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E D Atkins

Publications and source records attributed to E D Atkins.

36 records · Page 2Linked to original sources
PubMed1974

X-ray fibre diffraction of cartilage proteoglycan aggregates containing hyaluronic acid.

Ordered conformations of proteoglycan-hyaluronic acid aggregates in the intercellular matrix in cartilage were observed by X-ray diffraction. The sodium salt form of three samples, (a) aggregated proteoglycan, (b) disaggregated proteoglycan and (c) reconstituted disaggregated proteoglycan, give essentially similar X-ray fibre-type diffraction photographs. The patterns correlate with the chondroitin 4-sulphate component and can be interpreted as twofold helical conformations, similar to that observed previously for the free acid form of chondroitin 4-sulphate (Isaac & Atkins, 1973). The information takes us one step nearer the situation found in cartilage in vivo.

Animals↗
PubMed1974

Crystallization of macromolecular heparin.

X-ray fibre-diffraction photographs were obtained from oriented films of the sodium salt of macromolecular heparin (molecular weight approx. 10(6)) prepared from rat skin. Two distinct molecular chain conformations corresponding to two different crystal lattices were observed as a function of relative humidity. The first conformation, obtained at 78% relative humidity, has a layer-line spacing of 1.73nm, which can be interpreted as an approximate twofold helix. On increasing the relative humidity to 84% a second phase with a layer-line repeat of 1.65nm is obtained with the reflexions indexing on a triclinic unit cell similar to that obtained previously (Nieduszynski & Atkins, 1973) for pig mucosal heparin.

Animals↗
PubMed1973

Hyaluronates: relation between molecular conformations.

The discovery that both potassium and sodium salts of hyaluronic acid can exist in a double-strand helical conformation that will convert to the already known single-strand helical structures illustrates the remarkable conformational versatility of this biopolymer. X-ray diffraction was used to monitor variations in molecular conformation as a function of several independent, controllable variables, such as relative humidity, temperature, and applied tension. A scheme is presented for the interrelation of a range of hyaluronate conformations.

Humidity↗
PubMed1973

X-ray-diffraction patterns from chondroitin 4-sulphate, dermatan sulphate and heparan sulphate.

Ordered conformations from the sodium salts of chondroitin 4-sulphate, dermatan sulphate and heparan sulphate were observed by X-ray diffraction. Chondroitin 4-sulphate shows similar threefold helical character to that previously reported for chondroitin 6-sulphate and hyaluronates. Dermatan sulphate forms an eightfold helix with an axial rise per disaccharide of 0.93nm, which favours the l-iduronic acid moiety in the normal C1 chair form. The layer-line spacing and axial projection in heparan sulphate of 1.86nm favours a tetrasaccharide repeat with glycosidic linkages alternating beta-d-(1-->4) and alpha-d-(1-->4).

Animals↗
PubMed1973

Conformation of the mucopolysaccharides. X-ray fibre diffraction of heparin.

Oriented films of the sodium salt of heparin crystallize in a triclinic unit cell. The X-ray diffraction results favour a tetrasaccharide covalent repeating sequence but the measured molecular repeat of 1.59nm is inconsistent with all alpha-(1-->4)(1ax-->4eq)-glycosidic linkages as generally accepted. Three models are proposed for the molecular shape of heparin, which depend on the chair conformation adopted by the hexuronic acid moieties. Model I has both uronic acids in the C1 chair form, model II has one uronic acid in each of the C1 and 1C chairs and model III has both in the 1C chair form. The merits of these models are discussed.

Animals↗
PubMed1972

The conformation of the mucopolysaccharides. Hyaluronates.

X-ray-diffraction patterns of hyaluronate fibres from a variety of sources were obtained. Sodium hyaluronate gives well-defined patterns which index on a hexagonal unit cell with dimensions a=1.17+/-nm and a fibre repeat-distance of 2.85+/-0.03nm. A further form of sodium hyaluronate is produced by annealing at 60 degrees C in 75% relative humidity. This stable state indexes on a hexagonal unit cell of unchanged fibre repeat-distance but with a=1.87nm. The chain conformation is a threefold helix. Analysis of these diffraction patterns led to two tentative structures for sodium hyaluronate, involving different packing of the polysaccharide chains. The significance of side-chain interaction is discussed. Hyaluronic acid produces an X-ray pattern different from that obtained with the sodium salt. The fibre repeat-distance is 1.96+/-0.02nm and the unit cell appears to be monoclinic. The chain conformation is a twofold helix and conformational change between free acid and monovalent salt is discussed. These findings, together with model-building experiments, are interpreted as indicating a highly ordered structure, and the physical properties of hyaluronate solutions with regard to molecular shape and polyelectrolyte behaviour are rationalized.

Hyaluronic Acid↗