals in embryonic fowl bones.

Animals↗
PubMed1992

Growth of mineral crystals in turkey tendon collagen fibers.

Bone and several other vertebrate mineralized tissues are formed by the organized growth of crystals of carbonated apatite within a matrix of type 1 collagen fibers. The development of this process in isolated fibrils of young turkey leg tendons has been studied by transmission electron microscopy. Collagen banding, presumably due to ion concentration, precedes the appearance of any crystals. The smallest crystals observed are short needles in bands near the surface of the fibrils. Longer needles, up to the length of the collagen gap regions, were also seen, and, evidently at a later stage, single crystal belts extending partly or wholly through the fibrils. Finally, in mature tendon crystal platelets, seemingly derived from the cracking of belts, extend partly into the collagen overlap zone. In the least mineralized tendon, extrafibrillar mineral-containing vesicles have occasionally been observed adjacent to regions of radiating needle crystal growth in the fibrils, and, more commonly, smaller particles adjacent to bands of very small needles.

Aging↗
PubMed1991

Crystal organization in rat bone lamellae.

The plate-shaped crystals of rat bone are arranged in parallel layers that form coherent structures up to the level of individual lamellae. The crystal layers of the thin lamellae are parallel to the lamellar boundary, whereas those of the thicker lamellae are oblique to the boundary. The basic structure of rat bone can be described as 'rotated plywood'; a structure hitherto unrecognized in either biologic or synthetic materials.

Animals↗
PubMed1991

Electron imaging and diffraction study of individual crystals of bone, mineralized tendon and synthetic carbonate apatite.

A transmission electron microscope study of carbonate apatite crystals isolated from bone and mineralizing tendon, as well as those produced synthetically under approximated-physiological conditions, shows that they are thin irregular shaped plates. Electron diffraction patterns of individual crystals confirm that the large developed crystal face is (100), and that the longest dimensions of the biogenic crystals are aligned with the crystallographic c axes. As the latter are also aligned with collagen fibril axes, the observations provide additional information on the tissue organization itself. The marked similarity between the biologic and synthetic crystals suggests that the biological environment in which the crystals form may not be primarily responsible for controlling their shape.

Animals↗
PubMed1989

Three-dimensional ordered distribution of crystals in turkey tendon collagen fibers.

The organization of apatite crystals and collagen fibrils in mineralized turkey tendon has been studied by electron microscopy and electron diffraction. To minimize artifactual distortions the tissue was examined, for the first time, as isolated fibrils in an aqueous environment of vitreous ice, as well as in conventionally prepared sections. The electron micrographs show that the plate-shaped apatite crystals are arranged in parallel arrays across the collagen fibrils. This provides direct evidence for highly asymmetric assembly in collagen fibrils, and, indeed, the fibrils were observed to be elongated rather than round in cross-section. There is, furthermore, a pronounced tendency for the layers of crystals to be coherently aligned in adjacent fibrils. These observations may also be important for understanding the mechanical behavior of bone at the molecular level, as such extended, aligned aggregates of flat crystals could develop into natural fracture planes in mature bone.

Animals↗
PubMed1989

Crystal size and organization in bone.

Size measurements of dispersed rat bone crystals show that with age a greater proportion exceeds 400 A in length. The surface fractures of more heavily mineralized bones tend to be smooth and stepped, whereas those of less mineralized bones are fibrous. These observations combined with information reported elsewhere on the crystal-collagen relations in adjacent fibrils in turkey tendon, suggest that some crystals grow out of the confines of the collagen gap regions to form extended aggregates of large flat crystals with well developed fracture planes.

Animals↗
PubMed1986

Organization of hydroxyapatite crystals within collagen fibrils.

Transmission electron micrographs of individual mineralized collagen fibrils show that hydroxyapatite crystals are located mainly within the fibrils at the level of the gap regions. The plate-shaped crystals are observed to be more or less uniformly stacked across the fibril diameter. We therefore suggest that the crystals are primarily located in 'grooves' created by contiguous adjacent gaps. The proposal is consistent with the observed crystal distribution in the fibril and with their average widths, which are almost 10-times greater than an individual gap diameter.

