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Your search keyword '"Murray, E.D."' showing total 46 results
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46 results on '"Murray, E.D."'

1. Ultrafast bond softening in bismuth: mapping a solid's interatomic potential with x-rays

Author

Fritz, D.M., Reis, D.A., Adams, B., Akre, R.A., Arthur, J., Blome, C., Bucksbaum, P.H., Cavalieri, A.L., Engemann, S., Fahy, S., Falcone, R.W., Fuoss, P.H., Gaffney, K.J., George, M.J., Hajdu, J., Hertlein, M.P., Hillyard, P.B., Hoegen, M. Horn-von, Kammler, M., Kaspar, J., Kienberger, R., Krejcik, P., Lee, S.H., Lindenberg, A.M., McFarland, B., Meyer, D., Montagne, T., Murray, E.D., Nelson, A.J., Nicoul, M., Pahl, R., Rudati, J., Schlarb, H., Siddons, D.P., Sokolowski-Tinten, K., Tschentscher, Th., von der Linde, D., and Hastings, J.B.

Subjects
Bismuth -- Research, Bismuth -- Structure, Bismuth -- Analysis
Published
2007

3. Heating rate affects thermal properties and network formation for vicilin and ovalumin at various pH values

Author

Arntfield, S.D. and Murray, E.D.

Subjects
Heating research -- Evaluation, Conformational analysis -- Research, Proteins -- Research, Business, Food/cooking/nutrition
Abstract

The effect of heating rate on the properties and protein network formation with ovalbumin and vicilin was evaluated at 3 different pH levels (5, 7, and 9) and the corresponding changes, noted with differential scanning calorimetry and dynamic rheology. Slower heating rates rates were found to result in stronger protein networks and with structural changes most apparent at pH 5. However, heating rate did not affect network characteristics and had remained independent from the thermal stimulus.

Published
1992

11. Role of the Thermal Denaturation-Aggregation Relationship in Determining the Rheological Properties of Heat Induced Networks for Ovalbumin and Vicilin.

Author

ARNTFIELD, S.D., MURRAY, E.D., ISMOND, M.A.H., and BERNATSKY, A.M.

Subjects
*RHEOLOGY, *OVALBUMINS, *VICILIN, *DENATURATION of proteins, *DIFFERENTIAL scanning calorimetry
Abstract

Heat-induced denaturation (determined by differential scanning calorimetry plus ANS fluorescence) and structure development (assessed by dynamic testing) were monitored for ovalbumin and vicilin to evaluate the importance of these processes on the rheological characteristics of resulting protein networks. Protein denaturation preceded structure development, based on an increase in the storage modulus (G'). Reduction of the temperature between denaturation and aggregation through pH manipulation or inclusion of stabilizing salts lowered G' values in the resulting network. In contrast, in the presence of SDS, G' values increased with (ovalbumin) or were unrelated to (vicilin) reduced temperature differences. This demonstrated the importance of a balance of attractive and repulsive forces when examining network characteristics. [ABSTRACT FROM AUTHOR]

Published
1989
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14. Role of Noncovalent Forces in Micellization Using Legumin from Vicia faba as a Study System.

Author

ISMOND, M.A.H., GEORGIOU, C., ARNTFIELD, S.D., and MURRAY, E.D.

Subjects
LEGUMIN, PROTEINS, MICELLES, THERMAL properties, ANIONS, URINE
Abstract

BSTRACT The seed storage protein, legumin, from Vicia faba interacted to form micelles and elaborate protein networks under varying conditions. Several molecular parameters correlated with observed micelle interaction parameters; these included thermal properties as indicators of protein stability and surface hydrophobicity as an assessment for potential hydrophobic interactions. The optimal pH for micelle formation ranged from 5.5 to 6.5, values at which electrostatic repulsions were minimal and surface hydrophobicites were adequate to allow hydrophobic interactions. The micelle response was affected by anions both in terms of concentration and type of anion. Finally, gradual denaturation of legumin with increasing urea concentrations had a negative impact on the micelle response. [ABSTRACT FROM AUTHOR]

Published
1990
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16. Protein carboxyl methyltransferase facilitates conversion of atypical L-isoaspartyl peptides to normal L-aspartyl peptides.

Author

Johnson, B.A., Murray, E.D., Clarke, S., Glass, D.B., and Aswad, D.W.

Abstract

Prolonged incubation of L-isoaspartate-containing forms of lactate dehydrogenase (231-242), sperm activating peptide, and adrenocorticotropin (22-27) at 37 degrees C, pH 7.4, with S-adenosyl-L-methionine and protein carboxyl methyltransferase from bovine brain leads to extensive conversion of the atypical isopeptide bond to a normal peptide bond. For the lactate dehydrogenase-related peptide, conversion was 80% complete after 24 h. For the other two peptides, conversion reached a level of approximately 65% after 48 h. The mechanism of conversion involves (i) rapid enzymatic methylation of the alpha-carboxyl of the L-iso-Asp residue; (ii) nonenzymatic demethylation resulting in formation of an L-aspartyl cyclic imide; and (iii) a slow, nonenzymatic hydrolysis of the cyclic imide to form a mixture of 15-25% normal L-Asp peptide and 75-85% L-iso-Asp peptide. The regenerated L-iso-Asp peptide is remethylated and the cycle is repeated. The extent of conversion is limited by a competing side reaction wherein the L-imide slowly racemizes, leading to the formation of mainly D-iso-Asp peptide, which is not a substrate for the methyltransferase. The ability of protein carboxyl methyltransferase to initiate conversion of L-iso-Asp residues to normal L-Asp suggests a possible role for this enzyme in facilitating the repair or degradation of deamidated proteins in vivo.

Published
1987
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