Animals↗
PubMed1986

Structural study of a mutant type I collagen from a patient with lethal osteogenesis imperfecta containing an intramolecular disulfide bond in the triple-helical domain.

We have built molecular models of collagen type I from a patient with lethal osteogenesis imperfecta incorporating one or two mutant alpha 1(I)-chains which contain a cysteine substituting a glycine near the C-terminal end. In either case, the cysteines can only be accommodated with considerable distortion of the native collagen structure, which disrupts inter-chain contacts. The disturbance of the triple helix is limited to a small local region. This suggests that the most important consequence of the mutation is delayed helix formation leading to overmodification and decreased collagen production, rather than the structural abnormality of the folded molecules, which are only marginally unstable.

Collagen↗
PubMed1986

Protein conformation in rat tooth enamel.

Orientated 0.47 nm reflections in X-ray diffraction patterns of developing rat tooth enamel were confirmed using a wide range of specimen preparations and experimental conditions. This indicates that some of the organic matrix proteins adopt a beta-sheet conformation.

Animals↗
PubMed1984

Enamel rod relations in the developing rat incisor.

Scanning electron microscopic and X-ray diffraction studies have shown that mandibular rat incisor teeth have two sets of rods which decussate at angles between 60 and 80% in both the most immature zone and the zone just beyond the opaque margin. A less well oriented interrod enamel component was found at right angles to both sets of rods. The information provides additional views of this complex tissue. Furthermore, it has been shown that the Wistar rat incisal enamel ultrastructure facilitates the use of X-ray diffraction to determine molecular relations between the crystals and matrix constituents as the rods are not all at 90 degrees to one another.

Ameloblasts↗
PubMed1982

Adenine-guanine base pairing ribosomal RNA.

Analyses of secondary structures proposed for ribosomal RNA's show that, of the different kinds of base pairs directly adjoining the ends of postulated double-helical regions, only A-G with A at the 5' end significantly exceeds the number expected for a random base distribution. An A(syn)-G(trans) hydrogen-bonded basepair is proposed. This could fit at the end of an undistorted double helix, but would prevent further base stacking, thus favoring a break in the double helix to produce a non-linear tertiary structure.

Adenine↗
PubMed1979

The limiting collagen microfibril. The minimum structure demonstrating native axial periodicity.

Collagen fibers were grown from solutions of acid-soluble or neutral salt-soluble collagen in 0.5 M acetic acid by rapid dialysis. The collagen was obtained under conditions where protease inhibitors were present at every stage of extraction and purification. Under the conditions used, length-wise but not lateral filament growth proceeded rapidly and gel-like networks were formed, Water readily exuded from the networks. The networks were stretched to fibrous form during drying. Small-angle X-ray diffraction showed the stretched fibrils to be highly ordered, showing up to 20 orders of the 670 A meridional periodicity. Intermediate- and wide-angle photographs show equatorial reflections at a spacing corresponding to approximately 12.5 A which is related to the intermolecular distance but none related to a microfibrillar packing at the 35-40 A level. Electron microscopy of the gel networks before stretching shows the presence of thin filaments with diameters predominantly in the 35-40 A range. No cross-striated fibrils are seen in electron micrographs of either stretched fibers or unstretched fibers. Thus, intermolecular packing in accord with the 670 A axial periodicity can take place within approximately 40 A diameter thin filaments. These correspond to the structures previously postulated to be collagen 'microfibrils'.

Animals↗
PubMed1977

Structural analysis of denaturant-protein interactions: comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme.

This paper summarizes our crystallographic studies of the interaction of denaturants with cross-linked triclinic lysozyme. Electron density maps of various bromoethanol-lysozyme complexes are analyzed and compared to those reported earlier for SDS-lysozyme complexes. Despite differences in the chemical nature and size of the two denaturants their mode of interaction with the protein is quite similar, suggesting the existence of a general mechanism for binding of hydrophobic-hydrophilic denaturants to proteins. Our results are consistent with the conclusion that lysozyme consists of two domains connected by a flexible segment and that this segment represents an internal degree of freedom of the protein.

Ethanol↗